ID   V5VCW7_ACIBA            Unreviewed;       275 AA.
AC   V5VCW7;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   10-APR-2019, entry version 57.
DE   RecName: Full=Methionine aminopeptidase {ECO:0000256|HAMAP-Rule:MF_01974, ECO:0000256|RuleBase:RU003653};
DE            Short=MAP {ECO:0000256|HAMAP-Rule:MF_01974};
DE            Short=MetAP {ECO:0000256|HAMAP-Rule:MF_01974};
DE            EC=3.4.11.18 {ECO:0000256|HAMAP-Rule:MF_01974, ECO:0000256|RuleBase:RU003653};
DE   AltName: Full=Peptidase M {ECO:0000256|HAMAP-Rule:MF_01974};
GN   Name=map {ECO:0000256|HAMAP-Rule:MF_01974,
GN   ECO:0000313|EMBL:PZM18289.1};
GN   Synonyms=map1 {ECO:0000313|EMBL:AKA30982.1}, map_1
GN   {ECO:0000313|EMBL:KZA22651.1}, map_2 {ECO:0000313|EMBL:ASF78035.1},
GN   map_3 {ECO:0000313|EMBL:SSU31322.1}, map_4
GN   {ECO:0000313|EMBL:SSM92346.1};
GN   ORFNames=A7M79_08180 {ECO:0000313|EMBL:OIH08354.1}, A7M90_04815
GN   {ECO:0000313|EMBL:OIG72371.1}, A7N09_12540
GN   {ECO:0000313|EMBL:OIF74617.1}, AB719_04705
GN   {ECO:0000313|EMBL:RDJ61195.1}, ABUW_1234
GN   {ECO:0000313|EMBL:AKA30982.1}, B4R90_02870
GN   {ECO:0000313|EMBL:OVL12321.1}, B9X91_03550
GN   {ECO:0000313|EMBL:OTL50035.1}, B9X95_11705
GN   {ECO:0000313|EMBL:OTM85450.1}, BGC29_02575
GN   {ECO:0000313|EMBL:ODP71121.1}, BWP00_06705
GN   {ECO:0000313|EMBL:OOD23107.1}, C2U32_08280
GN   {ECO:0000313|EMBL:AUT38008.1}, CBE85_00465
GN   {ECO:0000313|EMBL:OWK68248.1}, CBI29_02666
GN   {ECO:0000313|EMBL:ASF78035.1}, CEJ63_06330
GN   {ECO:0000313|EMBL:PAM74467.1}, CHQ89_03925
GN   {ECO:0000313|EMBL:OZT31344.1}, CPI82_15740
GN   {ECO:0000313|EMBL:PHQ01666.1}, CSB70_2491
GN   {ECO:0000313|EMBL:AVI33300.1}, CYQ93_08695
GN   {ECO:0000313|EMBL:RIL16084.1}, D3X42_16650
GN   {ECO:0000313|EMBL:RJO46114.1}, DCD77_06610
GN   {ECO:0000313|EMBL:PUV05937.1}, DOL94_04640
GN   {ECO:0000313|EMBL:PZM18289.1}, EA682_04370
GN   {ECO:0000313|EMBL:RSR22014.1}, IX87_07995
GN   {ECO:0000313|EMBL:AIL78573.1}, LV38_03303
GN   {ECO:0000313|EMBL:KZA22651.1}, NCTC13305_03581
GN   {ECO:0000313|EMBL:SUU32078.1}, SAMEA104305177_05951
GN   {ECO:0000313|EMBL:SSM92346.1}, SAMEA104305229_00525
GN   {ECO:0000313|EMBL:SSQ29282.1}, SAMEA104305242_02396
GN   {ECO:0000313|EMBL:SVJ98723.1}, SAMEA104305268_01571
GN   {ECO:0000313|EMBL:SSS25337.1}, SAMEA104305283_01206
GN   {ECO:0000313|EMBL:SSS24419.1}, SAMEA104305292_00658
GN   {ECO:0000313|EMBL:SSS43150.1}, SAMEA104305318_02021
GN   {ECO:0000313|EMBL:SST23566.1}, SAMEA104305320_04046
GN   {ECO:0000313|EMBL:SSU45021.1}, SAMEA104305325_02373
GN   {ECO:0000313|EMBL:SST82402.1}, SAMEA104305337_07399
GN   {ECO:0000313|EMBL:SSU31322.1}, SAMEA104305351_02247
GN   {ECO:0000313|EMBL:SSU74255.1};
OS   Acinetobacter baumannii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Acinetobacter;
OC   Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=470 {ECO:0000313|EMBL:PZM18289.1, ECO:0000313|Proteomes:UP000248662};
RN   [1] {ECO:0000313|EMBL:AIL78573.1, ECO:0000313|Proteomes:UP000028932}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AB030 {ECO:0000313|EMBL:AIL78573.1}, and AB30
RC   {ECO:0000313|Proteomes:UP000028932};
RA   Loewen P.C., Kumar A.;
RT   "Genome sequence of Acinetobacter baumannii AB030 genome.";
RL   Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AKA30982.1, ECO:0000313|Proteomes:UP000032746}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AB5075-UW {ECO:0000313|EMBL:AKA30982.1,
RC   ECO:0000313|Proteomes:UP000032746};
RX   PubMed=25845845;
RA   Gallagher L.A., Ramage E., Weiss E.J., Radey M., Hayden H.S.,
RA   Held K.G., Huse H.K., Zurawski D.V., Brittnacher M.J., Manoil C.;
RT   "Resources for Genetic and Genomic Analysis of Emerging Pathogen
RT   Acinetobacter baumannii.";
RL   J. Bacteriol. 197:2027-2035(2015).
RN   [3] {ECO:0000313|Proteomes:UP000032746}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AB5075-UW {ECO:0000313|Proteomes:UP000032746};
RA   Gallagher L.A., Hayden H.S., Weiss E.J., Hager K.R., Ramage E.,
RA   Radey M.R., Bydalek R., Manoil C., Miller S.I., Brittnacher M.J.;
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:CQR89265.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CHI-32 {ECO:0000313|EMBL:CQR89265.1};
RA   Jones S Lim;
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN   [5] {ECO:0000313|EMBL:RDJ61195.1, ECO:0000313|Proteomes:UP000254935}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KMDRAB19 {ECO:0000313|EMBL:RDJ61195.1,
RC   ECO:0000313|Proteomes:UP000254935};
RA   Feng Y., Chiu C.-H.;
RT   "Genome analysis of of clinical invasive Acinetobacter baumannii
RT   isolates in Taiwan.";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
RN   [6] {ECO:0000313|EMBL:KZA22651.1, ECO:0000313|Proteomes:UP000076314}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AB3638 {ECO:0000313|EMBL:KZA22651.1,
RC   ECO:0000313|Proteomes:UP000076314};
RA   Arivett B.A., Fiester S.E., Ream D.C., Actis L.A.;
RT   "Draft sequences of Acinetobacter baumannii isolates from wounded
RT   military personnel.";
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
RN   [7] {ECO:0000313|Proteomes:UP000179770, ECO:0000313|Proteomes:UP000179791, ECO:0000313|Proteomes:UP000179937}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=XH639 {ECO:0000313|EMBL:OIH08354.1,
RC   ECO:0000313|Proteomes:UP000179791}, XH647
RC   {ECO:0000313|EMBL:OIG72371.1, ECO:0000313|Proteomes:UP000179937}, and
RC   XH694 {ECO:0000313|EMBL:OIF74617.1,
RC   ECO:0000313|Proteomes:UP000179770};
RA   Hua X., Yu Y.;
RT   "The evolution of Acinetobacter baumannii in vivo.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN   [8] {ECO:0000313|EMBL:ODP71121.1, ECO:0000313|Proteomes:UP000094982}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=XH198 {ECO:0000313|EMBL:ODP71121.1,
RC   ECO:0000313|Proteomes:UP000094982};
RA   Mu X., Wang N., Li X., Shi K., Zhou Z., Yu Y., Hua X.;
RT   "The effect of colistin resistance-associated mutations on the fitness
RT   of Acinetobacter baumannii.";
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
RN   [9] {ECO:0000313|EMBL:OOD23107.1, ECO:0000313|Proteomes:UP000188718}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17945 {ECO:0000313|EMBL:OOD23107.1,
RC   ECO:0000313|Proteomes:UP000188718};
RA   Kozyreva V.K., Truong C.-L., Greninger A.L., Mukhopadhyay R.,
RA   Crandall J., Chaturvedi V.;
RT   "Validation and Implementation of CLIA-Compliant Whole Genome
RT   Sequencing (WGS) in Public Health Laboratory.";
RL   Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
RN   [10] {ECO:0000313|EMBL:OVL12321.1, ECO:0000313|Proteomes:UP000195460}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ABUH557 {ECO:0000313|EMBL:OVL12321.1,
RC   ECO:0000313|Proteomes:UP000195460};
RA   Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA   Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL   Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
RN   [11] {ECO:0000313|EMBL:OWK68248.1, ECO:0000313|Proteomes:UP000197394}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AB360 {ECO:0000313|EMBL:OWK68248.1,
RC   ECO:0000313|Proteomes:UP000197394};
RA   Wareham D.W., Bean D.C.;
RT   "Draft genome sequence of MDR A. baumannii AB360.";
RL   Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
RN   [12] {ECO:0000313|EMBL:OTL50035.1, ECO:0000313|Proteomes:UP000194699, ECO:0000313|Proteomes:UP000194957}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PR350 {ECO:0000313|EMBL:OTM85450.1,
RC   ECO:0000313|Proteomes:UP000194699}, and PR354
RC   {ECO:0000313|EMBL:OTL50035.1, ECO:0000313|Proteomes:UP000194957};
RA   Song R., Chenine A.L., Ruprecht R.M.;
RL   Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
RN   [13] {ECO:0000313|EMBL:PAM74467.1, ECO:0000313|Proteomes:UP000216072}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AB75 {ECO:0000313|EMBL:PAM74467.1,
RC   ECO:0000313|Proteomes:UP000216072};
RA   Chen Q.;
RT   "Carbapenem-resistant Acinetobacter baumannii strains.";
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN   [14] {ECO:0000313|EMBL:ASF78035.1, ECO:0000313|Proteomes:UP000197701}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A85 {ECO:0000313|EMBL:ASF78035.1,
RC   ECO:0000313|Proteomes:UP000197701};
RA   Hamidian M., Wick R.R., Hawkey J., Holt K.E., Hall R.M.;
RT   "Complete genome sequence of Acinetobacter baumannii strain A85
RT   belonging to global clone 1 (GC1).";
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN   [15] {ECO:0000313|EMBL:OZT31344.1, ECO:0000313|Proteomes:UP000216874}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DR1 {ECO:0000313|EMBL:OZT31344.1,
RC   ECO:0000313|Proteomes:UP000216874};
RA   Srinivasan V.B., Rajamohan G.;
RT   "Genome sequence, assembly and annotation.";
RL   Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
RN   [16] {ECO:0000313|EMBL:PHQ01666.1, ECO:0000313|Proteomes:UP000223291}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=I43 {ECO:0000313|EMBL:PHQ01666.1,
RC   ECO:0000313|Proteomes:UP000223291};
RA   Siqueira K.A., Mello I.S., Mendes T.A., Soares M.A.;
RT   "Draft genome of Acinetobacter baumannii strain I43, a mercury
RT   resistant bacteria.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
RN   [17] {ECO:0000313|EMBL:AUT38008.1, ECO:0000313|Proteomes:UP000236385}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ABNIH28 {ECO:0000313|EMBL:AUT38008.1,
RC   ECO:0000313|Proteomes:UP000236385};
RG   NISC Comparative Sequencing Program;
RA   Weingarten R.A., Johnson R.C., Conlan S., Ramsburg A.M., Dekker J.P.,
RA   Lau A.F., Khil P., Odom R.T., Deming C., Park M., Thomas P.J.,
RA   Henderson D.K., Palmore T.N., Segre J.A., Frank K.M.;
RT   "Genomic Analysis of Hospital Plumbing Reveals Diverse Reservoir of
RT   Bacterial Plasmids Conferring Carbapenem Resistance.";
RL   Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
RN   [18] {ECO:0000313|EMBL:AUT38008.1, ECO:0000313|Proteomes:UP000236385}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ABNIH28 {ECO:0000313|EMBL:AUT38008.1,
RC   ECO:0000313|Proteomes:UP000236385};
RA   Gaut B.S., Morton B.R., Clegg M.T., Duvall M.R.;
RL   Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
RN   [19] {ECO:0000313|EMBL:AVI33300.1, ECO:0000313|Proteomes:UP000257523}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AR_0070 {ECO:0000313|EMBL:AVI33300.1,
RC   ECO:0000313|Proteomes:UP000257523};
RA   Benahmed F.H., Lutgring J.D., Yoo B., Machado M., Brown A.,
RA   McAllister G., Perry A., Halpin A.L., Vavikolanu K., Ott S., Zhao X.,
RA   Tallon L., Sadzewicz L., Aluvathingal J., Nadendla S.,
RA   Voskania-kordi A., Simonyan V., Patel J., Shawar R.M.;
RT   "FDA/CDC Antimicrobial Resistant Isolate Bank Genome Sequencing.";
RL   Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
RN   [20] {ECO:0000313|EMBL:RIL16084.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=APC25 {ECO:0000313|EMBL:RIL16084.1};
RA   Freitas D.Y., Araujo S., Folador A.R.C., Ramos R.T.J., Azevedo J.S.N.,
RA   Tacao M., Silva A., Henriques I., Barauna R.A.;
RT   "Extended spectrum beta-lactamase-producing Gram-negative bacteria
RT   recovered from an Amazonian mesotrophic lake.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [21] {ECO:0000313|EMBL:PUV05937.1, ECO:0000313|Proteomes:UP000251219}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SH37 {ECO:0000313|EMBL:PUV05937.1,
RC   ECO:0000313|Proteomes:UP000251219};
RA   Yang Y., Yu Y.;
RT   "Sulbactam resistance mechanism of Acinetobacter baumannii.";
RL   Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [22] {ECO:0000313|EMBL:PZM18289.1, ECO:0000313|Proteomes:UP000248662}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R10 {ECO:0000313|EMBL:PZM18289.1,
RC   ECO:0000313|Proteomes:UP000248662};
RA   Bonnin R.A., Levy M., Cuzon G., Dortet L., Naas T.;
RT   "Carbapenemase-producing Acinetobacter spp. from environmental sources
RT   in an hospital from French Polynesia.";
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN   [23] {ECO:0000313|EMBL:SUU32078.1, ECO:0000313|Proteomes:UP000255154}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC13305 {ECO:0000313|EMBL:SUU32078.1,
RC   ECO:0000313|Proteomes:UP000255154};
RG   Pathogen Informatics;
RA   Doyle S.;
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN   [24] {ECO:0000313|Proteomes:UP000252694, ECO:0000313|Proteomes:UP000253591, ECO:0000313|Proteomes:UP000258872}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4300STDY7045681 {ECO:0000313|EMBL:SSM92346.1,
RC   ECO:0000313|Proteomes:UP000264059}, 4300STDY7045733
RC   {ECO:0000313|EMBL:SSQ29282.1, ECO:0000313|Proteomes:UP000263963},
RC   4300STDY7045746 {ECO:0000313|EMBL:SVJ98723.1,
RC   ECO:0000313|Proteomes:UP000258872}, 4300STDY7045773
RC   {ECO:0000313|EMBL:SSS25337.1}, 4300STDY7045788
RC   {ECO:0000313|EMBL:SSS24419.1, ECO:0000313|Proteomes:UP000264160},
RC   4300STDY7045797 {ECO:0000313|EMBL:SSS43150.1,
RC   ECO:0000313|Proteomes:UP000262639}, 4300STDY7045823
RC   {ECO:0000313|EMBL:SST23566.1, ECO:0000313|Proteomes:UP000252694},
RC   4300STDY7045825 {ECO:0000313|EMBL:SSU45021.1,
RC   ECO:0000313|Proteomes:UP000263100}, 4300STDY7045830
RC   {ECO:0000313|EMBL:SST82402.1, ECO:0000313|Proteomes:UP000264417},
RC   4300STDY7045842 {ECO:0000313|EMBL:SSU31322.1,
RC   ECO:0000313|Proteomes:UP000263147}, and 4300STDY7045856
RC   {ECO:0000313|EMBL:SSU74255.1, ECO:0000313|Proteomes:UP000253591};
RG   Pathogen Informatics;
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
RN   [25] {ECO:0000313|EMBL:RJO46114.1, ECO:0000313|Proteomes:UP000266128}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC1 {ECO:0000313|EMBL:RJO46114.1,
RC   ECO:0000313|Proteomes:UP000266128};
RA   Cerezales M., Xanthopoulou K., Ertel J., Bustamante Z., Seifert H.,
RA   Gallego L., Higgins P.G.;
RT   "Acinetobacter baumannii analysis by core genome MLST in two hospitals
RT   in Bolivia: endemicity of international clone 7 isolates.";
RL   Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
RN   [26] {ECO:0000213|PDB:6MRF}
RP   X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 12-272.
RA   Edwards T.E., Mayclin S.J., Lorimer D.D., Horanyi P.S.,
RA   Seattle Structural Genomics Center for Infectious Disease.;
RT   "Crystal structure of a Methionine aminopeptidase MetAP from
RT   Acinetobacter baumannii.";
RL   Submitted (OCT-2018) to the PDB data bank.
RN   [27] {ECO:0000313|EMBL:RSR22014.1, ECO:0000313|Proteomes:UP000273400}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TG89524 {ECO:0000313|EMBL:RSR22014.1,
RC   ECO:0000313|Proteomes:UP000273400};
RA   Sahl J.W.;
RT   "GWAS and RNA-Seq identify cryptic mechanisms of antimicrobial
RT   resistance in Acinetobacter baumannii.";
RL   Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Removes the N-terminal methionine from nascent proteins.
CC       The N-terminal methionine is often cleaved when the second residue
CC       in the primary sequence is small and uncharged (Met-Ala-, Cys,
CC       Gly, Pro, Ser, Thr, or Val). Requires deformylation of the
CC       N(alpha)-formylated initiator methionine before it can be
CC       hydrolyzed. {ECO:0000256|HAMAP-Rule:MF_01974}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of N-terminal amino acids, preferentially
CC         methionine, from peptides and arylamides.; EC=3.4.11.18;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01974,
CC         ECO:0000256|RuleBase:RU003653};
CC   -!- COFACTOR:
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01974, ECO:0000256|RuleBase:RU003653};
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01974, ECO:0000256|RuleBase:RU003653};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01974, ECO:0000256|RuleBase:RU003653};
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01974, ECO:0000256|RuleBase:RU003653};
CC       Note=Binds 2 divalent metal cations per subunit. Has a high-
CC       affinity and a low affinity metal-binding site. The true nature of
CC       the physiological cofactor is under debate. The enzyme is active
CC       with cobalt, zinc, manganese or divalent iron ions. Most likely,
CC       methionine aminopeptidases function as mononuclear Fe(2+)-
CC       metalloproteases under physiological conditions, and the
CC       catalytically relevant metal-binding site has been assigned to the
CC       histidine-containing high-affinity site. {ECO:0000256|HAMAP-
CC       Rule:MF_01974, ECO:0000256|RuleBase:RU003653};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01974}.
CC   -!- SIMILARITY: Belongs to the peptidase M24A family. Methionine
CC       aminopeptidase type 1 subfamily. {ECO:0000256|HAMAP-
CC       Rule:MF_01974}.
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DR   EMBL; CP009257; AIL78573.1; -; Genomic_DNA.
DR   EMBL; CP008706; AKA30982.1; -; Genomic_DNA.
DR   EMBL; CP021782; ASF78035.1; -; Genomic_DNA.
DR   EMBL; CP026125; AUT38008.1; -; Genomic_DNA.
DR   EMBL; CP027178; AVI33300.1; -; Genomic_DNA.
DR   EMBL; CVLF01000087; CQR89265.1; -; Genomic_DNA.
DR   EMBL; LRDW01000036; KZA22651.1; -; Genomic_DNA.
DR   EMBL; MDWM01000086; ODP71121.1; -; Genomic_DNA.
DR   EMBL; LYIX01002080; OIF74617.1; -; Genomic_DNA.
DR   EMBL; LYKI01000023; OIG72371.1; -; Genomic_DNA.
DR   EMBL; LYKQ01000028; OIH08354.1; -; Genomic_DNA.
DR   EMBL; MTGG01000011; OOD23107.1; -; Genomic_DNA.
DR   EMBL; NGCH01000216; OTL50035.1; -; Genomic_DNA.
DR   EMBL; NGEL01000129; OTM85450.1; -; Genomic_DNA.
DR   EMBL; NCYH01000005; OVL12321.1; -; Genomic_DNA.
DR   EMBL; NGKM01000001; OWK68248.1; -; Genomic_DNA.
DR   EMBL; NOXP01000002; OZT31344.1; -; Genomic_DNA.
DR   EMBL; NKKG01000021; PAM74467.1; -; Genomic_DNA.
DR   EMBL; NXDV01000014; PHQ01666.1; -; Genomic_DNA.
DR   EMBL; QCXV01000006; PUV05937.1; -; Genomic_DNA.
DR   EMBL; QKWF01000036; PZM18289.1; -; Genomic_DNA.
DR   EMBL; LFHE01000044; RDJ61195.1; -; Genomic_DNA.
DR   EMBL; PYSX01000006; RIL16084.1; -; Genomic_DNA.
DR   EMBL; QXPV01000132; RJO46114.1; -; Genomic_DNA.
DR   EMBL; RFDM01000003; RSR22014.1; -; Genomic_DNA.
DR   EMBL; UFGS01000161; SSM92346.1; -; Genomic_DNA.
DR   EMBL; UFJW01000005; SSQ29282.1; -; Genomic_DNA.
DR   EMBL; UFLV01000015; SSS24419.1; -; Genomic_DNA.
DR   EMBL; UFLS01000087; SSS25337.1; -; Genomic_DNA.
DR   EMBL; UFLY01000003; SSS43150.1; -; Genomic_DNA.
DR   EMBL; UFMQ01000008; SST23566.1; -; Genomic_DNA.
DR   EMBL; UFNA01000096; SST82402.1; -; Genomic_DNA.
DR   EMBL; UFNQ01000022; SSU31322.1; -; Genomic_DNA.
DR   EMBL; UFNW01000445; SSU45021.1; -; Genomic_DNA.
DR   EMBL; UFNX01000008; SSU74255.1; -; Genomic_DNA.
DR   EMBL; UFSC01000003; SUU32078.1; -; Genomic_DNA.
DR   EMBL; UIRJ01000068; SVJ98723.1; -; Genomic_DNA.
DR   RefSeq; WP_001089491.1; NZ_ULHD01000042.1.
DR   PDB; 6MRF; X-ray; 1.65 A; A=12-272.
DR   PDBsum; 6MRF; -.
DR   STRING; 470.IX87_07995; -.
DR   EnsemblBacteria; AIL78573; AIL78573; IX87_07995.
DR   EnsemblBacteria; AKA30982; AKA30982; ABUW_1234.
DR   EnsemblBacteria; AKQ26271; AKQ26271; ACX60_05910.
DR   EnsemblBacteria; AMN02327; AMN02327; AZE33_14285.
DR   EnsemblBacteria; BAP65968; BAP65968; IOMTU433_1184.
DR   EnsemblBacteria; KMV05062; KMV05062; AB895_0353.
DR   EnsemblBacteria; KMV10717; KMV10717; AB988_0028.
DR   EnsemblBacteria; KQD20501; KQD20501; APD06_11055.
DR   EnsemblBacteria; KQK46469; KQK46469; AQ482_07905.
DR   EnsemblBacteria; KUI76164; KUI76164; AQ480_02225.
DR   EnsemblBacteria; KZA22651; KZA22651; LV38_03303.
DR   EnsemblBacteria; OBE59901; OBE59901; A7934_09120.
DR   EnsemblBacteria; ODP71121; ODP71121; BGC29_02575.
DR   GeneID; 31348596; -.
DR   KEGG; abaa:IX88_14615; -.
DR   KEGG; abau:IX87_07995; -.
DR   KEGG; abk:LX00_12565; -.
DR   KEGG; abw:BL01_08915; -.
DR   PATRIC; fig|470.1288.peg.1761; -.
DR   eggNOG; ENOG4105CA1; Bacteria.
DR   eggNOG; COG0024; LUCA.
DR   KO; K01265; -.
DR   OrthoDB; 1285136at2; -.
DR   Proteomes; UP000028932; Chromosome.
DR   Proteomes; UP000032746; Chromosome.
DR   Proteomes; UP000076314; Unassembled WGS sequence.
DR   Proteomes; UP000094982; Unassembled WGS sequence.
DR   Proteomes; UP000179770; Unassembled WGS sequence.
DR   Proteomes; UP000179791; Unassembled WGS sequence.
DR   Proteomes; UP000179937; Unassembled WGS sequence.
DR   Proteomes; UP000188718; Unassembled WGS sequence.
DR   Proteomes; UP000194699; Unassembled WGS sequence.
DR   Proteomes; UP000194957; Unassembled WGS sequence.
DR   Proteomes; UP000195460; Unassembled WGS sequence.
DR   Proteomes; UP000197394; Unassembled WGS sequence.
DR   Proteomes; UP000197701; Chromosome.
DR   Proteomes; UP000216072; Unassembled WGS sequence.
DR   Proteomes; UP000216874; Unassembled WGS sequence.
DR   Proteomes; UP000223291; Unassembled WGS sequence.
DR   Proteomes; UP000236385; Chromosome.
DR   Proteomes; UP000248662; Unassembled WGS sequence.
DR   Proteomes; UP000251219; Unassembled WGS sequence.
DR   Proteomes; UP000252694; Unassembled WGS sequence.
DR   Proteomes; UP000253591; Unassembled WGS sequence.
DR   Proteomes; UP000254935; Unassembled WGS sequence.
DR   Proteomes; UP000255154; Unassembled WGS sequence.
DR   Proteomes; UP000257523; Chromosome.
DR   Proteomes; UP000258872; Unassembled WGS sequence.
DR   Proteomes; UP000262639; Unassembled WGS sequence.
DR   Proteomes; UP000263100; Unassembled WGS sequence.
DR   Proteomes; UP000263147; Unassembled WGS sequence.
DR   Proteomes; UP000263963; Unassembled WGS sequence.
DR   Proteomes; UP000264059; Unassembled WGS sequence.
DR   Proteomes; UP000264160; Unassembled WGS sequence.
DR   Proteomes; UP000264417; Unassembled WGS sequence.
DR   Proteomes; UP000266128; Unassembled WGS sequence.
DR   Proteomes; UP000273400; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0070006; F:metalloaminopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0070084; P:protein initiator methionine removal; IEA:UniProtKB-UniRule.
DR   CDD; cd01086; MetAP1; 1.
DR   HAMAP; MF_01974; MetAP_1; 1.
DR   InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR   InterPro; IPR000994; Pept_M24.
DR   InterPro; IPR001714; Pept_M24_MAP.
DR   InterPro; IPR002467; Pept_M24A_MAP1.
DR   Pfam; PF00557; Peptidase_M24; 1.
DR   PRINTS; PR00599; MAPEPTIDASE.
DR   SUPFAM; SSF55920; SSF55920; 1.
DR   TIGRFAMs; TIGR00500; met_pdase_I; 1.
DR   PROSITE; PS00680; MAP_1; 1.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0000213|PDB:6MRF};
KW   Aminopeptidase {ECO:0000256|HAMAP-Rule:MF_01974,
KW   ECO:0000256|RuleBase:RU003653, ECO:0000313|EMBL:PZM18289.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000028932,
KW   ECO:0000313|Proteomes:UP000032746, ECO:0000313|Proteomes:UP000076314,
KW   ECO:0000313|Proteomes:UP000094982};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01974,
KW   ECO:0000313|EMBL:PZM18289.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01974,
KW   ECO:0000256|RuleBase:RU003653};
KW   Protease {ECO:0000256|HAMAP-Rule:MF_01974,
KW   ECO:0000256|RuleBase:RU003653}.
FT   DOMAIN       19    256       Peptidase_M24. {ECO:0000259|Pfam:
FT                                PF00557}.
FT   METAL       110    110       Divalent metal cation 1.
FT                                {ECO:0000256|HAMAP-Rule:MF_01974}.
FT   METAL       121    121       Divalent metal cation 1.
FT                                {ECO:0000256|HAMAP-Rule:MF_01974}.
FT   METAL       121    121       Divalent metal cation 2; catalytic.
FT                                {ECO:0000256|HAMAP-Rule:MF_01974}.
FT   METAL       185    185       Divalent metal cation 2; catalytic; via
FT                                tele nitrogen. {ECO:0000256|HAMAP-Rule:
FT                                MF_01974}.
FT   METAL       218    218       Divalent metal cation 2; catalytic.
FT                                {ECO:0000256|HAMAP-Rule:MF_01974}.
FT   METAL       249    249       Divalent metal cation 1.
FT                                {ECO:0000256|HAMAP-Rule:MF_01974}.
FT   METAL       249    249       Divalent metal cation 2; catalytic.
FT                                {ECO:0000256|HAMAP-Rule:MF_01974}.
FT   BINDING      92     92       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01974}.
FT   BINDING     192    192       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01974}.
SQ   SEQUENCE   275 AA;  30374 MW;  6D82AB2AE6DC1802 CRC64;
     MNSTYTAPRR LIKTPDEIEK MRIAGRLAAE VLDMIKPHIK AGVSTLELDT ICRNHIENVQ
     HAIPACVGYG GAPGRPAFQH SICTSVNHVV CHGIPSENKI LKNGDILNID VTVIKDGYHG
     DTNMMYIVGG ETSILANRLC KVAQEAMYRG MATVRDGSYL GDIGHAIQKY VESERFSVVR
     EYCGHGIGTV FHDEPQVLHY GQAGTGMRLE AGMTFTIEPM VNAGVWQTKL LGDKWTVVTK
     DHKLSAQYEH TILVTKTGIE VLTARPEEDL SRFNQ
//