ID   V5VCW7_ACIBA            Unreviewed;       275 AA.
AC   V5VCW7;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   26-NOV-2014, entry version 9.
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=map {ECO:0000256|HAMAP-Rule:MF_01974,
GN   ECO:0000313|EMBL:BAP65968.1};
GN   ORFNames=ABBL099_00550 {ECO:0000313|EMBL:KFG14104.1}, BL01_08915
GN   {ECO:0000313|EMBL:AIA51932.1}, FL75_13250
GN   {ECO:0000313|EMBL:KEF45144.1}, FL80_16995
GN   {ECO:0000313|EMBL:KEF47159.1}, GQ86_18650
GN   {ECO:0000313|EMBL:KFB64928.1}, IOMTU433_1184
GN   {ECO:0000313|EMBL:BAP65968.1}, IX87_07995
GN   {ECO:0000313|EMBL:AIL78573.1}, IX88_14615
GN   {ECO:0000313|EMBL:AIL76380.1}, LX00_12565
GN   {ECO:0000313|EMBL:AIS07185.1}, P795_5275
GN   {ECO:0000313|EMBL:AHB90780.1};
OS   Acinetobacter baumannii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Acinetobacter;
OC   Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=470 {ECO:0000313|Proteomes:UP000018698};
RN   [1] {ECO:0000313|Proteomes:UP000018698}
RP   NUCLEOTIDE SEQUENCE.
RA   Wang X., Zhang Z., Hao Q., Gu W., Liu X., Guo B., Wu J., Yu J.,
RA   Jing H., Xiao J., Yang W.;
RT   "Complete Genome Sequence of Acinetobacter baumannii ZW85-1.";
RL   Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AHB90780.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ZW85-1 {ECO:0000313|EMBL:AHB90780.1};
RX   PubMed=24459253;
RA   Wang X., Zhang Z., Hao Q., Wu J., Xiao J., Jing H.;
RT   "Complete Genome Sequence of Acinetobacter baumannii ZW85-1.";
RL   Genome Announc. 2:e01083-13(2014).
RN   [3] {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 (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:KFB64928.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=TCM206 {ECO:0000313|EMBL:KFB64928.1};
RA   Chen Y.;
RT   "Draft genome sequence of Acinetobacter baumannii TCM206 in China.";
RL   Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
RN   [5] {ECO:0000313|EMBL:KEF45144.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BR097 {ECO:0000313|EMBL:KEF45144.1}, and BU310
RC   {ECO:0000313|EMBL:KEF47159.1};
RA   Golemboski D., Eardly B.D.;
RT   "Draft genome sequence of respiratory and urinary tract isolates of
RT   Acinetobacter baumannii from the same patient.";
RL   Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
RN   [6] {ECO:0000313|EMBL:KFG14104.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ABBL099 {ECO:0000313|EMBL:KFG14104.1};
RA   Ozer E.A., Fitzpatrick M.A., Hauser A.R.;
RT   "Draft Genome Sequence of Acinetobacter baumannii Strain ABBL099.";
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
RN   [7] {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   [8] {ECO:0000313|EMBL:AIL76380.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=AB031 {ECO:0000313|EMBL:AIL76380.1};
RA   Loewen P.C., Kumar A.;
RT   "Genome sequence of Acinetobacter baumannii AB031.";
RL   Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
RN   [9] {ECO:0000313|EMBL:AIS07185.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=AbH12O-A2 {ECO:0000313|EMBL:AIS07185.1};
RA   Merino M., Alvarez-Fraga L., Rumbo-Feal S., Aransay A.M., Lavin J.L.,
RA   Bou G., Poza M.;
RT   "Complete genome sequence of the multiresistant Acinetobacter
RT   baumannii AbH12O-A2 strain isolated during a large outbreak in
RT   Spain.";
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN   [10] {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.
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       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; CP006768; AHB90780.1; -; Genomic_DNA.
DR   EMBL; CP007535; AIA51932.1; -; Genomic_DNA.
DR   EMBL; CP009256; AIL76380.1; -; Genomic_DNA.
DR   EMBL; CP009257; AIL78573.1; -; Genomic_DNA.
DR   EMBL; CP009534; AIS07185.1; -; Genomic_DNA.
DR   EMBL; AP014649; BAP65968.1; -; Genomic_DNA.
DR   EMBL; JNFY01000006; KEF45144.1; -; Genomic_DNA.
DR   EMBL; JNFZ01000009; KEF47159.1; -; Genomic_DNA.
DR   EMBL; JMRW01000008; KFB64928.1; -; Genomic_DNA.
DR   EMBL; JPDG01000023; KFG14104.1; -; Genomic_DNA.
DR   RefSeq; YP_008889913.1; NC_023028.1.
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:AHB90780.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000018698};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018698}.
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
//