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CLPS_DEIRA
ID   CLPS_DEIRA              Reviewed;         113 AA.
AC   Q9RWS9;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2001, sequence version 2.
DT   25-MAY-2022, entry version 112.
DE   RecName: Full=ATP-dependent Clp protease adapter protein ClpS {ECO:0000255|HAMAP-Rule:MF_00302};
GN   Name=clpS {ECO:0000255|HAMAP-Rule:MF_00302}; OrderedLocusNames=DR_0586;
OS   Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS   4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=243230;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC   9279 / R1 / VKM B-1422;
RX   PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA   White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA   Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA   Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA   Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA   Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA   Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA   Fraser C.M.;
RT   "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT   R1.";
RL   Science 286:1571-1577(1999).
CC   -!- FUNCTION: Involved in the modulation of the specificity of the ClpAP-
CC       mediated ATP-dependent protein degradation. {ECO:0000255|HAMAP-
CC       Rule:MF_00302}.
CC   -!- SUBUNIT: Binds to the N-terminal domain of the chaperone ClpA.
CC       {ECO:0000255|HAMAP-Rule:MF_00302}.
CC   -!- SIMILARITY: Belongs to the ClpS family. {ECO:0000255|HAMAP-
CC       Rule:MF_00302}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF10166.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE000513; AAF10166.1; ALT_INIT; Genomic_DNA.
DR   PIR; B75500; B75500.
DR   RefSeq; NP_294309.1; NC_001263.1.
DR   RefSeq; WP_027479522.1; NC_001263.1.
DR   AlphaFoldDB; Q9RWS9; -.
DR   SMR; Q9RWS9; -.
DR   STRING; 243230.DR_0586; -.
DR   EnsemblBacteria; AAF10166; AAF10166; DR_0586.
DR   KEGG; dra:DR_0586; -.
DR   PATRIC; fig|243230.17.peg.764; -.
DR   eggNOG; COG2127; Bacteria.
DR   HOGENOM; CLU_134358_0_0_0; -.
DR   InParanoid; Q9RWS9; -.
DR   OMA; NDDYTSM; -.
DR   OrthoDB; 1829294at2; -.
DR   Proteomes; UP000002524; Chromosome I.
DR   GO; GO:0051087; F:chaperone binding; IBA:GO_Central.
DR   GO; GO:0030163; P:protein catabolic process; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.1390.10; -; 1.
DR   HAMAP; MF_00302; ClpS; 1.
DR   InterPro; IPR022935; ClpS.
DR   InterPro; IPR003769; ClpS_core.
DR   InterPro; IPR014719; Ribosomal_L7/12_C/ClpS-like.
DR   PANTHER; PTHR33473; PTHR33473; 1.
DR   Pfam; PF02617; ClpS; 1.
DR   SUPFAM; SSF54736; SSF54736; 1.
PE   3: Inferred from homology;
KW   Reference proteome.
FT   CHAIN           1..113
FT                   /note="ATP-dependent Clp protease adapter protein ClpS"
FT                   /id="PRO_0000215704"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          92..113
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   113 AA;  12730 MW;  138C83480B806AE3 CRC64;
     MTRPTIPPGP PGAEGRTQTL ERTETKKPRL WRVLLLNDDY TPMDYVVQVL EQFFRKTEQE
     AELIMLAVHH KGQGVAGVYT RDVAETKVAQ VTAHAQREGH PLRVVAEPES EGE
 
 
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