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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 //