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}. 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; 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 //