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CLPR_SYNY3
ID   CLPR_SYNY3              Reviewed;         225 AA.
AC   P74466;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   25-MAY-2022, entry version 115.
DE   RecName: Full=Putative ATP-dependent Clp protease proteolytic subunit-like;
DE   AltName: Full=Endopeptidase Clp-like;
GN   Name=clpR; OrderedLocusNames=slr0164;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC   unclassified Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
CC   -!- FUNCTION: Has lost the two conserved residues (Ser and His) proposed to
CC       be part of the active site. Therefore it could be inactive.
CC   -!- SIMILARITY: Belongs to the peptidase S14 family. {ECO:0000305}.
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DR   EMBL; BA000022; BAA18567.1; -; Genomic_DNA.
DR   PIR; S76438; S76438.
DR   AlphaFoldDB; P74466; -.
DR   SMR; P74466; -.
DR   STRING; 1148.1653655; -.
DR   PaxDb; P74466; -.
DR   EnsemblBacteria; BAA18567; BAA18567; BAA18567.
DR   KEGG; syn:slr0164; -.
DR   eggNOG; COG0740; Bacteria.
DR   InParanoid; P74466; -.
DR   OMA; ICDTINY; -.
DR   PhylomeDB; P74466; -.
DR   Proteomes; UP000001425; Chromosome.
DR   GO; GO:0009368; C:endopeptidase Clp complex; IBA:GO_Central.
DR   GO; GO:0004176; F:ATP-dependent peptidase activity; IBA:GO_Central.
DR   GO; GO:0051117; F:ATPase binding; IBA:GO_Central.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IBA:GO_Central.
DR   CDD; cd07017; S14_ClpP_2; 1.
DR   InterPro; IPR001907; ClpP.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR023562; ClpP/TepA.
DR   PANTHER; PTHR10381; PTHR10381; 1.
DR   Pfam; PF00574; CLP_protease; 1.
DR   PRINTS; PR00127; CLPPROTEASEP.
DR   SUPFAM; SSF52096; SSF52096; 1.
PE   3: Inferred from homology;
KW   Reference proteome.
FT   CHAIN           1..225
FT                   /note="Putative ATP-dependent Clp protease proteolytic
FT                   subunit-like"
FT                   /id="PRO_0000179697"
SQ   SEQUENCE   225 AA;  24882 MW;  F7782CCEC17028DB CRC64;
     MEITAVQSSY YGDMAFKTPP PDLESLLLKE RIVYLGMPLF SSDEVKQQVG IDVTQLIIAQ
     LLYLQFDDPD KPIYFYINST GTSWYTGDAV GFETEAFAIC DTLNYIKPPV HTICIGQAMG
     TAAMILSSGT KGYRASLPHA TIVLNQNRTG AQGQATDIQI RAKEVISNKQ TMLEILSLNT
     GQTQEKLAKD MDRTFYLTPA QAKEYGLIDR VLESPAELPK PMAVI
 
 
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