GenomeNet

Database: UniProt
Entry: A0A0A0X392_9SPIO
LinkDB: A0A0A0X392_9SPIO
Original site: A0A0A0X392_9SPIO 
ID   A0A0A0X392_9SPIO        Unreviewed;       480 AA.
AC   A0A0A0X392;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   25-OCT-2017, entry version 10.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   ORFNames=JO41_03175 {ECO:0000313|EMBL:AIW88922.1};
OS   Treponema sp. OMZ 838.
OC   Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Treponema.
OX   NCBI_TaxID=1539298 {ECO:0000313|EMBL:AIW88922.1, ECO:0000313|Proteomes:UP000030314};
RN   [1] {ECO:0000313|EMBL:AIW88922.1, ECO:0000313|Proteomes:UP000030314}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OMZ 838 {ECO:0000313|EMBL:AIW88922.1,
RC   ECO:0000313|Proteomes:UP000030314};
RA   Chan Y., Ma A.P.Y., Lacap D.C., Huo Y.-B., Leung F.C., Watt R.M.;
RT   "Complete genome sequence for Treponema sp. OMZ 838 (ATCC 700772, DSM
RT   16789) isolated from a necrotizing ulcerative gingivitis lesion.";
RL   Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP009227; AIW88922.1; -; Genomic_DNA.
DR   RefSeq; WP_044013780.1; NZ_CP009227.1.
DR   EnsemblBacteria; AIW88922; AIW88922; JO41_03175.
DR   KEGG; trm:JO41_03175; -.
DR   Proteomes; UP000030314; 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   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:AIW88922.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000030314};
KW   Hydrolase {ECO:0000256|RuleBase:RU004386};
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:UP000030314};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   480 AA;  52402 MW;  7A6B2EEAA5A59FEA CRC64;
     MELTYKAKTA WENLTESELA EMQTLSQHYI SFLNIGKTER ECAAHIIRQA KEAGFKPLEE
     VIKSGKAPAG TKVYLNNKDK SVVMMVLGED IMQGMNIVGA HIDSPRLDVK QMPLYEDSNL
     VFLKTHYYGG IKKYQWTAIP LAIHGVIFTK EGKKVEICIG EDENDPVLFI NDLLIHLSKK
     QLQETLAEGI TAEQLNVLVG NMKPATPDES DDKKKDKSKE DKKGDKASPV KENILKILNQ
     KYGITEEDFR VAELEIVPAG KARNVGLDNS MIAGHGHDDR VCAYTTLKAM LEVSGTPAKT
     AVALFADKEE IGSVGNTGMT ALYFENMVAE IAALQKAPCD LGVRRAFANS CMLSADVSAG
     YDPAFTSVFE KLNSAFIGNG ICINKYTGSG GKGGSNDANA EYLQKIRHLF DTNNVVWQTA
     ELGMTDAGGG GTIAYILAKY GTEVVDCGVP VLSMHAPIEL ISKADLLMAY RAYKAFLKAH
//
DBGET integrated database retrieval system