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Database: UniProt
Entry: K0AZ77_CLOA9
LinkDB: K0AZ77_CLOA9
Original site: K0AZ77_CLOA9 
ID   K0AZ77_CLOA9            Unreviewed;       476 AA.
AC   K0AZ77;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   22-NOV-2017, entry version 26.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   Name=apeA {ECO:0000313|EMBL:AFS78000.1};
GN   OrderedLocusNames=Curi_c09840 {ECO:0000313|EMBL:AFS78000.1};
OS   Clostridium acidurici (strain ATCC 7906 / DSM 604 / BCRC 14475 / CIP
OS   104303 / NCIMB 10678 / 9a) (Gottschalkia acidurici).
OC   Bacteria; Firmicutes; Tissierellia; Tissierellales; Gottschalkiaceae;
OC   Gottschalkia.
OX   NCBI_TaxID=1128398 {ECO:0000313|EMBL:AFS78000.1, ECO:0000313|Proteomes:UP000006094};
RN   [1] {ECO:0000313|EMBL:AFS78000.1, ECO:0000313|Proteomes:UP000006094}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 7906 / CIP 104303 / DSM 604 / NCIMB 10678 / BCRC 14475 /
RC   NCCB 46094 / 9a {ECO:0000313|Proteomes:UP000006094};
RX   PubMed=23240052; DOI=10.1371/journal.pone.0051662;
RA   Hartwich K., Poehlein A., Daniel R.;
RT   "The purine-utilizing bacterium Clostridium acidurici 9a: a genome-
RT   guided metabolic reconsideration.";
RL   PLoS ONE 7:E51662-E51662(2012).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU004387};
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|RuleBase:RU004386}.
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DR   EMBL; CP003326; AFS78000.1; -; Genomic_DNA.
DR   MEROPS; M18.004; -.
DR   EnsemblBacteria; AFS78000; AFS78000; Curi_c09840.
DR   KEGG; cad:Curi_c09840; -.
DR   PATRIC; fig|1128398.3.peg.984; -.
DR   OMA; YQWVTIP; -.
DR   OrthoDB; POG091H01QL; -.
DR   Proteomes; UP000006094; Chromosome.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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|RuleBase:RU004386,
KW   ECO:0000313|EMBL:AFS78000.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006094};
KW   Hydrolase {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:AFS78000.1};
KW   Metal-binding {ECO:0000256|RuleBase:RU004386};
KW   Metalloprotease {ECO:0000256|RuleBase:RU004386};
KW   Protease {ECO:0000256|RuleBase:RU004386};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006094};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   476 AA;  53054 MW;  8917AD6BFE20EC9D CRC64;
     MIKKTDGKAL QEKLTHKWRN VWEELEDSQL DIVKNMGEEY KIFLDKGKTE REVVSNIVKM
     AEENGYVSLE SIIKKKIKVV PGTKIYANNK DKSVAMFIIG KEKIEDGMNI IASHVDSPRI
     DLKQFPLYEQ DGLGLLKTHY YGGVKKYQWV TLPLSLHGVV IKSNGEKIHI TIGEDEKDPV
     FFITDLLPHL AKDQMEKKMG EGITGEGLNI LFGSIPYNDS EISEKVKLNI LNILNEKYGI
     MEQDFTTAEF EIVPAGKARD VGIDRSMIGG YGQDDRVCVY TSLKSMLDTS TPNRTAVALF
     SDKEEVGSLG NTGMESRFFE NAVAEIINLT EESYNELKLK RALANSKVLS ADTVGAFDPN
     YPDVLDKRNS PFLGKGICLV KYTGARGKSS TNDANSEYIS EIRKIFNNNN IIWQMGELGK
     VDQGGGGTIA YILANYGAEV VDCGVSLLSV HGPFEISSKA DIYMTYEGYK AFYKEA
//
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