ID   V5VCW7_ACIBA            Unreviewed;       275 AA.
AC   V5VCW7;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   13-APR-2016, entry version 25.
DE   RecName: Full=Methionine aminopeptidase {ECO:0000256|HAMAP-Rule:MF_01974};
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};
DE   AltName: Full=Peptidase M {ECO:0000256|HAMAP-Rule:MF_01974};
GN   Name=map3 {ECO:0000313|EMBL:CRL95227.1};
GN   Synonyms=map {ECO:0000256|HAMAP-Rule:MF_01974,
GN   ECO:0000313|EMBL:BAP65968.1}, map1 {ECO:0000313|EMBL:AKA30982.1};
GN   ORFNames=AB895_0353 {ECO:0000313|EMBL:KMV05062.1}, AB987_2690
GN   {ECO:0000313|EMBL:KMV27219.1}, AB988_0028
GN   {ECO:0000313|EMBL:KMV10717.1}, ABCIP7010_2514
GN   {ECO:0000313|EMBL:CRL95227.1}, ABR2090_1208
GN   {ECO:0000313|EMBL:CRX64132.1}, ABR2091_2512
GN   {ECO:0000313|EMBL:CUW35909.1}, ABUW_1234
GN   {ECO:0000313|EMBL:AKA30982.1}, AC795_04265
GN   {ECO:0000313|EMBL:KPA50106.1}, ACX60_05910
GN   {ECO:0000313|EMBL:AKQ26271.1}, AN415_01306
GN   {ECO:0000313|EMBL:ALJ87216.1}, APB90_02655
GN   {ECO:0000313|EMBL:KQE81176.1}, APC61_11100
GN   {ECO:0000313|EMBL:KRI70112.1}, APC83_11450
GN   {ECO:0000313|EMBL:KRJ33643.1}, APD06_11055
GN   {ECO:0000313|EMBL:KQD20501.1}, AQ482_07905
GN   {ECO:0000313|EMBL:KQK46469.1}, ASZ75_13910
GN   {ECO:0000313|EMBL:KRT99055.1}, ASZ76_13115
GN   {ECO:0000313|EMBL:KRT99951.1}, IOMTU433_1184
GN   {ECO:0000313|EMBL:BAP65968.1}, IX87_07995
GN   {ECO:0000313|EMBL:AIL78573.1}, KBNAB1_1198
GN   {ECO:0000313|EMBL:ALX98757.1}, RU84_05625
GN   {ECO:0000313|EMBL:AJB66358.1}, TE32_05490
GN   {ECO:0000313|EMBL:AKJ45008.1}, UO01_16465
GN   {ECO:0000313|EMBL:KKZ44945.1};
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:KRT99055.1, ECO:0000313|Proteomes:UP000051533, ECO:0000313|Proteomes:UP000053448}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MRSN5540 {ECO:0000313|EMBL:KRT99055.1,
RC   ECO:0000313|Proteomes:UP000053448}, and MRSN6269
RC   {ECO:0000313|EMBL:KRT99951.1, ECO:0000313|Proteomes:UP000051533};
RX   PubMed=23812239; DOI=10.1093/infdis/jit293;
RA   Lesho E., Yoon E.J., McGann P., Snesrud E., Kwak Y., Milillo M.,
RA   Onmus-Leone F., Preston L., St Clair K., Nikolich M., Viscount H.,
RA   Wortmann G., Zapor M., Grillot-Courvalin C., Courvalin P.,
RA   Clifford R., Waterman P.E.;
RT   "Emergence of colistin-resistance in extremely drug-resistant
RT   Acinetobacter baumannii containing a novel pmrCAB operon during
RT   colistin therapy of wound infections.";
RL   J. Infect. Dis. 208:1142-1151(2013).
RN   [2] {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   [3] {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   [4] {ECO:0000313|EMBL:AJB66358.1, ECO:0000313|Proteomes:UP000031136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=6200 {ECO:0000313|EMBL:AJB66358.1,
RC   ECO:0000313|Proteomes:UP000031136};
RA   McCorrison J., Sanka R., Adams M., Brinkac L., Sutton G., Bonomo R.,
RA   Rojas L.;
RL   Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
RN   [5] {ECO:0000313|EMBL:ALJ87216.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=D36 {ECO:0000313|EMBL:ALJ87216.1};
RX   PubMed=26679588;
RA   Hamidian M., Hawkey J., Holt K.E., Hall R.M.;
RT   "Genome Sequence of Acinetobacter baumannii Strain D36, an Antibiotic-
RT   Resistant Isolate from Lineage 2 of Global Clone 1.";
RL   Genome Announc. 3:e01478-15(2015).
RN   [6] {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   [7] {ECO:0000313|EMBL:KQK46469.1, ECO:0000313|Proteomes:UP000053083}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ab18 {ECO:0000313|EMBL:KQK46469.1,
RC   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   [8] {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   [9] {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   [10] {ECO:0000313|EMBL:KKZ44945.1, ECO:0000313|Proteomes:UP000034216}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=161/07 {ECO:0000313|EMBL:KKZ44945.1,
RC   ECO:0000313|Proteomes:UP000034216};
RA   Sahl J., Zarrilli R.;
RT   "Genomic epidemiology of Acinetobacter baumannii strains assigned to
RT   the ST25 clonal lineage; the evolution of a globally relevant clone.";
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
RN   [11] {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   [12] {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   [13] {ECO:0000313|EMBL:CRL95227.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CIP70.10 {ECO:0000313|EMBL:CRL95227.1}, and R2090
RC   {ECO:0000313|EMBL:CRX64132.1};
RA   Wibberg Daniel;
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
RN   [14] {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   [15] {ECO:0000313|EMBL:KMV27219.1, ECO:0000313|Proteomes:UP000036137}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B8300 {ECO:0000313|EMBL:KMV27219.1,
RC   ECO:0000313|Proteomes:UP000036137};
RA   Vijaykumar S., Balaji V., Biswas I.;
RT   "Complete genome sequence of Acinetobacter baumannii strain B8300 that
RT   displays high twitching motility.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN   [16] {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   [17] {ECO:0000313|EMBL:KPA50106.1, ECO:0000313|Proteomes:UP000049182}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TCM331 {ECO:0000313|EMBL:KPA50106.1,
RC   ECO:0000313|Proteomes:UP000049182};
RA   Chen Y.;
RT   "Draft genome sequence of Acinetobacter baumannii TCM331 in China.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN   [18] {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   [19] {ECO:0000313|Proteomes:UP000050849, ECO:0000313|Proteomes:UP000051044, ECO:0000313|Proteomes:UP000051259}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ABBL018 {ECO:0000313|EMBL:KRI70112.1,
RC   ECO:0000313|Proteomes:UP000050849}, ABBL038
RC   {ECO:0000313|EMBL:KRJ33643.1, ECO:0000313|Proteomes:UP000051259},
RC   ABBL059 {ECO:0000313|EMBL:KQD20501.1,
RC   ECO:0000313|Proteomes:UP000051322}, and ABBL094
RC   {ECO:0000313|EMBL:KQE81176.1, ECO:0000313|Proteomes:UP000051044};
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   [20] {ECO:0000313|EMBL:KRT99055.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=MRSN5540 {ECO:0000313|EMBL:KRT99055.1}, and MRSN6269
RC   {ECO:0000313|EMBL:KRT99951.1};
RA   Zhang Y., Guo Z.;
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
RN   [21] {ECO:0000313|EMBL:CUW35909.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=R2091 {ECO:0000313|EMBL:CUW35909.1};
RA   Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN   [22] {ECO:0000313|EMBL:ALX98757.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=KBN10P02143 {ECO:0000313|EMBL:ALX98757.1};
RA   Lee Y.-W., Lee W.-K.;
RT   "Complete genome sequence of multidrug-resistant Acinetobacter
RT   baumannii strain KBN10P02143 isolated from Korea.";
RL   Submitted (JAN-2016) 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: Release of N-terminal amino acids,
CC       preferentially methionine, from peptides and arylamides.
CC       {ECO:0000256|HAMAP-Rule:MF_01974}.
CC   -!- COFACTOR:
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01974};
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01974};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01974};
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01974};
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};
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; CP010397; AJB66358.1; -; 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; CP012952; ALJ87216.1; -; Genomic_DNA.
DR   EMBL; CP013924; ALX98757.1; -; Genomic_DNA.
DR   EMBL; AP014649; BAP65968.1; -; Genomic_DNA.
DR   EMBL; CVLF01000087; CQR89265.1; -; Genomic_DNA.
DR   EMBL; LN865143; CRL95227.1; -; Genomic_DNA.
DR   EMBL; LN868200; CRX64132.1; -; Genomic_DNA.
DR   EMBL; LN997846; CUW35909.1; -; Genomic_DNA.
DR   EMBL; JZCA01000048; KKZ44945.1; -; Genomic_DNA.
DR   EMBL; LFYZ01000001; KMV05062.1; -; Genomic_DNA.
DR   EMBL; LFYW01000001; KMV10717.1; -; Genomic_DNA.
DR   EMBL; LFYY01000001; KMV27219.1; -; Genomic_DNA.
DR   EMBL; LGHQ01000006; KPA50106.1; -; Genomic_DNA.
DR   EMBL; LLFE01000041; KQD20501.1; -; Genomic_DNA.
DR   EMBL; LLGV01000105; KQE81176.1; -; Genomic_DNA.
DR   EMBL; LMBN01000110; KQK46469.1; -; Genomic_DNA.
DR   EMBL; LLCY01000039; KRI70112.1; -; Genomic_DNA.
DR   EMBL; LLDS01000073; KRJ33643.1; -; Genomic_DNA.
DR   EMBL; LNCW01000033; KRT99055.1; -; Genomic_DNA.
DR   EMBL; LNCX01000028; KRT99951.1; -; Genomic_DNA.
DR   RefSeq; WP_001089491.1; NZ_LORJ01000003.1.
DR   STRING; 575584.HMPREF0010_02353; -.
DR   EnsemblBacteria; AIA51932; AIA51932; BL01_08915.
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; BAP65968; BAP65968; IOMTU433_1184.
DR   EnsemblBacteria; KGF60633; KGF60633; LH92_12295.
DR   EnsemblBacteria; KHX40556; KHX40556; RQ85_11030.
DR   EnsemblBacteria; KJC70013; KJC70013; SG91_03630.
DR   EnsemblBacteria; KJC74977; KJC74977; SG99_01140.
DR   EnsemblBacteria; KJC77760; KJC77760; SG88_01280.
DR   EnsemblBacteria; KJC81102; KJC81102; SG93_04835.
DR   EnsemblBacteria; KJC85046; KJC85046; SG98_02525.
DR   EnsemblBacteria; KJC89333; KJC89333; SG95_02540.
DR   EnsemblBacteria; KJC93105; KJC93105; SF14_02540.
DR   EnsemblBacteria; KJC96364; KJC96364; SG97_01880.
DR   EnsemblBacteria; KJD00834; KJD00834; SG96_02155.
DR   EnsemblBacteria; KJD03626; KJD03626; SG89_03285.
DR   EnsemblBacteria; KJD07383; KJD07383; SG92_03085.
DR   EnsemblBacteria; KJD12477; KJD12477; SG94_02405.
DR   EnsemblBacteria; KJD14335; KJD14335; SG90_03075.
DR   EnsemblBacteria; KJG94182; KJG94182; QU96_1174.
DR   EnsemblBacteria; KJX73186; KJX73186; WH42_07110.
DR   EnsemblBacteria; KKA96472; KKA96472; VM83_11790.
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; UP000031136; Chromosome.
DR   Proteomes; UP000031644; Chromosome.
DR   Proteomes; UP000032746; Chromosome.
DR   Proteomes; UP000034216; Unassembled WGS sequence.
DR   Proteomes; UP000035522; Chromosome.
DR   Proteomes; UP000036024; Chromosome.
DR   Proteomes; UP000036137; Unassembled WGS sequence.
DR   Proteomes; UP000036720; Unassembled WGS sequence.
DR   Proteomes; UP000037552; Unassembled WGS sequence.
DR   Proteomes; UP000049182; Unassembled WGS sequence.
DR   Proteomes; UP000050849; Unassembled WGS sequence.
DR   Proteomes; UP000051044; Unassembled WGS sequence.
DR   Proteomes; UP000051259; Unassembled WGS sequence.
DR   Proteomes; UP000051322; Unassembled WGS sequence.
DR   Proteomes; UP000051533; Unassembled WGS sequence.
DR   Proteomes; UP000053083; Unassembled WGS sequence.
DR   Proteomes; UP000053448; 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:0000313|EMBL:KQD20501.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000028932,
KW   ECO:0000313|Proteomes:UP000031136, ECO:0000313|Proteomes:UP000031644,
KW   ECO:0000313|Proteomes:UP000032746};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01974,
KW   ECO:0000256|RuleBase:RU003652, ECO:0000313|EMBL:KQD20501.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01974};
KW   Protease {ECO:0000256|HAMAP-Rule:MF_01974}.
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
//