UniProt: G0AM68

Database: UniProt
Entry: G0AM68_BORBD

LinkDB:  G0AM68_BORBD 
Original site:  G0AM68_BORBD

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Ontology (4)   
   GO (4)   
Gene (1)   
   KEGG GENES (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (3)   
   InterPro (2)   
   Pfam (1)   
Literature (2)   
   PubMed (2)   
All databases (12)   

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ID   G0AM68_BORBD            Unreviewed;       423 AA.
AC   G0AM68;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   24-JAN-2024, entry version 58.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   OrderedLocusNames=BbiDN127_0637 {ECO:0000313|EMBL:AEL18794.1};
OS   Borrelia bissettiae (strain DSM 17990 / CIP 109136 / DN127) (Borreliella
OS   bissettiae).
OC   Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Borreliaceae;
OC   Borreliella.
OX   NCBI_TaxID=521010 {ECO:0000313|EMBL:AEL18794.1, ECO:0000313|Proteomes:UP000001634};
RN   [1] {ECO:0000313|Proteomes:UP000001634}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17990 / CIP 109136 / DN127
RC   {ECO:0000313|Proteomes:UP000001634};
RA   Mongodin E.F., Casjens S.R., Fraser-Liggett C.M., Qiu W.-G., Dunn J.J.,
RA   Luft B.J., Schutzer S.E.;
RT   "Complete genome sequence of Borrelia bissettii strain DN127.";
RL   Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DN127;
RA   Mongodin E.F., Casjens S.R., Fraser-Liggett C.M., Qiu W.-G., Dunn J.J.,
RA   Luft B.J., Schutzer S.E.;
RL   Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:AEL18794.1, ECO:0000313|Proteomes:UP000001634}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17990 / CIP 109136 / DN127
RC   {ECO:0000313|Proteomes:UP000001634};
RX   PubMed=22207749; DOI=10.1128/JB.06263-11;
RA   Schutzer S.E., Fraser-Liggett C.M., Qiu W.G., Kraiczy P., Mongodin E.F.,
RA   Dunn J.J., Luft B.J., Casjens S.R.;
RT   "Whole-Genome Sequences of Borrelia bissettii, Borrelia valaisiana, and
RT   Borrelia spielmanii.";
RL   J. Bacteriol. 194:545-546(2012).
RN   [4] {ECO:0000313|EMBL:AEL18794.1, ECO:0000313|Proteomes:UP000001634}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17990 / CIP 109136 / DN127
RC   {ECO:0000313|Proteomes:UP000001634};
RX   PubMed=26813420; DOI=10.1099/ijsem.0.000897;
RA   Margos G., Lane R.S., Fedorova N., Koloczek J., Piesman J., Hojgaard A.,
RA   Sing A., Fingerle V.;
RT   "Borrelia bissettiae sp. nov. and Borrelia californiensis sp. nov. prevail
RT   in diverse enzootic transmission cycles.";
RL   Int. J. Syst. Evol. Microbiol. 66:1447-1452(2016).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947,
CC         ECO:0000256|RuleBase:RU004387};
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|ARBA:ARBA00008290, ECO:0000256|RuleBase:RU004386}.
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DR   EMBL; CP002746; AEL18794.1; -; Genomic_DNA.
DR   RefSeq; WP_014023842.1; NC_015921.1.
DR   AlphaFoldDB; G0AM68; -.
DR   STRING; 521010.BbiDN127_0637; -.
DR   KEGG; bbs:BbiDN127_0637; -.
DR   eggNOG; COG1362; Bacteria.
DR   HOGENOM; CLU_019532_2_0_12; -.
DR   Proteomes; UP000001634; 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   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.30.250.10; Aminopeptidase i, Domain 2; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR001948; Peptidase_M18.
DR   InterPro; IPR023358; Peptidase_M18_dom2.
DR   PANTHER; PTHR28570; ASPARTYL AMINOPEPTIDASE; 1.
DR   PANTHER; PTHR28570:SF3; ASPARTYL AMINOPEPTIDASE; 1.
DR   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
DR   SUPFAM; SSF101821; Aminopeptidase/glucanase lid domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW   ECO:0000256|RuleBase:RU004386};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU004386};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU004386};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW   ECO:0000256|RuleBase:RU004386};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU004386};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   423 AA;  47602 MW;  01642E5ECEE2FD33 CRC64;
     MVHDETLEPK FFQSLLDNSP TPYHLVNYIE EKLINYFNAQ QLKLEEKWKI ETGSYYIKKE
     GTSLIAFNID VEKKYEPFLI ATAHTDSPGL KLKIDATEKT SGVFYNHIEV YGSPIISTWI
     DRDLSLAGIV YFKKNEHIDS KLINIENIGI IPNLAIHLNR QINEGFKYNA HDNLTIISST
     KKPIKDNILE QLGIEHKNFL SCDLIFTESQ PSKIIGTEGE FLASKNLDNK SGCHAIMNSY
     VHTNNDKNKI AVFFDNEEIG SLTSRGADSN FLSEVLERID LALNLTREEH LIKTSKSFNI
     SIDSVHGIHP GYTSKHDPNY QATLGRGMVV KNSANFRYAT TSTGFAKLKN LAIKNNIKIQ
     EIIMKANVPS GTTIGPISNA RTGIETIDIG TPMWAMHSLR ETVSIADHIE AIKLLRAFFE
     KGI
//

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