ID   V5VCW7_ACIBA            Unreviewed;       275 AA.
AC   V5VCW7;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   27-MAY-2015, entry version 15.
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=map1 {ECO:0000313|EMBL:AKA30982.1};
GN   Synonyms=map {ECO:0000256|HAMAP-Rule:MF_01974,
GN   ECO:0000313|EMBL:BAP65968.1};
GN   ORFNames=ABUW_1234 {ECO:0000313|EMBL:AKA30982.1}, BL01_08915
GN   {ECO:0000313|EMBL:AIA51932.1}, IOMTU433_1184
GN   {ECO:0000313|EMBL:BAP65968.1}, IX87_07995
GN   {ECO:0000313|EMBL:AIL78573.1}, LH92_12295
GN   {ECO:0000313|EMBL:KGF60633.1}, QU96_1174
GN   {ECO:0000313|EMBL:KJG94182.1}, RQ24_04615
GN   {ECO:0000313|EMBL:KJG81168.1}, RQ37_03770
GN   {ECO:0000313|EMBL:KJE63625.1}, RQ42_05190
GN   {ECO:0000313|EMBL:KJE61738.1}, RQ49_01840
GN   {ECO:0000313|EMBL:KJF15001.1}, RQ64_07755
GN   {ECO:0000313|EMBL:KJF11281.1}, RQ85_11030
GN   {ECO:0000313|EMBL:KHX40556.1}, RQ98_01200
GN   {ECO:0000313|EMBL:KJE73081.1}, RR20_01165
GN   {ECO:0000313|EMBL:KJE68647.1}, RR21_08695
GN   {ECO:0000313|EMBL:KJF02887.1}, RR22_11905
GN   {ECO:0000313|EMBL:KJF05880.1}, RR27_02775
GN   {ECO:0000313|EMBL:KJE74574.1}, RU84_05625
GN   {ECO:0000313|EMBL:AJB66358.1}, SF14_02540
GN   {ECO:0000313|EMBL:KJC93105.1}, SG88_01280
GN   {ECO:0000313|EMBL:KJC77760.1}, SG89_03285
GN   {ECO:0000313|EMBL:KJD03626.1}, SG90_03075
GN   {ECO:0000313|EMBL:KJD14335.1}, SG91_03630
GN   {ECO:0000313|EMBL:KJC70013.1}, SG92_03085
GN   {ECO:0000313|EMBL:KJD07383.1}, SG93_04835
GN   {ECO:0000313|EMBL:KJC81102.1}, SG94_02405
GN   {ECO:0000313|EMBL:KJD12477.1}, SG95_02540
GN   {ECO:0000313|EMBL:KJC89333.1}, SG96_02155
GN   {ECO:0000313|EMBL:KJD00834.1}, SG97_01880
GN   {ECO:0000313|EMBL:KJC96364.1}, SG98_02525
GN   {ECO:0000313|EMBL:KJC85046.1}, SG99_01140
GN   {ECO:0000313|EMBL:KJC74977.1};
OS   Acinetobacter baumannii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Acinetobacter;
OC   Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=470 {ECO:0000313|EMBL:KHX40556.1, ECO:0000313|Proteomes:UP000032746};
RN   [1] {ECO:0000313|EMBL:AIL78573.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=AB030 {ECO:0000313|EMBL:AIL78573.1};
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:KGF60633.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=MAR002 {ECO:0000313|EMBL:KGF60633.1};
RA   Alvarez-Fraga L., Rumbo-Feal S., Merino M., Bou G., Poza M.;
RT   "Complete genome of a biofilm superproducing strain of Acinetobacter
RT   baumannii.";
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:BAP65968.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=IOMTU 433 {ECO:0000313|EMBL:BAP65968.1};
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}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=6200 {ECO:0000313|EMBL:AJB66358.1};
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:KJC70013.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ORAB01 {ECO:0000313|EMBL:KJD14335.1}, ORAB02
RC   {ECO:0000313|EMBL:KJD07383.1}, ORAB03 {ECO:0000313|EMBL:KJD12477.1},
RC   ORAB08 {ECO:0000313|EMBL:KJC93105.1}, ORAB09
RC   {ECO:0000313|EMBL:KJC89333.1}, ORAB10 {ECO:0000313|EMBL:KJD00834.1},
RC   ORAB13 {ECO:0000313|EMBL:KJC81102.1}, ORAB14
RC   {ECO:0000313|EMBL:KJC85046.1}, ORAB15 {ECO:0000313|EMBL:KJC74977.1},
RC   ORAB16 {ECO:0000313|EMBL:KJD03626.1}, ORAB17
RC   {ECO:0000313|EMBL:KJC77760.1}, ORAB18 {ECO:0000313|EMBL:KJC70013.1},
RC   and ORAB19 {ECO:0000313|EMBL:KJC96364.1};
RA   Adams M., Brinkac L., Sanka R., Wright M., Sutton G., Bonomo R.,
RA   Buser G., Beldavs Z., Pfeiffer C., Cassidy M., Cunningham M.,
RA   Tierheimer J., Rudin S.;
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
RN   [6] {ECO:0000313|EMBL:KHX40556.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=UH175_674 {ECO:0000313|EMBL:KJE74574.1}, UH17_151
RC   {ECO:0000313|EMBL:KJG81168.1}, UH326_445
RC   {ECO:0000313|EMBL:KHX40556.1}, UH381_484
RC   {ECO:0000313|EMBL:KJE73081.1}, UH475_361
RC   {ECO:0000313|EMBL:KJF11281.1}, UH514_289
RC   {ECO:0000313|EMBL:KJF15001.1}, UH592_583
RC   {ECO:0000313|EMBL:KJE68647.1}, UH592_595
RC   {ECO:0000313|EMBL:KJF02887.1}, UH592_599
RC   {ECO:0000313|EMBL:KJF05880.1}, UH66_253 {ECO:0000313|EMBL:KJE63625.1},
RC   and UH66_271 {ECO:0000313|EMBL:KJE61738.1};
RA   Adams M., Brinkac L., Sanka R., Wright M., Sutton G., Bonomo R.,
RA   Jacobs M.;
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
RN   [7] {ECO:0000313|EMBL:KJG94182.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=WA2859 {ECO:0000313|EMBL:KJG94182.1};
RA   Wang C., Geng X., Chen G., Zhao Q., Zhou L.;
RT   "Whole-Genome Sequence Analysis of the Acinetobacter baumannii
RT   Clinical Isolate WA2859.";
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN   [8] {ECO:0000313|EMBL:AKA30982.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=AB5075-UW {ECO:0000313|EMBL:AKA30982.1};
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   [9] {ECO:0000313|EMBL:AIA51932.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=AC29 {ECO:0000313|EMBL:AIA51932.1};
RA   Lean S.S., Suhaili Z., Yeo C.C., Thong K.-L.;
RT   "Comparative genomics of polymyxin-resistant and susceptible
RT   Acinetobacter baumannii isolated from the same patient.";
RL   Submitted (APR-2015) 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; CP007535; AIA51932.1; -; Genomic_DNA.
DR   EMBL; CP009257; AIL78573.1; -; Genomic_DNA.
DR   EMBL; CP010397; AJB66358.1; -; Genomic_DNA.
DR   EMBL; CP008706; AKA30982.1; -; Genomic_DNA.
DR   EMBL; AP014649; BAP65968.1; -; Genomic_DNA.
DR   EMBL; JRHB01000001; KGF60633.1; -; Genomic_DNA.
DR   EMBL; JWUX02000289; KHX40556.1; -; Genomic_DNA.
DR   EMBL; JZCE01000005; KJC70013.1; -; Genomic_DNA.
DR   EMBL; JZCH01000002; KJC74977.1; -; Genomic_DNA.
DR   EMBL; JZCF01000002; KJC77760.1; -; Genomic_DNA.
DR   EMBL; JZCJ01000008; KJC81102.1; -; Genomic_DNA.
DR   EMBL; JZCI01000004; KJC85046.1; -; Genomic_DNA.
DR   EMBL; JZCL01000004; KJC89333.1; -; Genomic_DNA.
DR   EMBL; JZCM01000004; KJC93105.1; -; Genomic_DNA.
DR   EMBL; JZCD01000003; KJC96364.1; -; Genomic_DNA.
DR   EMBL; JZCK01000004; KJD00834.1; -; Genomic_DNA.
DR   EMBL; JZCG01000005; KJD03626.1; -; Genomic_DNA.
DR   EMBL; JZCO01000004; KJD07383.1; -; Genomic_DNA.
DR   EMBL; JZCN01000004; KJD12477.1; -; Genomic_DNA.
DR   EMBL; JZCP01000005; KJD14335.1; -; Genomic_DNA.
DR   EMBL; JZIX01000006; KJE61738.1; -; Genomic_DNA.
DR   EMBL; JZIZ01000005; KJE63625.1; -; Genomic_DNA.
DR   EMBL; JZIY01000003; KJE68647.1; -; Genomic_DNA.
DR   EMBL; JZJA01000003; KJE73081.1; -; Genomic_DNA.
DR   EMBL; JZJB01000006; KJE74574.1; -; Genomic_DNA.
DR   EMBL; JZJE01000024; KJF02887.1; -; Genomic_DNA.
DR   EMBL; JZJD01000056; KJF05880.1; -; Genomic_DNA.
DR   EMBL; JZJF01000018; KJF11281.1; -; Genomic_DNA.
DR   EMBL; JZJG01000005; KJF15001.1; -; Genomic_DNA.
DR   EMBL; JWXB02000010; KJG81168.1; -; Genomic_DNA.
DR   EMBL; JXOC01000001; KJG94182.1; -; Genomic_DNA.
DR   RefSeq; WP_001089491.1; NZ_KN708634.1.
DR   ProteinModelPortal; V5VCW7; -.
DR   EnsemblBacteria; AHB90780; AHB90780; P795_5275.
DR   EnsemblBacteria; AIA51932; AIA51932; BL01_08915.
DR   EnsemblBacteria; AIL76380; AIL76380; IX88_14615.
DR   EnsemblBacteria; AIL78573; AIL78573; IX87_07995.
DR   EnsemblBacteria; AIS07185; AIS07185; LX00_12565.
DR   EnsemblBacteria; AJB66358; AJB66358; RU84_05625.
DR   EnsemblBacteria; KEF45144; KEF45144; FL75_13250.
DR   EnsemblBacteria; KEF47159; KEF47159; FL80_16995.
DR   EnsemblBacteria; KFB64928; KFB64928; GQ86_18650.
DR   EnsemblBacteria; KFG14104; KFG14104; ABBL099_00550.
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; KHV25527; KHV25527; RW63_04620.
DR   EnsemblBacteria; KHV28669; KHV28669; RW57_01585.
DR   EnsemblBacteria; KHV33176; KHV33176; RW60_02595.
DR   EnsemblBacteria; KHV33855; KHV33855; RW58_12575.
DR   EnsemblBacteria; KHV39540; KHV39540; RW62_03690.
DR   KEGG; abaz:P795_5275; -.
DR   KO; K01265; -.
DR   Proteomes; UP000027328; Chromosome.
DR   Proteomes; UP000028932; Chromosome.
DR   Proteomes; UP000031136; Chromosome.
DR   Proteomes; UP000031644; Chromosome.
DR   Proteomes; UP000032746; Chromosome.
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:KHX40556.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000027328,
KW   ECO:0000313|Proteomes:UP000028932};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01974,
KW   ECO:0000256|RuleBase:RU003652};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01974};
KW   Protease {ECO:0000256|HAMAP-Rule:MF_01974}.
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
//