ID K0UTC7_MYCVA Unreviewed; 420 AA.
AC K0UTC7;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 28-MAR-2018, entry version 35.
DE RecName: Full=Probable M18 family aminopeptidase 2 {ECO:0000256|HAMAP-Rule:MF_00467};
DE EC=3.4.11.- {ECO:0000256|HAMAP-Rule:MF_00467};
GN Name=apeB {ECO:0000256|HAMAP-Rule:MF_00467};
GN ORFNames=MVAC_16073 {ECO:0000313|EMBL:EJZ08275.1};
OS Mycobacterium vaccae ATCC 25954.
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1194972 {ECO:0000313|EMBL:EJZ08275.1, ECO:0000313|Proteomes:UP000006072};
RN [1] {ECO:0000313|EMBL:EJZ08275.1, ECO:0000313|Proteomes:UP000006072}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25954 {ECO:0000313|EMBL:EJZ08275.1,
RC ECO:0000313|Proteomes:UP000006072};
RX PubMed=23105074; DOI=10.1128/JB.01462-12;
RA Ho Y.S., Adroub S.A., Abadi M., Al Alwan B., Alkhateeb R., Gao G.,
RA Ragab A., Ali S., van Soolingen D., Bitter W., Pain A., Abdallah A.M.;
RT "Complete Genome Sequence of Mycobacterium vaccae Type Strain ATCC
RT 25954.";
RL J. Bacteriol. 194:6339-6340(2012).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_00467, ECO:0000256|RuleBase:RU004387};
CC -!- SIMILARITY: Belongs to the peptidase M18 family.
CC {ECO:0000256|HAMAP-Rule:MF_00467, ECO:0000256|RuleBase:RU004386}.
CC -!- CAUTION: The sequence shown here is derived from an
CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC preliminary data. {ECO:0000313|EMBL:EJZ08275.1}.
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DR EMBL; ALQA01000033; EJZ08275.1; -; Genomic_DNA.
DR RefSeq; WP_003930440.1; NZ_JH814690.1.
DR MEROPS; M18.002; -.
DR EnsemblBacteria; EJZ08275; EJZ08275; MVAC_16073.
DR PATRIC; fig|1194972.3.peg.3211; -.
DR OrthoDB; POG091H01I4; -.
DR Proteomes; UP000006072; Unassembled WGS sequence.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR Gene3D; 2.30.250.10; -; 1.
DR HAMAP; MF_00467; Aminopeptidase_M18_2; 1.
DR InterPro; IPR022984; M18_aminopeptidase_2.
DR InterPro; IPR001948; Peptidase_M18.
DR InterPro; IPR023358; Peptidase_M18_dom2.
DR PANTHER; PTHR28570; PTHR28570; 1.
DR Pfam; PF02127; Peptidase_M18; 1.
DR PRINTS; PR00932; AMINO1PTASE.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|HAMAP-Rule:MF_00467,
KW ECO:0000256|RuleBase:RU004386, ECO:0000313|EMBL:EJZ08275.1};
KW Complete proteome {ECO:0000313|Proteomes:UP000006072};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_00467,
KW ECO:0000256|RuleBase:RU004386};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00467,
KW ECO:0000256|RuleBase:RU004386};
KW Metalloprotease {ECO:0000256|HAMAP-Rule:MF_00467,
KW ECO:0000256|RuleBase:RU004386};
KW Protease {ECO:0000256|HAMAP-Rule:MF_00467,
KW ECO:0000256|RuleBase:RU004386};
KW Reference proteome {ECO:0000313|Proteomes:UP000006072};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_00467, ECO:0000256|RuleBase:RU004386}.
FT METAL 77 77 Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
FT METAL 151 151 Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
FT METAL 395 395 Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
SQ SEQUENCE 420 AA; 44949 MW; 969B333CFC351436 CRC64;
MPASPHGLCE FIDASPSPFH VCRTAAERLR TAGFTEVSES DPWSGAGDFF TVRAGSLIAW
RTDEDDRALP FRIVGAHTDS PNLRVKQHPD RYVSGWQVVA LQPYGGAWLN SWLDRDLGIS
GRLSVRDGNA IRHTLVRVDE PILRVPQLAI HLSEDRKGVE LNPQRHVNAV WGVGDGPRSF
LGFVADEAGV DEDDVLGFDL MTHDLTPSRL AGVDGELVSA PRLDNQATCY AGLEAFLAAG
ADAGVLPVLV LFDHEEVGSQ SDHGAQSELL LTVLERITLA AGGSREDFLR RLPTSMVASG
DMAHATHPNY PERHEPGHLI EVNAGPVLKV QPNLRYATDG RTAAAFALAC AQAGVNLQRY
EHRADLPCGS TIGPMTAANT GIPTVDVGAA QLAMHSAREV MGAADVADYS AALQAFLSPA
//
