ID   V5VCW7_ACIBA            Unreviewed;       275 AA.
AC   V5VCW7;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   01-APR-2015, entry version 13.
DE   SubName: Full=Methionine aminopeptidase {ECO:0000313|EMBL:KHV18126.1};
DE            EC=3.4.11.18 {ECO:0000313|EMBL:KHV18126.1};
GN   Name=map {ECO:0000256|HAMAP-Rule:MF_01974,
GN   ECO:0000313|EMBL:BAP65968.1};
GN   ORFNames=IOMTU433_1184 {ECO:0000313|EMBL:BAP65968.1}, LH92_12295
GN   {ECO:0000313|EMBL:KGF60633.1}, PK64_09360
GN   {ECO:0000313|EMBL:KII23988.1}, RQ85_11030
GN   {ECO:0000313|EMBL:KHX40556.1}, RW49_11850
GN   {ECO:0000313|EMBL:KHT85672.1}, RW56_05425
GN   {ECO:0000313|EMBL:KHV22247.1}, RW57_01585
GN   {ECO:0000313|EMBL:KHV28669.1}, RW58_12575
GN   {ECO:0000313|EMBL:KHV33855.1}, RW59_04665
GN   {ECO:0000313|EMBL:KHV18126.1}, RW60_02595
GN   {ECO:0000313|EMBL:KHV33176.1}, RW62_03690
GN   {ECO:0000313|EMBL:KHV39540.1}, RW63_04620
GN   {ECO:0000313|EMBL:KHV25527.1};
OS   Acinetobacter baumannii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Acinetobacter;
OC   Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=470 {ECO:0000313|EMBL:KHV18126.1};
RN   [1] {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   [2] {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   [3] {ECO:0000313|EMBL:KII23988.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=M3AC9-7 {ECO:0000313|EMBL:KII23988.1};
RA   Martinez T., Ropelewski A., Robledo I.E.;
RT   "Draft Genome Sequence of a KPC-Producing Acinetobacrter baumannii
RT   clinical isolate from Puerto Rico.";
RL   Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:KHV18126.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ABUH16665 {ECO:0000313|EMBL:KHV39540.1}, ABUH222351
RC   {ECO:0000313|EMBL:KHV25527.1}, ABUH304350
RC   {ECO:0000313|EMBL:KHV18126.1}, ABUH304352
RC   {ECO:0000313|EMBL:KHV28669.1}, ABUH404571
RC   {ECO:0000313|EMBL:KHV33855.1}, ABUH42783
RC   {ECO:0000313|EMBL:KHT85672.1}, ABUH463346
RC   {ECO:0000313|EMBL:KHV22247.1}, ABUH524354
RC   {ECO:0000313|EMBL:KHV33176.1}, and UH326_445
RC   {ECO:0000313|EMBL:KHX40556.1};
RA   Adams M., Brinkac L., Sanka R., Wright M., Sutton G., Bonomo R.,
RA   Jacobs M.;
RL   Submitted (DEC-2014) 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; AP014649; BAP65968.1; -; Genomic_DNA.
DR   EMBL; JRHB01000001; KGF60633.1; -; Genomic_DNA.
DR   EMBL; JWRU01000060; KHT85672.1; -; Genomic_DNA.
DR   EMBL; JWSF01000009; KHV18126.1; -; Genomic_DNA.
DR   EMBL; JWSE01000012; KHV22247.1; -; Genomic_DNA.
DR   EMBL; JWSG01000009; KHV25527.1; -; Genomic_DNA.
DR   EMBL; JWSH01000003; KHV28669.1; -; Genomic_DNA.
DR   EMBL; JWSI01000006; KHV33176.1; -; Genomic_DNA.
DR   EMBL; JWSJ01000043; KHV33855.1; -; Genomic_DNA.
DR   EMBL; JWSK01000009; KHV39540.1; -; Genomic_DNA.
DR   EMBL; JWUX01000292; KHX40556.1; -; Genomic_DNA.
DR   EMBL; JTEC01000012; KII23988.1; -; Genomic_DNA.
DR   RefSeq; YP_008889913.1; NC_023028.1.
DR   ProteinModelPortal; V5VCW7; -.
DR   EnsemblBacteria; AHB90780; AHB90780; P795_5275.
DR   EnsemblBacteria; AIA51932; AIA51932; BL01_08915.
DR   GeneID; 17862901; -.
DR   KEGG; abaz:P795_5275; -.
DR   KO; K01265; -.
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:KHV18126.1};
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
//