ID   V5VCW7_ACIBA            Unreviewed;       275 AA.
AC   V5VCW7;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   07-SEP-2016, entry version 29.
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:BAP65968.1};
GN   Synonyms=map1 {ECO:0000313|EMBL:AKA30982.1}, map_1
GN   {ECO:0000313|EMBL:KZA22651.1};
GN   ORFNames=AB895_0353 {ECO:0000313|EMBL:KMV05062.1}, AB988_0028
GN   {ECO:0000313|EMBL:KMV10717.1}, ABUW_1234
GN   {ECO:0000313|EMBL:AKA30982.1}, ACX60_05910
GN   {ECO:0000313|EMBL:AKQ26271.1}, APD06_11055
GN   {ECO:0000313|EMBL:KQD20501.1}, AQ480_02225
GN   {ECO:0000313|EMBL:KUI76164.1}, AQ482_07905
GN   {ECO:0000313|EMBL:KQK46469.1}, AZE33_14285
GN   {ECO:0000313|EMBL:AMN02327.1}, IOMTU433_1184
GN   {ECO:0000313|EMBL:BAP65968.1}, IX87_07995
GN   {ECO:0000313|EMBL:AIL78573.1}, LV38_03303
GN   {ECO:0000313|EMBL:KZA22651.1}, TE32_05490
GN   {ECO:0000313|EMBL:AKJ45008.1};
OS   Acinetobacter baumannii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Acinetobacter;
OC   Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=470 {ECO:0000313|EMBL:KQD20501.1, ECO:0000313|Proteomes:UP000051322};
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:BAP65968.1, ECO:0000313|Proteomes:UP000031644}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IOMTU 433 {ECO:0000313|EMBL:BAP65968.1,
RC   ECO:0000313|Proteomes:UP000031644};
RA   Tada T., Shrestha S., Miyoshi-Akiyama T., Shimada K., Kirikae T.;
RT   "Complete genome sequence of Acinetobacter baumannii IOMTU433.";
RL   Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:AKA30982.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=AB5075-UW {ECO:0000313|EMBL:AKA30982.1};
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   [4] {ECO:0000313|EMBL:KQK46469.1, ECO:0000313|Proteomes:UP000053083, ECO:0000313|Proteomes:UP000054136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ab03 {ECO:0000313|EMBL:KUI76164.1,
RC   ECO:0000313|Proteomes:UP000054136}, and Ab18
RC   {ECO:0000313|EMBL:KQK46469.1, ECO:0000313|Proteomes:UP000053083};
RA   Leite G., Oliveira M.S., Perdigao-Neto L.V., Rocha C.K., Guimaraes T.,
RA   Rizek C.F., Levin A.S., Costa S.F.;
RT   "Antimicrobial combinations against pan-resistant Acinetobacter
RT   baumannii isolates with different mechanisms of resistance.";
RL   PLoS ONE 0:0-0(2015).
RN   [5] {ECO:0000313|EMBL:AKQ26271.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 17978-mff {ECO:0000313|EMBL:AKQ26271.1};
RX   PubMed=26170289; DOI=10.1073/pnas.1502966112;
RA   Weber B.S., Ly P.M., Irwin J.N., Pukatzki S., Feldman M.F.;
RT   "A multidrug resistance plasmid contains the molecular switch for type
RT   VI secretion in Acinetobacter baumannii.";
RL   Proc. Natl. Acad. Sci. U.S.A. 112:9442-9447(2015).
RN   [6] {ECO:0000313|EMBL:AKJ45008.1, ECO:0000313|Proteomes:UP000035522}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=XH386 {ECO:0000313|EMBL:AKJ45008.1,
RC   ECO:0000313|Proteomes:UP000035522};
RA   Fang Y., Hua X., Feng Y., Lil X., Weng J., Ruan Z., Shang S., Yu Y.;
RT   "Complete genome sequence of a multi-drug resistant ST208
RT   Acinetobacter baumannii.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
RN   [7] {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   [8] {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   [9] {ECO:0000313|Proteomes:UP000036024}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17978-mff {ECO:0000313|Proteomes:UP000036024};
RA   Weber B.S., Ly P.M., Irwin J.N., Pukatzki S., Feldman M.F.;
RT   "A multidrug resistance plasmid contains the molecular switch for type
RT   VI secretion in Acinetobacter baumannii.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN   [10] {ECO:0000313|EMBL:KMV05062.1, ECO:0000313|Proteomes:UP000036720}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B8342 {ECO:0000313|EMBL:KMV05062.1,
RC   ECO:0000313|Proteomes:UP000036720};
RA   Vijaykumar S., Balaji V., Biswas I.;
RT   "Complete genome sequence of Acinetobacter baumannii strain B8342, a
RT   motility positive clinical isolate.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN   [11] {ECO:0000313|EMBL:KMV10717.1, ECO:0000313|Proteomes:UP000037552}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SP1917 {ECO:0000313|EMBL:KMV10717.1,
RC   ECO:0000313|Proteomes:UP000037552};
RA   Vijaykumar S., Balaji V., Biswas I.;
RT   "Draft genome sequences of two multidrug resistant Acinetobacter
RT   baumannii isolates from Southern India.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN   [12] {ECO:0000313|EMBL:KQD20501.1, ECO:0000313|Proteomes:UP000051322}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ABBL059 {ECO:0000313|EMBL:KQD20501.1,
RC   ECO:0000313|Proteomes:UP000051322};
RA   Ozer E.A., Fitzpatrick M.A., Hauser A.R.;
RT   "The utility of whole genome sequencing in characterizing
RT   Acinetobacter epidemiology and analyzing hospital outbreaks.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [13] {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   [14] {ECO:0000313|EMBL:AMN02327.1, ECO:0000313|Proteomes:UP000070590}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=XH858 {ECO:0000313|EMBL:AMN02327.1,
RC   ECO:0000313|Proteomes:UP000070590};
RA   Feng Y., Hua X., Yu Y.;
RT   "Complete genome of Acinetobacter baumannii str. XH858.";
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: Release of N-terminal amino acids,
CC       preferentially methionine, from peptides and arylamides.
CC       {ECO:0000256|HAMAP-Rule:MF_01974, 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}.
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DR   EMBL; CP009257; AIL78573.1; -; Genomic_DNA.
DR   EMBL; CP008706; AKA30982.1; -; Genomic_DNA.
DR   EMBL; CP010779; AKJ45008.1; -; Genomic_DNA.
DR   EMBL; CP012004; AKQ26271.1; -; Genomic_DNA.
DR   EMBL; CP014528; AMN02327.1; -; Genomic_DNA.
DR   EMBL; AP014649; BAP65968.1; -; Genomic_DNA.
DR   EMBL; CVLF01000087; CQR89265.1; -; Genomic_DNA.
DR   EMBL; LFYZ01000001; KMV05062.1; -; Genomic_DNA.
DR   EMBL; LFYW01000001; KMV10717.1; -; Genomic_DNA.
DR   EMBL; LLFE01000041; KQD20501.1; -; Genomic_DNA.
DR   EMBL; LMBN01000110; KQK46469.1; -; Genomic_DNA.
DR   EMBL; LMZH01000026; KUI76164.1; -; Genomic_DNA.
DR   EMBL; LRDW01000036; KZA22651.1; -; Genomic_DNA.
DR   RefSeq; WP_001089491.1; NZ_LRMK01000083.1.
DR   STRING; 575584.HMPREF0010_02353; -.
DR   EnsemblBacteria; AIL78573; AIL78573; IX87_07995.
DR   EnsemblBacteria; AJB66358; AJB66358; RU84_05625.
DR   EnsemblBacteria; AKA30982; AKA30982; ABUW_1234.
DR   EnsemblBacteria; AKJ45008; AKJ45008; TE32_05490.
DR   EnsemblBacteria; AKQ26271; AKQ26271; ACX60_05910.
DR   EnsemblBacteria; BAP65968; BAP65968; IOMTU433_1184.
DR   EnsemblBacteria; CQR67878; CQR67878; CQR67878.
DR   EnsemblBacteria; CRF38470; CRF38470; CRF38470.
DR   EnsemblBacteria; KGF60633; KGF60633; LH92_12295.
DR   EnsemblBacteria; KHT74985; KHT74985; RW53_02290.
DR   EnsemblBacteria; KHT85672; KHT85672; RW49_11850.
DR   EnsemblBacteria; KHV18126; KHV18126; RW59_04665.
DR   EnsemblBacteria; KHV22247; KHV22247; RW56_05425.
DR   EnsemblBacteria; KHV28669; KHV28669; RW57_01585.
DR   EnsemblBacteria; KHV33176; KHV33176; RW60_02595.
DR   EnsemblBacteria; KHV33855; KHV33855; RW58_12575.
DR   EnsemblBacteria; KHX40556; KHX40556; RQ85_11030.
DR   EnsemblBacteria; KHY10257; KHY10257; RQ47_01330.
DR   EnsemblBacteria; KIA15515; KIA15515; RP89_09635.
DR   EnsemblBacteria; KJE61738; KJE61738; RQ42_05190.
DR   EnsemblBacteria; KJE63625; KJE63625; RQ37_03770.
DR   EnsemblBacteria; KJE68647; KJE68647; RR20_01165.
DR   EnsemblBacteria; KJE73081; KJE73081; RQ98_01200.
DR   EnsemblBacteria; KJE74574; KJE74574; RR27_02775.
DR   EnsemblBacteria; KJF02887; KJF02887; RR21_08695.
DR   EnsemblBacteria; KJF05880; KJF05880; RR22_11905.
DR   EnsemblBacteria; KJF11281; KJF11281; RQ64_07755.
DR   EnsemblBacteria; KJF15001; KJF15001; RQ49_01840.
DR   EnsemblBacteria; KJG75542; KJG75542; RQ82_03725.
DR   EnsemblBacteria; KJG77179; KJG77179; RQ80_13680.
DR   EnsemblBacteria; KJG81168; KJG81168; RQ24_04615.
DR   EnsemblBacteria; KKA96472; KKA96472; VM83_11790.
DR   EnsemblBacteria; KKZ40688; KKZ40688; UN98_08720.
DR   EnsemblBacteria; KKZ44945; KKZ44945; UO01_16465.
DR   EnsemblBacteria; KMV03238; KMV03238; AB994_1981.
DR   EnsemblBacteria; KMV05062; KMV05062; AB895_0353.
DR   EnsemblBacteria; KMV10717; KMV10717; AB988_0028.
DR   EnsemblBacteria; KMV27219; KMV27219; AB987_2690.
DR   EnsemblBacteria; KOP89520; KOP89520; AKG97_01110.
DR   EnsemblBacteria; KPA50106; KPA50106; AC795_04265.
DR   KEGG; abaa:IX88_14615; -.
DR   KEGG; abau:IX87_07995; -.
DR   KEGG; abk:LX00_12565; -.
DR   KEGG; abw:BL01_08915; -.
DR   eggNOG; ENOG4105CA1; Bacteria.
DR   eggNOG; COG0024; LUCA.
DR   KO; K01265; -.
DR   Proteomes; UP000028932; Chromosome.
DR   Proteomes; UP000031644; Chromosome.
DR   Proteomes; UP000032746; Chromosome.
DR   Proteomes; UP000035522; Chromosome.
DR   Proteomes; UP000036024; Chromosome.
DR   Proteomes; UP000036720; Unassembled WGS sequence.
DR   Proteomes; UP000037552; Unassembled WGS sequence.
DR   Proteomes; UP000051322; Unassembled WGS sequence.
DR   Proteomes; UP000053083; Unassembled WGS sequence.
DR   Proteomes; UP000054136; Unassembled WGS sequence.
DR   Proteomes; UP000070590; Chromosome.
DR   Proteomes; UP000076314; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0070006; F:metalloaminopeptidase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0070084; P:protein initiator methionine removal; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.90.230.10; -; 1.
DR   HAMAP; MF_01974; MetAP_1; 1.
DR   InterPro; IPR001714; Pept_M24_MAP.
DR   InterPro; IPR000994; Pept_M24_structural-domain.
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   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|HAMAP-Rule:MF_01974,
KW   ECO:0000256|RuleBase:RU003653, ECO:0000313|EMBL:KQD20501.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000028932,
KW   ECO:0000313|Proteomes:UP000031644, ECO:0000313|Proteomes:UP000032746,
KW   ECO:0000313|Proteomes:UP000035522};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01974,
KW   ECO:0000313|EMBL:KQD20501.1};
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
//