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Database: UniProt
Entry: F8L6R9_SIMNZ
LinkDB: F8L6R9_SIMNZ
Original site: F8L6R9_SIMNZ 
ID   F8L6R9_SIMNZ            Unreviewed;       426 AA.
AC   F8L6R9;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   22-NOV-2017, entry version 43.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   Name=apeB {ECO:0000313|EMBL:CCB88417.1};
GN   OrderedLocusNames=SNE_A05400 {ECO:0000313|EMBL:CCB88417.1};
OS   Simkania negevensis (strain ATCC VR-1471 / Z).
OC   Bacteria; Chlamydiae; Parachlamydiales; Simkaniaceae; Simkania.
OX   NCBI_TaxID=331113 {ECO:0000313|EMBL:CCB88417.1, ECO:0000313|Proteomes:UP000000496};
RN   [1] {ECO:0000313|EMBL:CCB88417.1, ECO:0000313|Proteomes:UP000000496}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-1471 / Z {ECO:0000313|Proteomes:UP000000496};
RX   PubMed=21690563; DOI=10.1093/molbev/msr161;
RA   Collingro A., Tischler P., Weinmaier T., Penz T., Heinz E.,
RA   Brunham R.C., Read T.D., Bavoil P.M., Sachse K., Kahane S.,
RA   Friedman M.G., Rattei T., Myers G.S., Horn M.;
RT   "Unity in variety--the pan-genome of the chlamydiae.";
RL   Mol. Biol. Evol. 28:3253-3270(2011).
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; FR872582; CCB88417.1; -; Genomic_DNA.
DR   RefSeq; WP_013942884.1; NC_015713.1.
DR   STRING; 331113.SNE_A05400; -.
DR   MEROPS; M18.002; -.
DR   EnsemblBacteria; CCB88417; CCB88417; SNE_A05400.
DR   KEGG; sng:SNE_A05400; -.
DR   eggNOG; ENOG4105DFM; Bacteria.
DR   eggNOG; COG1362; LUCA.
DR   KO; K01267; -.
DR   OMA; CFDHEEI; -.
DR   OrthoDB; POG091H01I4; -.
DR   Proteomes; UP000000496; Chromosome gsn.131.
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:CCB88417.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000496};
KW   Hydrolase {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:CCB88417.1};
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:UP000000496};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   426 AA;  47293 MW;  DCCF9B378D839A37 CRC64;
     MNYAPLQDLI LFLQSSPTPW HAVSQIGLRL AQQDFTPLEE GEKWDLKPGE RYFVERGGSL
     CAFTLPKNTP VRSTILASHT DSPALKLKPH PLFVEEGIPF LRVESYGSPI ISTWINRDLA
     IGGRLLVGTP DGEIEEKLIY LDQTPVLIPT LAIHLDREQN DKPKPVSKQD HLCPLLGIEA
     KGKDPDSLFH DLLKPVVTDN LLGFDLYLVP CDAPRIIGQN SSLLASYRLD NLVSAHASLL
     ALLATDKIPE ETIQMAIFWN HEEIGSQTDE GASSPFFLDV MTRISLSFKL GEENFIRLKR
     HSQLISIDLA HAYHPLHKKK YDSNNAPRMG KGIVIKHNAN QRYATQGLTS AHLVQTCQKE
     NIPYQDFACH SDLPCGSTVG ALTATRTGIP TVDIGLAQLS MHAARELIAV EDHHTLCRLL
     KALLLK
//
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