ID   V5VCW7_ACIBA            Unreviewed;       275 AA.
AC   V5VCW7;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   22-JUL-2015, entry version 17.
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}, MRSN16875_00815
GN   {ECO:0000313|EMBL:KKD29809.1}, RQ24_04615
GN   {ECO:0000313|EMBL:KJG81168.1}, RQ85_11030
GN   {ECO:0000313|EMBL:KHX40556.1}, RU84_05625
GN   {ECO:0000313|EMBL:AJB66358.1}, VM83_11790
GN   {ECO:0000313|EMBL:KKA96472.1}, WH42_07110
GN   {ECO:0000313|EMBL:KJX73186.1};
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};
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:KKD29809.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=MRSN16875 {ECO:0000313|EMBL:KKD29809.1};
RX   PubMed=25824815;
RA   Jones C.L., Clancy M., Honnold C., Singh S., Snesrud E.,
RA   Onmus-Leone F., McGann P., Ong A., Kwak Y., Waterman P.,
RA   Zurawski D.V., Clifford R.J., Lesho E.;
RT   "A Fatal Outbreak of an Emerging Clone of Extensively Drug-Resistant
RT   Acinetobacter baumannii with Enhanced Virulence.";
RL   Clin. Infect. Dis. 0:0-0(2015).
RN   [6] {ECO:0000313|EMBL:KHX40556.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=UH17_151 {ECO:0000313|EMBL:KJG81168.1}, 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 (FEB-2015) to the EMBL/GenBank/DDBJ databases.
RN   [7] {ECO:0000313|EMBL:KJX73186.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Ab5 {ECO:0000313|EMBL:KJX73186.1};
RA   Opazo A.F., Lopes B.S., Gonzalez-Rocha G., Amyes S.G.;
RT   "Draft genome sequence of the Acinetobacter baumannii multidrug-
RT   resistant strain Ab5 from Chile.";
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN   [8] {ECO:0000313|EMBL:KKA96472.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=718532 {ECO:0000313|EMBL:KKA96472.1};
RA   Yim A.K., Leung A.K., Yu A.C.;
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN   [9] {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   [10] {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.
RN   [11] {ECO:0000313|EMBL:KKA96472.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=718532 {ECO:0000313|EMBL:KKA96472.1};
RA   Tsui S.K., Ip M., Chan T.-F., Kwok J.S.;
RT   "Draft Genome of a Resistant Acinetobacter baumannii Strain from a
RT   Patient in Hong Kong, China.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN   [12] {ECO:0000313|EMBL:CQR67878.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CHI-32 {ECO:0000313|EMBL:CQR89265.1}, CHI-34
RC   {ECO:0000313|EMBL:CRF38470.1}, and CHI-45-1
RC   {ECO:0000313|EMBL:CQR67878.1};
RA   Jones S Lim;
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; CVLE01000052; CQR67878.1; -; Genomic_DNA.
DR   EMBL; CVLF01000087; CQR89265.1; -; Genomic_DNA.
DR   EMBL; CVLD01000073; CRF38470.1; -; Genomic_DNA.
DR   EMBL; JRHB01000001; KGF60633.1; -; Genomic_DNA.
DR   EMBL; JWUX02000289; KHX40556.1; -; Genomic_DNA.
DR   EMBL; JWXB02000010; KJG81168.1; -; Genomic_DNA.
DR   EMBL; LANH01000043; KJX73186.1; -; Genomic_DNA.
DR   EMBL; JZUF01000007; KKA96472.1; -; Genomic_DNA.
DR   EMBL; LAZK01000001; KKD29809.1; -; Genomic_DNA.
DR   RefSeq; WP_001089491.1; NZ_LAZK01000001.1.
DR   STRING; 575584.HMPREF0010_02353; -.
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; abaa:IX88_14615; -.
DR   KEGG; abau:IX87_07995; -.
DR   KEGG; abk:LX00_12565; -.
DR   KEGG; abw:BL01_08915; -.
DR   KO; K01265; -.
DR   Proteomes; UP000027328; Chromosome.
DR   Proteomes; UP000028932; Chromosome.
DR   Proteomes; UP000031136; Chromosome.
DR   Proteomes; UP000031644; Chromosome.
DR   Proteomes; UP000032746; Chromosome.
DR   Proteomes; UP000033509; 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: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
//