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}. 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; 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 //