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Database: UniProt
Entry: T0NAG9_9CLOT
LinkDB: T0NAG9_9CLOT
Original site: T0NAG9_9CLOT 
ID   T0NAG9_9CLOT            Unreviewed;       433 AA.
AC   T0NAG9;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   22-NOV-2017, entry version 22.
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=M918_10705 {ECO:0000313|EMBL:EQB87135.1};
OS   Clostridium sp. BL8.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1354301 {ECO:0000313|EMBL:EQB87135.1, ECO:0000313|Proteomes:UP000015873};
RN   [1] {ECO:0000313|EMBL:EQB87135.1, ECO:0000313|Proteomes:UP000015873}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BL8 {ECO:0000313|EMBL:EQB87135.1,
RC   ECO:0000313|Proteomes:UP000015873};
RX   PubMed=25076986; DOI=10.1186/1757-4749-6-30;
RA   Marathe N.P., Shetty S.A., Lanjekar V.B., Rasane M.H., Ranade D.R.,
RA   Shouche Y.S.;
RT   "Genome sequencing of multidrug resistant novel Clostridium sp. BL8
RT   reveals its potential for pathogenicity.";
RL   Gut Pathog 6:30-30(2014).
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:EQB87135.1}.
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DR   EMBL; AUPA01000202; EQB87135.1; -; Genomic_DNA.
DR   RefSeq; WP_021284388.1; NZ_AUPA01000202.1.
DR   EnsemblBacteria; EQB87135; EQB87135; M918_10705.
DR   PATRIC; fig|1354301.3.peg.3280; -.
DR   OrthoDB; POG091H01I4; -.
DR   Proteomes; UP000015873; 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   HAMAP; MF_00467; Aminopeptidase_M18_2; 1.
DR   InterPro; IPR022984; M18_aminopeptidase_2.
DR   InterPro; IPR001948; Peptidase_M18.
DR   InterPro; IPR023367; Peptidase_M42_dom2.
DR   PANTHER; PTHR28570; PTHR28570; 1.
DR   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
DR   SUPFAM; SSF101821; SSF101821; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|HAMAP-Rule:MF_00467,
KW   ECO:0000256|RuleBase:RU004386, ECO:0000313|EMBL:EQB87135.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000015873};
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:UP000015873};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00467, ECO:0000256|RuleBase:RU004386}.
FT   METAL        84     84       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
FT   METAL       161    161       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
FT   METAL       409    409       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
SQ   SEQUENCE   433 AA;  48192 MW;  D30F98A89020E2F3 CRC64;
     MTKELQFAQE LIDFLYDSPT AFHAVENLRK ELSNTGFEEL KEEDKWNLKK GGRYFTTKNN
     SALVAFVVGN GEIENHGFKI VGAHTDSPTF RIKPACEMVV EGTYVRLNTE VYGGPILNTW
     LDRPLSVAGR VVIKGENILY PKNVLVNIKK PILIIPNLAI HMNREVNKGV ELNAQRDTLP
     LLSLVNEELE KGNYLLNAIA KELGVDAKEI IDFDLFLYEF EKGSIIGLND EFISAGRLDD
     LQMVHAGIAA LKDAPVTEGT NVMVCFDNEE IGSSTKQGAD SEMLANILER IALAFGKERE
     DFFRALSRSF LISGDNAHAV HPNNPDKHDP TNRPVINKGP VIKINANFAY TTDSDSSAVY
     EELCKAAQVP YQKFVNRSDV RGGSTIGPIS STHLNIRSID IGNPTLAMHS IRELAGVMDH
     TYVMKSYLEF YKL
//
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