ID   V5VCW7_ACIBA            Unreviewed;       275 AA.
AC   V5VCW7;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   24-JUL-2024, entry version 89.
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}, map3
GN   {ECO:0000313|EMBL:CUW35909.1}, map_2 {ECO:0000313|EMBL:KZA12740.1};
GN   ORFNames=A7M90_04815 {ECO:0000313|EMBL:OIG72371.1}, ABR2091_2512
GN   {ECO:0000313|EMBL:CUW35909.1}, ABUW_1234
GN   {ECO:0000313|EMBL:AKA30982.1}, APD17_10230
GN   {ECO:0000313|EMBL:KQD54506.1}, AUO97_00550
GN   {ECO:0000313|EMBL:APP29388.1}, B9W25_05720
GN   {ECO:0000313|EMBL:PRN35987.1}, B9X95_11705
GN   {ECO:0000313|EMBL:OTM85450.1}, CBE85_00465
GN   {ECO:0000313|EMBL:OWK68248.1}, CV954_005965
GN   {ECO:0000313|EMBL:PQL84274.1}, DOL94_04640
GN   {ECO:0000313|EMBL:PZM18289.1}, EA706_00955
GN   {ECO:0000313|EMBL:RSQ49839.1}, EA722_08630
GN   {ECO:0000313|EMBL:RSP76616.1}, EJ507_19900
GN   {ECO:0000313|EMBL:RTB85817.1}, F2P40_02010
GN   {ECO:0000313|EMBL:MQR48113.1}, F4T85_00585
GN   {ECO:0000313|EMBL:MQZ66891.1}, FJU42_15260
GN   {ECO:0000313|EMBL:TPU61657.1}, G3N53_09925
GN   {ECO:0000313|EMBL:NDW41392.1}, GNY86_13630
GN   {ECO:0000313|EMBL:MVM92566.1}, GSE42_14095
GN   {ECO:0000313|EMBL:MYM79056.1}, IAG11_02480
GN   {ECO:0000313|EMBL:MBD0218758.1}, IMO23_12425
GN   {ECO:0000313|EMBL:QPF12406.1}, ITE13_14325
GN   {ECO:0000313|EMBL:MBP4960678.1}, LV35_03405
GN   {ECO:0000313|EMBL:KZA12740.1}, MKP18_000955
GN   {ECO:0000313|EMBL:EKU3567577.1}, P9867_17035
GN   {ECO:0000313|EMBL:MDK4883330.1}, SAMEA104305318_02021
GN   {ECO:0000313|EMBL:SST23566.1}, SAMEA4394745_01927
GN   {ECO:0000313|EMBL:SSI43005.1};
OS   Acinetobacter baumannii.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=470 {ECO:0000313|EMBL:PZM18289.1, ECO:0000313|Proteomes:UP000248662};
RN   [1] {ECO:0000313|EMBL:APP29388.1, ECO:0000313|Proteomes:UP000072389}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17978 {ECO:0000313|Proteomes:UP000072389}, and ATCC
RC   17978-VU {ECO:0000313|EMBL:APP29388.1};
RX   PubMed=25136007; DOI=10.1128/AAC.03074-14;
RA   Fernando D.M., Xu W., Loewen P.C., Zhanel G.G., Kumar A.;
RT   "Triclosan can select for an AdeIJK-overexpressing mutant of Acinetobacter
RT   baumannii ATCC 17978 that displays reduced susceptibility to multiple
RT   antibiotics.";
RL   Antimicrob. Agents Chemother. 58:6424-6431(2014).
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., Held K.G.,
RA   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., Radey M.R.,
RA   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:KQD54506.1, ECO:0000313|Proteomes:UP000051023}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ABBL067b {ECO:0000313|EMBL:KQD54506.1,
RC   ECO:0000313|Proteomes:UP000051023};
RA   Ozer E.A., Fitzpatrick M.A., Hauser A.R.;
RT   "The utility of whole genome sequencing in characterizing Acinetobacter
RT   epidemiology and analyzing hospital outbreaks.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [5] {ECO:0000313|EMBL:CUW35909.1, ECO:0000313|Proteomes:UP000066661}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R2091 {ECO:0000313|EMBL:CUW35909.1};
RA   Wibberg D.;
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN   [6] {ECO:0000313|EMBL:APP29388.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 17978-VU {ECO:0000313|EMBL:APP29388.1};
RA   Singh M.K., Fernando D.M., Kumar A.;
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN   [7] {ECO:0000313|EMBL:KZA12740.1, ECO:0000313|Proteomes:UP000076296}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AB2828 {ECO:0000313|EMBL:KZA12740.1,
RC   ECO:0000313|Proteomes:UP000076296};
RA   Arivett B.A., Fiester S.E., Ream D.C., Actis L.A.;
RT   "Draft sequences of Acinetobacter baumannii isolates from wounded military
RT   personnel.";
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
RN   [8] {ECO:0000313|EMBL:OIG72371.1, ECO:0000313|Proteomes:UP000179937}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=XH647 {ECO:0000313|EMBL:OIG72371.1,
RC   ECO:0000313|Proteomes:UP000179937};
RA   Hua X., Yu Y.;
RT   "The evolution of Acinetobacter baumannii in vivo.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN   [9] {ECO:0000313|EMBL:APP29388.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 17978-VU {ECO:0000313|EMBL:APP29388.1};
RA   Singh M., Fernando D., Kumar A.;
RL   Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
RN   [10] {ECO:0000313|EMBL:MYM79056.1, ECO:0000313|Proteomes:UP000480763}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DMS06669 {ECO:0000313|EMBL:MYM79056.1,
RC   ECO:0000313|Proteomes:UP000480763};
RX   PubMed=29137647;
RA   Si-Tuan N., Ngoc H.M., Hang P.T.T., Nguyen C., Van P.H., Huong N.T.;
RT   "New eight genes identified at the clinical multidrug-resistant
RT   Acinetobacter baumannii DMS06669 strain in a Vietnam hospital.";
RL   Ann. Clin. Microbiol. Antimicrob. 16:0-74(2017).
RN   [11] {ECO:0000313|EMBL:PRN35987.1, ECO:0000313|Proteomes:UP000237823}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KUFAR57 {ECO:0000313|EMBL:PRN35987.1,
RC   ECO:0000313|Proteomes:UP000237823};
RA   Nasser K., Habibi N., Khan M.W., Purohit P., Al-Obaid I., Dhar R.,
RA   Al-Fouzan W., Mustafa A.S.;
RT   "Comparison of Acinetobacter baumannii whole genome sequences from two
RT   major hospitals in Kuwait.";
RL   Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
RN   [12] {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   [13] {ECO:0000313|EMBL:OTM85450.1, ECO:0000313|Proteomes:UP000194699}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PR350 {ECO:0000313|EMBL:OTM85450.1,
RC   ECO:0000313|Proteomes:UP000194699};
RA   Song R., Chenine A.L., Ruprecht R.M.;
RL   Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
RN   [14] {ECO:0000313|EMBL:PQL84274.1, ECO:0000313|Proteomes:UP000233757}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZQ8 {ECO:0000313|EMBL:PQL84274.1,
RC   ECO:0000313|Proteomes:UP000233757};
RA   Qasim Z.J.;
RT   "Acinetobacter baumanii whole genome sequence.";
RL   Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
RN   [15] {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 in
RT   an hospital from French Polynesia.";
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN   [16] {ECO:0000313|Proteomes:UP000252694, ECO:0000313|Proteomes:UP000262697}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4300STDY6542375 {ECO:0000313|EMBL:SSI43005.1,
RC   ECO:0000313|Proteomes:UP000262697}, and 4300STDY7045823
RC   {ECO:0000313|EMBL:SST23566.1, ECO:0000313|Proteomes:UP000252694};
RG   Pathogen Informatics;
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
RN   [17] {ECO:0007829|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 Acinetobacter
RT   baumannii.";
RL   Submitted (OCT-2018) to the PDB data bank.
RN   [18] {ECO:0000313|Proteomes:UP000269597, ECO:0000313|Proteomes:UP000272401}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TG22168 {ECO:0000313|EMBL:RSQ49839.1,
RC   ECO:0000313|Proteomes:UP000272401}, and TG31299
RC   {ECO:0000313|EMBL:RSP76616.1, ECO:0000313|Proteomes:UP000269597};
RA   Sahl J.W.;
RT   "GWAS and RNA-Seq identify cryptic mechanisms of antimicrobial resistance
RT   in Acinetobacter baumannii.";
RL   Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
RN   [19] {ECO:0000313|EMBL:RTB85817.1, ECO:0000313|Proteomes:UP000277944}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R348 {ECO:0000313|EMBL:RTB85817.1,
RC   ECO:0000313|Proteomes:UP000277944};
RA   D'Souza R., Fouts D., Singh I., Nguyen K.;
RL   Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
RN   [20] {ECO:0000313|EMBL:TPU61657.1, ECO:0000313|Proteomes:UP000315888}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MRSN14237 {ECO:0000313|EMBL:TPU61657.1,
RC   ECO:0000313|Proteomes:UP000315888};
RA   Mcgann P., Snesrud E., Galac M.R.;
RT   "A Diverse Panel of Clinical Acinetobacter baumannii for Research Use.";
RL   Submitted (JUN-2019) to the EMBL/GenBank/DDBJ databases.
RN   [21] {ECO:0000313|EMBL:MQZ66891.1, ECO:0000313|Proteomes:UP000420346}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AMA26 {ECO:0000313|EMBL:MQZ66891.1,
RC   ECO:0000313|Proteomes:UP000420346};
RA   Maria R.S., Adams M.D.;
RT   "Distinct mechanisms of dissemination of NDM-1 metallo-beta-betalactamase
RT   in Acinetobacter species spp. in Argentina.";
RL   Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
RN   [22] {ECO:0000313|EMBL:MQR48113.1, ECO:0000313|Proteomes:UP000461234}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ABS103 {ECO:0000313|EMBL:MQR48113.1,
RC   ECO:0000313|Proteomes:UP000461234};
RA   Douraghi M., Aris P., Kenyon J., Hamidian M.;
RT   "Genetic environment of the oxa23 gene and comparative analysis of
RT   carbapenem resistant Acinetobacter baumannii isolates belonging to global
RT   clone 1, lineage 2 recovered in a burns hospital outbreak in 2012-2013.";
RL   Submitted (OCT-2019) to the EMBL/GenBank/DDBJ databases.
RN   [23] {ECO:0000313|EMBL:MVM92566.1, ECO:0000313|Proteomes:UP000439424}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ac576 {ECO:0000313|EMBL:MVM92566.1,
RC   ECO:0000313|Proteomes:UP000439424};
RA   Fedrigo N.H., Cerdeira L., Fuga B., Marini P.V.B., Shinohara D.R.,
RA   Carrara-Marroni F.E., Lincopan N., Tognim M.C.B.;
RT   "Multidrug-resistant Acinetobacter baumannii moving toward extensively
RT   drug-resistant over fifteen years in South of Brazil.";
RL   Submitted (NOV-2019) to the EMBL/GenBank/DDBJ databases.
RN   [24] {ECO:0000313|EMBL:MYM79056.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DMS06669 {ECO:0000313|EMBL:MYM79056.1};
RA   Nguyen S.-T.;
RL   Submitted (DEC-2019) to the EMBL/GenBank/DDBJ databases.
RN   [25] {ECO:0000313|EMBL:NDW41392.1, ECO:0000313|Proteomes:UP000470018}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SP816 {ECO:0000313|EMBL:NDW41392.1,
RC   ECO:0000313|Proteomes:UP000470018};
RA   Veeraraghavan B., Mathur P., Vijayakumar S., Vasudevan K., Lincy M.,
RA   Kirubananthan A.;
RT   "Whole genome shot-gun sequencing of clinical Carbapenem resistant A.
RT   baumannii.";
RL   Submitted (FEB-2020) to the EMBL/GenBank/DDBJ databases.
RN   [26] {ECO:0000313|EMBL:MBD0218758.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=A86 {ECO:0000313|EMBL:MBD0218758.1};
RA   Abouelfetouh A., Mattock J., Turner D., Li E., Evans B.A.;
RT   "Diversity of carbapenem-resistant Acinetobacter baumannii and
RT   bacteriophage-mediated spread of the Oxa23 carbapenemase.";
RL   Submitted (AUG-2020) to the EMBL/GenBank/DDBJ databases.
RN   [27] {ECO:0000313|EMBL:QPF12406.1, ECO:0000313|Proteomes:UP000594659}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Res13-Abat-PEA21-P4-01-A {ECO:0000313|EMBL:QPF12406.1,
RC   ECO:0000313|Proteomes:UP000594659};
RA   Poulin-Laprade D., Brouard J.-S., Gagnon N., Turcotte A., Langlois A.,
RA   Matte J.J., Carrillo C.D., Zaheer R., McAllister T., Topp E., Talbot G.;
RT   "Resistance determinants and their genetic context in bacteria from a
RT   longitudinal study of pigs reared under conventional and antibiotic-free
RT   husbandry practices.";
RL   Submitted (SEP-2020) to the EMBL/GenBank/DDBJ databases.
RN   [28] {ECO:0000313|EMBL:MBP4960678.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=E314 {ECO:0000313|EMBL:MBP4960678.1};
RA   Frenk S., Rakovitsky N.;
RT   "Epidemiology and genetic characterization of 247 CRAB isolated from
RT   infections.";
RL   Submitted (DEC-2020) to the EMBL/GenBank/DDBJ databases.
RN   [29] {ECO:0000313|EMBL:MDK4883330.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CPO519 {ECO:0000313|EMBL:MDK4883330.1};
RA   Macesic N.;
RT   "Genomic dissection of endemic carbapenem resistance: metallo-beta-
RT   lactamase gene dissemination through clonal, plasmid and integron transfer
RT   pathways.";
RL   Submitted (JAN-2023) to the EMBL/GenBank/DDBJ databases.
RN   [30] {ECO:0000313|EMBL:EMN1070674.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=2021GN-00227 {ECO:0000313|EMBL:EKU3567577.1};
RG   Clinical and Environmental Microbiology Branch: Whole genome sequencing antimicrobial resistance pathogens in the healthcare setting;
RL   Submitted (FEB-2024) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Removes the N-terminal methionine from nascent proteins. The
CC       N-terminal methionine is often cleaved when the second residue in the
CC       primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser,
CC       Thr, or Val). Requires deformylation of the N(alpha)-formylated
CC       initiator methionine before it can be hydrolyzed.
CC       {ECO:0000256|ARBA:ARBA00002521, ECO:0000256|HAMAP-Rule:MF_01974}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of N-terminal amino acids, preferentially methionine,
CC         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;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01974};
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01974};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01974};
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01974};
CC       Note=Binds 2 divalent metal cations per subunit. Has a high-affinity
CC       and a low affinity metal-binding site. The true nature of the
CC       physiological cofactor is under debate. The enzyme is active with
CC       cobalt, zinc, manganese or divalent iron ions. Most likely, methionine
CC       aminopeptidases function as mononuclear Fe(2+)-metalloproteases under
CC       physiological conditions, and the catalytically relevant metal-binding
CC       site has been assigned to the histidine-containing high-affinity site.
CC       {ECO:0000256|HAMAP-Rule:MF_01974};
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-Rule:MF_01974}.
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DR   EMBL; CP008706; AKA30982.1; -; Genomic_DNA.
DR   EMBL; CP018664; APP29388.1; -; Genomic_DNA.
DR   EMBL; LN997846; CUW35909.1; -; Genomic_DNA.
DR   EMBL; ABFEVW020000005; EKU3567577.1; -; Genomic_DNA.
DR   EMBL; ABFEVW030000005; EMN1070674.1; -; Genomic_DNA.
DR   EMBL; LLFO01000047; KQD54506.1; -; Genomic_DNA.
DR   EMBL; LRDT01000044; KZA12740.1; -; Genomic_DNA.
DR   EMBL; JACSVK010000003; MBD0218758.1; -; Genomic_DNA.
DR   EMBL; JAEHMK010000019; MBP4960678.1; -; Genomic_DNA.
DR   EMBL; JARTMM010000087; MDK4883330.1; -; Genomic_DNA.
DR   EMBL; WIOC01000002; MQR48113.1; -; Genomic_DNA.
DR   EMBL; VYTH01000001; MQZ66891.1; -; Genomic_DNA.
DR   EMBL; WPIP01000105; MVM92566.1; -; Genomic_DNA.
DR   EMBL; WWCH01000001; MYM79056.1; -; Genomic_DNA.
DR   EMBL; JAAGTY010000009; NDW41392.1; -; Genomic_DNA.
DR   EMBL; LYKI01000023; OIG72371.1; -; Genomic_DNA.
DR   EMBL; NGEL01000129; OTM85450.1; -; Genomic_DNA.
DR   EMBL; NGKM01000001; OWK68248.1; -; Genomic_DNA.
DR   EMBL; PHJU02000014; PQL84274.1; -; Genomic_DNA.
DR   EMBL; NEPB01000008; PRN35987.1; -; Genomic_DNA.
DR   EMBL; QKWF01000036; PZM18289.1; -; Genomic_DNA.
DR   EMBL; CP062919; QPF12406.1; -; Genomic_DNA.
DR   EMBL; RFBY01000023; RSP76616.1; -; Genomic_DNA.
DR   EMBL; RFCO01000002; RSQ49839.1; -; Genomic_DNA.
DR   EMBL; RWXH01000089; RTB85817.1; -; Genomic_DNA.
DR   EMBL; UFDJ01000008; SSI43005.1; -; Genomic_DNA.
DR   EMBL; UFMQ01000008; SST23566.1; -; Genomic_DNA.
DR   EMBL; VHGY01000042; TPU61657.1; -; Genomic_DNA.
DR   RefSeq; WP_001089491.1; NZ_WYAT01000001.1.
DR   PDB; 6MRF; X-ray; 1.65 A; A=12-272.
DR   PDBsum; 6MRF; -.
DR   STRING; 1096995.BJAB07104_02683; -.
DR   GeneID; 66396496; -.
DR   KEGG; abw:BL01_08915; -.
DR   PATRIC; fig|470.1288.peg.1761; -.
DR   eggNOG; COG0024; Bacteria.
DR   OMA; FYGDHAY; -.
DR   OrthoDB; 9802055at2; -.
DR   Proteomes; UP000032746; Chromosome.
DR   Proteomes; UP000051023; Unassembled WGS sequence.
DR   Proteomes; UP000066661; Chromosome I.
DR   Proteomes; UP000072389; Chromosome.
DR   Proteomes; UP000076296; Unassembled WGS sequence.
DR   Proteomes; UP000179937; Unassembled WGS sequence.
DR   Proteomes; UP000194699; Unassembled WGS sequence.
DR   Proteomes; UP000197394; Unassembled WGS sequence.
DR   Proteomes; UP000233757; Unassembled WGS sequence.
DR   Proteomes; UP000237823; Unassembled WGS sequence.
DR   Proteomes; UP000248662; Unassembled WGS sequence.
DR   Proteomes; UP000252694; Unassembled WGS sequence.
DR   Proteomes; UP000262697; Unassembled WGS sequence.
DR   Proteomes; UP000269597; Unassembled WGS sequence.
DR   Proteomes; UP000272401; Unassembled WGS sequence.
DR   Proteomes; UP000277944; Unassembled WGS sequence.
DR   Proteomes; UP000315888; Unassembled WGS sequence.
DR   Proteomes; UP000420346; Unassembled WGS sequence.
DR   Proteomes; UP000439424; Unassembled WGS sequence.
DR   Proteomes; UP000461234; Unassembled WGS sequence.
DR   Proteomes; UP000470018; Unassembled WGS sequence.
DR   Proteomes; UP000480763; Unassembled WGS sequence.
DR   Proteomes; UP000594659; Chromosome.
DR   Proteomes; UP000634608; Unassembled WGS sequence.
DR   Proteomes; UP000673677; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0004239; F:initiator methionyl aminopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0070006; F:metalloaminopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046914; F:transition metal ion binding; IEA:UniProt.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd01086; MetAP1; 1.
DR   Gene3D; 3.90.230.10; Creatinase/methionine aminopeptidase superfamily; 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   NCBIfam; TIGR00500; met_pdase_I; 1.
DR   PANTHER; PTHR43330; METHIONINE AMINOPEPTIDASE; 1.
DR   PANTHER; PTHR43330:SF8; METHIONINE AMINOPEPTIDASE 1D, MITOCHONDRIAL; 1.
DR   Pfam; PF00557; Peptidase_M24; 1.
DR   PRINTS; PR00599; MAPEPTIDASE.
DR   SUPFAM; SSF55920; Creatinase/aminopeptidase; 1.
DR   PROSITE; PS00680; MAP_1; 1.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:6MRF};
KW   Aminopeptidase {ECO:0000256|HAMAP-Rule:MF_01974,
KW   ECO:0000256|RuleBase:RU003653};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01974, 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, ECO:0000256|RuleBase:RU003653}.
FT   DOMAIN          19..256
FT                   /note="Peptidase M24"
FT                   /evidence="ECO:0000259|Pfam:PF00557"
FT   BINDING         92
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01974"
FT   BINDING         110
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01974"
FT   BINDING         121
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01974"
FT   BINDING         121
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01974"
FT   BINDING         185
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01974"
FT   BINDING         192
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01974"
FT   BINDING         218
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01974"
FT   BINDING         249
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01974"
FT   BINDING         249
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule: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
//