CLPS_ECOLI
ID CLPS_ECOLI Reviewed; 106 AA.
AC P0A8Q6; P75832;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 121.
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}; Synonyms=yljA;
GN OrderedLocusNames=b0881, JW0865;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP FUNCTION, AND INTERACTION WITH CLPA.
RX PubMed=11931773; DOI=10.1016/s1097-2765(02)00485-9;
RA Dougan D.A., Reid B.G., Horwich A.L., Bukau B.;
RT "ClpS, a substrate modulator of the ClpAP machine.";
RL Mol. Cell 9:673-683(2002).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH CLPA.
RX PubMed=12426582; DOI=10.1038/nsb869;
RA Zeth K., Ravelli R.B., Paal K., Cusack S., Bukau B., Dougan D.A.;
RT "Structural analysis of the adaptor protein ClpS in complex with the N-
RT terminal domain of ClpA.";
RL Nat. Struct. Biol. 9:906-911(2002).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEX WITH CLPA.
RX PubMed=12235156; DOI=10.1074/jbc.m208104200;
RA Guo F., Esser L., Singh S.K., Maurizi M.R., Xia D.;
RT "Crystal structure of the heterodimeric complex of the adaptor, ClpS, with
RT the N-domain of the AAA+ chaperone, ClpA.";
RL J. Biol. Chem. 277:46753-46762(2002).
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, ECO:0000269|PubMed:11931773}.
CC -!- SUBUNIT: Binds to the N-terminal domain of the chaperone ClpA.
CC {ECO:0000255|HAMAP-Rule:MF_00302, ECO:0000269|PubMed:12235156,
CC ECO:0000269|PubMed:12426582}.
CC -!- INTERACTION:
CC P0A8Q6; P0ABH9: clpA; NbExp=13; IntAct=EBI-561456, EBI-546140;
CC P0A8Q6; P0ABT2: dps; NbExp=5; IntAct=EBI-561456, EBI-549640;
CC -!- SIMILARITY: Belongs to the ClpS family. {ECO:0000255|HAMAP-
CC Rule:MF_00302}.
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DR EMBL; U00096; AAC73968.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35600.1; -; Genomic_DNA.
DR PIR; A64827; A64827.
DR RefSeq; NP_415402.1; NC_000913.3.
DR RefSeq; WP_000520781.1; NZ_STEB01000006.1.
DR PDB; 1LZW; X-ray; 2.50 A; A=1-106.
DR PDB; 1MBU; X-ray; 2.30 A; C/D=1-106.
DR PDB; 1MBV; X-ray; 3.30 A; B=1-106.
DR PDB; 1MBX; X-ray; 2.25 A; C/D=1-106.
DR PDB; 1MG9; X-ray; 2.30 A; A=1-106.
DR PDB; 1R6O; X-ray; 2.25 A; C/D=1-106.
DR PDB; 1R6Q; X-ray; 2.35 A; C/D=1-106.
DR PDB; 2W9R; X-ray; 1.70 A; A=1-106.
DR PDB; 2WA8; X-ray; 2.15 A; A/C=1-106.
DR PDB; 2WA9; X-ray; 2.90 A; A/B/C/D/E/F/G=1-106.
DR PDB; 3O1F; X-ray; 1.40 A; A/B=26-106.
DR PDB; 3O2B; X-ray; 2.05 A; A/C=2-106.
DR PDB; 3O2H; X-ray; 1.70 A; A=2-106.
DR PDB; 3O2O; X-ray; 2.90 A; A/B/C/D/E/F/G/H=22-106.
DR PDBsum; 1LZW; -.
DR PDBsum; 1MBU; -.
DR PDBsum; 1MBV; -.
DR PDBsum; 1MBX; -.
DR PDBsum; 1MG9; -.
DR PDBsum; 1R6O; -.
DR PDBsum; 1R6Q; -.
DR PDBsum; 2W9R; -.
DR PDBsum; 2WA8; -.
DR PDBsum; 2WA9; -.
DR PDBsum; 3O1F; -.
DR PDBsum; 3O2B; -.
DR PDBsum; 3O2H; -.
DR PDBsum; 3O2O; -.
DR AlphaFoldDB; P0A8Q6; -.
DR SMR; P0A8Q6; -.
DR BioGRID; 4261321; 77.
DR BioGRID; 852740; 2.
DR DIP; DIP-35408N; -.
DR IntAct; P0A8Q6; 43.
DR MINT; P0A8Q6; -.
DR STRING; 511145.b0881; -.
DR SWISS-2DPAGE; P0A8Q6; -.
DR jPOST; P0A8Q6; -.
DR PaxDb; P0A8Q6; -.
DR PRIDE; P0A8Q6; -.
DR EnsemblBacteria; AAC73968; AAC73968; b0881.
DR EnsemblBacteria; BAA35600; BAA35600; BAA35600.
DR GeneID; 58462759; -.
DR GeneID; 948443; -.
DR KEGG; ecj:JW0865; -.
DR KEGG; eco:b0881; -.
DR PATRIC; fig|1411691.4.peg.1396; -.
DR EchoBASE; EB3992; -.
DR eggNOG; COG2127; Bacteria.
DR HOGENOM; CLU_134358_2_1_6; -.
DR InParanoid; P0A8Q6; -.
DR OMA; NDDYTSM; -.
DR PhylomeDB; P0A8Q6; -.
DR BioCyc; EcoCyc:G6463-MON; -.
DR EvolutionaryTrace; P0A8Q6; -.
DR PRO; PR:P0A8Q6; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
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 GO; GO:0009408; P:response to heat; IMP:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; Reference proteome.
FT CHAIN 1..106
FT /note="ATP-dependent Clp protease adapter protein ClpS"
FT /id="PRO_0000215707"
FT HELIX 13..20
FT /evidence="ECO:0007829|PDB:2W9R"
FT STRAND 28..33
FT /evidence="ECO:0007829|PDB:3O1F"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:3O1F"
FT HELIX 40..51
FT /evidence="ECO:0007829|PDB:3O1F"
FT HELIX 55..68
FT /evidence="ECO:0007829|PDB:3O1F"
FT STRAND 69..76
FT /evidence="ECO:0007829|PDB:3O1F"
FT HELIX 78..94
FT /evidence="ECO:0007829|PDB:3O1F"
FT STRAND 100..105
FT /evidence="ECO:0007829|PDB:3O1F"
SQ SEQUENCE 106 AA; 12179 MW; 2E9DC8000EA3CE86 CRC64;
MGKTNDWLDF DQLAEEKVRD ALKPPSMYKV ILVNDDYTPM EFVIDVLQKF FSYDVERATQ
LMLAVHYQGK AICGVFTAEV AETKVAMVNK YARENEHPLL CTLEKA
