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Y219_RICPR
ID   Y219_RICPR              Reviewed;         412 AA.
AC   O05945;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Uncharacterized zinc protease RP219;
DE            EC=3.4.24.-;
GN   OrderedLocusNames=RP219;
OS   Rickettsia prowazekii (strain Madrid E).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=272947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Madrid E;
RX   PubMed=9274032; DOI=10.1099/00221287-143-8-2783;
RA   Andersson J.O., Andersson S.G.E.;
RT   "Genomic rearrangements during evolution of the obligate intracellular
RT   parasite Rickettsia prowazekii as inferred from an analysis of 52015 bp
RT   nucleotide sequence.";
RL   Microbiology 143:2783-2795(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Madrid E;
RX   PubMed=9823893; DOI=10.1038/24094;
RA   Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA   Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA   Kurland C.G.;
RT   "The genome sequence of Rickettsia prowazekii and the origin of
RT   mitochondria.";
RL   Nature 396:133-140(1998).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the peptidase M16 family. {ECO:0000305}.
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DR   EMBL; Y11780; CAA72467.1; -; Genomic_DNA.
DR   EMBL; AJ235270; CAA14682.1; -; Genomic_DNA.
DR   PIR; C71733; C71733.
DR   RefSeq; NP_220605.1; NC_000963.1.
DR   RefSeq; WP_004596018.1; NC_000963.1.
DR   AlphaFoldDB; O05945; -.
DR   SMR; O05945; -.
DR   STRING; 272947.RP219; -.
DR   MEROPS; M16.016; -.
DR   EnsemblBacteria; CAA14682; CAA14682; CAA14682.
DR   GeneID; 57569347; -.
DR   KEGG; rpr:RP219; -.
DR   PATRIC; fig|272947.5.peg.226; -.
DR   eggNOG; COG0612; Bacteria.
DR   HOGENOM; CLU_009902_3_0_5; -.
DR   OMA; WSNPDNV; -.
DR   Proteomes; UP000002480; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR011249; Metalloenz_LuxS/M16.
DR   InterPro; IPR011765; Pept_M16_N.
DR   InterPro; IPR001431; Pept_M16_Zn_BS.
DR   InterPro; IPR007863; Peptidase_M16_C.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 1.
DR   SUPFAM; SSF63411; SSF63411; 2.
DR   PROSITE; PS00143; INSULINASE; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Metalloprotease; Protease; Reference proteome;
KW   Zinc.
FT   CHAIN           1..412
FT                   /note="Uncharacterized zinc protease RP219"
FT                   /id="PRO_0000074427"
FT   ACT_SITE        52
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT   BINDING         49
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT   BINDING         53
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT   BINDING         129
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
SQ   SEQUENCE   412 AA;  46611 MW;  29656AEB381031AE CRC64;
     MKENFNVSKL KNGLTILTYN MPYVHSVAIN LIAKVGARYE NEEEEGISHF LEHMAFKGTK
     TRTAQQIAEE FDSIGGYFNA YTGHENTVYY ARVLSENCHK ALNILADIIQ NSIFADEEIA
     KEYQIIMQEI AHHHDNPDDL IYETFYNTVY KGQPLGKSIL GTTKTLVTFT KEHFLNFIGK
     HYNAENLYLS IAGNIEHNKI VMIAEELFAS LKQGVKSSFI PAKYIGGKGF IHKELEQTSL
     VLGFECTSYI NLGQLYQTYL LSIIFGGGMS SRLFQSIREK LGLAYVVGSY NSAYFDSGVF
     TIYASTAHNK LELLYREIKN EIIKITETVS TEEIIRAKMQ LRSNLQMAQE QNTYKSEEIG
     KNYSVFGKYI LPEEIIEIIT NIRADDIINT ANKIFSGTTT LAIIGPNDLN GF
 
 
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