ID V5VCW7_ACIBA Unreviewed; 275 AA. AC V5VCW7; DT 19-FEB-2014, integrated into UniProtKB/TrEMBL. DT 19-FEB-2014, sequence version 1. DT 24-JUN-2015, entry version 16. 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 Synonyms=map1 {ECO:0000313|EMBL:AKA30982.1}; 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}, MRSN16897_00815 GN {ECO:0000313|EMBL:KKD20914.1}, 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:KKD20914.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MRSN16875 {ECO:0000313|EMBL:KKD29809.1}, and MRSN16897 RC {ECO:0000313|EMBL:KKD20914.1}; 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: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: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 [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}. 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; 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; LAYM01000001; KKD20914.1; -; Genomic_DNA. DR EMBL; LAZK01000001; KKD29809.1; -; Genomic_DNA. DR RefSeq; WP_001089491.1; NZ_KN708634.1. 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 //