ID V5VCW7_ACIBA Unreviewed; 275 AA. AC V5VCW7; DT 19-FEB-2014, integrated into UniProtKB/TrEMBL. DT 19-FEB-2014, sequence version 1. DT 08-JUN-2016, entry version 27. DE RecName: Full=Methionine aminopeptidase {ECO:0000256|HAMAP-Rule:MF_01974, ECO:0000256|RuleBase:RU003653}; 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, ECO:0000256|RuleBase:RU003653}; 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 Synonyms=map1 {ECO:0000313|EMBL:AKA30982.1}; GN ORFNames=AB895_0353 {ECO:0000313|EMBL:KMV05062.1}, AB988_0028 GN {ECO:0000313|EMBL:KMV10717.1}, ABUW_1234 GN {ECO:0000313|EMBL:AKA30982.1}, ACX60_05910 GN {ECO:0000313|EMBL:AKQ26271.1}, APB90_02655 GN {ECO:0000313|EMBL:KQE81176.1}, APC61_11100 GN {ECO:0000313|EMBL:KRI70112.1}, APC83_11450 GN {ECO:0000313|EMBL:KRJ33643.1}, APD06_11055 GN {ECO:0000313|EMBL:KQD20501.1}, AQ482_07905 GN {ECO:0000313|EMBL:KQK46469.1}, ASZ75_13910 GN {ECO:0000313|EMBL:KRT99055.1}, ASZ76_13115 GN {ECO:0000313|EMBL:KRT99951.1}, AZE33_14285 GN {ECO:0000313|EMBL:AMN02327.1}, IOMTU433_1184 GN {ECO:0000313|EMBL:BAP65968.1}, IX87_07995 GN {ECO:0000313|EMBL:AIL78573.1}, TE32_05490 GN {ECO:0000313|EMBL:AKJ45008.1}, UO01_16465 GN {ECO:0000313|EMBL:KKZ44945.1}; OS Acinetobacter baumannii. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter; OC Acinetobacter calcoaceticus/baumannii complex. OX NCBI_TaxID=470 {ECO:0000313|EMBL:KQD20501.1, ECO:0000313|Proteomes:UP000051322}; RN [1] {ECO:0000313|EMBL:KRT99055.1, ECO:0000313|Proteomes:UP000051533, ECO:0000313|Proteomes:UP000053448} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MRSN5540 {ECO:0000313|EMBL:KRT99055.1, RC ECO:0000313|Proteomes:UP000053448}, and MRSN6269 RC {ECO:0000313|EMBL:KRT99951.1, ECO:0000313|Proteomes:UP000051533}; RX PubMed=23812239; DOI=10.1093/infdis/jit293; RA Lesho E., Yoon E.J., McGann P., Snesrud E., Kwak Y., Milillo M., RA Onmus-Leone F., Preston L., St Clair K., Nikolich M., Viscount H., RA Wortmann G., Zapor M., Grillot-Courvalin C., Courvalin P., RA Clifford R., Waterman P.E.; RT "Emergence of colistin-resistance in extremely drug-resistant RT Acinetobacter baumannii containing a novel pmrCAB operon during RT colistin therapy of wound infections."; RL J. Infect. Dis. 208:1142-1151(2013). RN [2] {ECO:0000313|EMBL:AIL78573.1, ECO:0000313|Proteomes:UP000028932} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AB030 {ECO:0000313|EMBL:AIL78573.1}, and AB30 RC {ECO:0000313|Proteomes:UP000028932}; 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 [3] {ECO:0000313|EMBL:BAP65968.1, ECO:0000313|Proteomes:UP000031644} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IOMTU 433 {ECO:0000313|EMBL:BAP65968.1, RC ECO:0000313|Proteomes:UP000031644}; 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:AKA30982.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=AB5075-UW {ECO:0000313|EMBL:AKA30982.1}; RX PubMed=25845845; RA Gallagher L.A., Ramage E., Weiss E.J., Radey M., Hayden H.S., RA Held K.G., Huse H.K., Zurawski D.V., Brittnacher M.J., Manoil C.; RT "Resources for Genetic and Genomic Analysis of Emerging Pathogen RT Acinetobacter baumannii."; RL J. Bacteriol. 197:2027-2035(2015). RN [5] {ECO:0000313|EMBL:KQK46469.1, ECO:0000313|Proteomes:UP000053083} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ab18 {ECO:0000313|EMBL:KQK46469.1, RC ECO:0000313|Proteomes:UP000053083}; RA Leite G., Oliveira M.S., Perdigao-Neto L.V., Rocha C.K., Guimaraes T., RA Rizek C.F., Levin A.S., Costa S.F.; RT "Antimicrobial combinations against pan-resistant Acinetobacter RT baumannii isolates with different mechanisms of resistance."; RL PLoS ONE 0:0-0(2015). RN [6] {ECO:0000313|EMBL:AKQ26271.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 17978-mff {ECO:0000313|EMBL:AKQ26271.1}; RX PubMed=26170289; DOI=10.1073/pnas.1502966112; RA Weber B.S., Ly P.M., Irwin J.N., Pukatzki S., Feldman M.F.; RT "A multidrug resistance plasmid contains the molecular switch for type RT VI secretion in Acinetobacter baumannii."; RL Proc. Natl. Acad. Sci. U.S.A. 112:9442-9447(2015). RN [7] {ECO:0000313|EMBL:AKJ45008.1, ECO:0000313|Proteomes:UP000035522} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=XH386 {ECO:0000313|EMBL:AKJ45008.1, RC ECO:0000313|Proteomes:UP000035522}; RA Fang Y., Hua X., Feng Y., Lil X., Weng J., Ruan Z., Shang S., Yu Y.; RT "Complete genome sequence of a multi-drug resistant ST208 RT Acinetobacter baumannii."; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. RN [8] {ECO:0000313|EMBL:KKZ44945.1, ECO:0000313|Proteomes:UP000034216} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=161/07 {ECO:0000313|EMBL:KKZ44945.1, RC ECO:0000313|Proteomes:UP000034216}; RA Sahl J., Zarrilli R.; RT "Genomic epidemiology of Acinetobacter baumannii strains assigned to RT the ST25 clonal lineage; the evolution of a globally relevant clone."; RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases. RN [9] {ECO:0000313|Proteomes:UP000032746} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AB5075-UW {ECO:0000313|Proteomes:UP000032746}; 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:CQR89265.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CHI-32 {ECO:0000313|EMBL:CQR89265.1}; RA Jones S Lim; RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases. RN [11] {ECO:0000313|Proteomes:UP000036024} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 17978-mff {ECO:0000313|Proteomes:UP000036024}; RA Weber B.S., Ly P.M., Irwin J.N., Pukatzki S., Feldman M.F.; RT "A multidrug resistance plasmid contains the molecular switch for type RT VI secretion in Acinetobacter baumannii."; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. RN [12] {ECO:0000313|EMBL:KMV05062.1, ECO:0000313|Proteomes:UP000036720} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B8342 {ECO:0000313|EMBL:KMV05062.1, RC ECO:0000313|Proteomes:UP000036720}; RA Vijaykumar S., Balaji V., Biswas I.; RT "Complete genome sequence of Acinetobacter baumannii strain B8342, a RT motility positive clinical isolate."; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. RN [13] {ECO:0000313|EMBL:KMV10717.1, ECO:0000313|Proteomes:UP000037552} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SP1917 {ECO:0000313|EMBL:KMV10717.1, RC ECO:0000313|Proteomes:UP000037552}; RA Vijaykumar S., Balaji V., Biswas I.; RT "Draft genome sequences of two multidrug resistant Acinetobacter RT baumannii isolates from Southern India."; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. RN [14] {ECO:0000313|Proteomes:UP000050849, ECO:0000313|Proteomes:UP000051044, ECO:0000313|Proteomes:UP000051259} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ABBL018 {ECO:0000313|EMBL:KRI70112.1, RC ECO:0000313|Proteomes:UP000050849}, ABBL038 RC {ECO:0000313|EMBL:KRJ33643.1, ECO:0000313|Proteomes:UP000051259}, RC ABBL059 {ECO:0000313|EMBL:KQD20501.1, RC ECO:0000313|Proteomes:UP000051322}, and ABBL094 RC {ECO:0000313|EMBL:KQE81176.1, ECO:0000313|Proteomes:UP000051044}; RA Ozer E.A., Fitzpatrick M.A., Hauser A.R.; RT "The utility of whole genome sequencing in characterizing RT Acinetobacter epidemiology and analyzing hospital outbreaks."; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [15] {ECO:0000313|EMBL:KRT99055.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MRSN5540 {ECO:0000313|EMBL:KRT99055.1}, and MRSN6269 RC {ECO:0000313|EMBL:KRT99951.1}; RA Zhang Y., Guo Z.; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. RN [16] {ECO:0000313|EMBL:AMN02327.1, ECO:0000313|Proteomes:UP000070590} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=XH858 {ECO:0000313|EMBL:AMN02327.1, RC ECO:0000313|Proteomes:UP000070590}; RA Feng Y., Hua X., Yu Y.; RT "Complete genome of Acinetobacter baumannii str. XH858."; RL Submitted (FEB-2016) 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). {ECO:0000256|SAAS:SAAS00578544}. CC -!- CATALYTIC ACTIVITY: Release of N-terminal amino acids, CC preferentially methionine, from peptides and arylamides. CC {ECO:0000256|HAMAP-Rule:MF_01974, ECO:0000256|RuleBase:RU003653}. CC -!- COFACTOR: CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01974, ECO:0000256|RuleBase:RU003653}; CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01974, ECO:0000256|RuleBase:RU003653}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01974, ECO:0000256|RuleBase:RU003653}; CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01974, ECO:0000256|RuleBase:RU003653}; 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, ECO:0000256|RuleBase:RU003653}; CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-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; CP009257; AIL78573.1; -; Genomic_DNA. DR EMBL; CP008706; AKA30982.1; -; Genomic_DNA. DR EMBL; CP010779; AKJ45008.1; -; Genomic_DNA. DR EMBL; CP012004; AKQ26271.1; -; Genomic_DNA. DR EMBL; CP014528; AMN02327.1; -; Genomic_DNA. DR EMBL; AP014649; BAP65968.1; -; Genomic_DNA. DR EMBL; CVLF01000087; CQR89265.1; -; Genomic_DNA. DR EMBL; JZCA01000048; KKZ44945.1; -; Genomic_DNA. DR EMBL; LFYZ01000001; KMV05062.1; -; Genomic_DNA. DR EMBL; LFYW01000001; KMV10717.1; -; Genomic_DNA. DR EMBL; LLFE01000041; KQD20501.1; -; Genomic_DNA. DR EMBL; LLGV01000105; KQE81176.1; -; Genomic_DNA. DR EMBL; LMBN01000110; KQK46469.1; -; Genomic_DNA. DR EMBL; LLCY01000039; KRI70112.1; -; Genomic_DNA. DR EMBL; LLDS01000073; KRJ33643.1; -; Genomic_DNA. DR EMBL; LNCW01000033; KRT99055.1; -; Genomic_DNA. DR EMBL; LNCX01000028; KRT99951.1; -; Genomic_DNA. DR RefSeq; WP_001089491.1; NZ_LRMK01000083.1. DR STRING; 575584.HMPREF0010_02353; -. DR EnsemblBacteria; AIL78573; AIL78573; IX87_07995. DR EnsemblBacteria; AJB66358; AJB66358; RU84_05625. DR EnsemblBacteria; AKA30982; AKA30982; ABUW_1234. DR EnsemblBacteria; AKJ45008; AKJ45008; TE32_05490. DR EnsemblBacteria; AKQ26271; AKQ26271; ACX60_05910. DR EnsemblBacteria; BAP65968; BAP65968; IOMTU433_1184. DR EnsemblBacteria; CQR67878; CQR67878; CQR67878. DR EnsemblBacteria; CRF38470; CRF38470; CRF38470. 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; KHV28669; KHV28669; RW57_01585. DR EnsemblBacteria; KHV33176; KHV33176; RW60_02595. DR EnsemblBacteria; KHV33855; KHV33855; RW58_12575. DR EnsemblBacteria; KHX40556; KHX40556; RQ85_11030. DR EnsemblBacteria; KHY10257; KHY10257; RQ47_01330. DR EnsemblBacteria; KIA15515; KIA15515; RP89_09635. DR EnsemblBacteria; KJE61738; KJE61738; RQ42_05190. DR EnsemblBacteria; KJE63625; KJE63625; RQ37_03770. DR EnsemblBacteria; KJE68647; KJE68647; RR20_01165. DR EnsemblBacteria; KJE73081; KJE73081; RQ98_01200. DR EnsemblBacteria; KJE74574; KJE74574; RR27_02775. DR EnsemblBacteria; KJF02887; KJF02887; RR21_08695. DR EnsemblBacteria; KJF05880; KJF05880; RR22_11905. DR EnsemblBacteria; KJF11281; KJF11281; RQ64_07755. DR EnsemblBacteria; KJF15001; KJF15001; RQ49_01840. DR EnsemblBacteria; KJG75542; KJG75542; RQ82_03725. DR EnsemblBacteria; KJG77179; KJG77179; RQ80_13680. DR EnsemblBacteria; KJG81168; KJG81168; RQ24_04615. DR EnsemblBacteria; KKA96472; KKA96472; VM83_11790. DR EnsemblBacteria; KKZ40688; KKZ40688; UN98_08720. DR EnsemblBacteria; KKZ44945; KKZ44945; UO01_16465. DR EnsemblBacteria; KMV03238; KMV03238; AB994_1981. DR EnsemblBacteria; KMV05062; KMV05062; AB895_0353. DR EnsemblBacteria; KMV10717; KMV10717; AB988_0028. DR EnsemblBacteria; KMV27219; KMV27219; AB987_2690. DR EnsemblBacteria; KOP89520; KOP89520; AKG97_01110. DR EnsemblBacteria; KPA50106; KPA50106; AC795_04265. DR KEGG; abaa:IX88_14615; -. DR KEGG; abau:IX87_07995; -. DR KEGG; abk:LX00_12565; -. DR KEGG; abw:BL01_08915; -. DR eggNOG; ENOG4105CA1; Bacteria. DR eggNOG; COG0024; LUCA. DR KO; K01265; -. DR Proteomes; UP000028932; Chromosome. DR Proteomes; UP000031644; Chromosome. DR Proteomes; UP000032746; Chromosome. DR Proteomes; UP000034216; Unassembled WGS sequence. DR Proteomes; UP000035522; Chromosome. DR Proteomes; UP000036024; Chromosome. DR Proteomes; UP000036720; Unassembled WGS sequence. DR Proteomes; UP000037552; Unassembled WGS sequence. DR Proteomes; UP000050849; Unassembled WGS sequence. DR Proteomes; UP000051044; Unassembled WGS sequence. DR Proteomes; UP000051259; Unassembled WGS sequence. DR Proteomes; UP000051322; Unassembled WGS sequence. DR Proteomes; UP000051533; Unassembled WGS sequence. DR Proteomes; UP000053083; Unassembled WGS sequence. DR Proteomes; UP000053448; Unassembled WGS sequence. DR Proteomes; UP000070590; 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:0000256|RuleBase:RU003653, ECO:0000313|EMBL:KQD20501.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000028932, KW ECO:0000313|Proteomes:UP000031644, ECO:0000313|Proteomes:UP000032746, KW ECO:0000313|Proteomes:UP000034216}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01974, KW ECO:0000256|RuleBase:RU003652, ECO:0000313|EMBL:KQD20501.1}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01974, KW ECO:0000256|RuleBase:RU003653}; KW Protease {ECO:0000256|HAMAP-Rule:MF_01974, KW ECO:0000256|RuleBase:RU003653}. FT DOMAIN 19 256 Peptidase_M24. {ECO:0000259|Pfam: FT PF00557}. 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 //