CLPS_CAUVC
ID CLPS_CAUVC Reviewed; 119 AA.
AC Q9A5I0;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 99.
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=CC_2467;
OS Caulobacter vibrioides (strain ATCC 19089 / CB15) (Caulobacter crescentus).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=190650;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19089 / CB15;
RX PubMed=11259647; DOI=10.1073/pnas.061029298;
RA Nierman W.C., Feldblyum T.V., Laub M.T., Paulsen I.T., Nelson K.E.,
RA Eisen J.A., Heidelberg J.F., Alley M.R.K., Ohta N., Maddock J.R.,
RA Potocka I., Nelson W.C., Newton A., Stephens C., Phadke N.D., Ely B.,
RA DeBoy R.T., Dodson R.J., Durkin A.S., Gwinn M.L., Haft D.H., Kolonay J.F.,
RA Smit J., Craven M.B., Khouri H.M., Shetty J., Berry K.J., Utterback T.R.,
RA Tran K., Wolf A.M., Vamathevan J.J., Ermolaeva M.D., White O.,
RA Salzberg S.L., Venter J.C., Shapiro L., Fraser C.M.;
RT "Complete genome sequence of Caulobacter crescentus.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:4136-4141(2001).
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}.
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DR EMBL; AE005673; AAK24438.1; -; Genomic_DNA.
DR PIR; B87555; B87555.
DR RefSeq; NP_421270.1; NC_002696.2.
DR PDB; 3DNJ; X-ray; 1.15 A; A/B=35-119.
DR PDB; 3G19; X-ray; 1.85 A; A=35-119.
DR PDB; 3G1B; X-ray; 1.45 A; A/B=35-119.
DR PDB; 3G3P; X-ray; 1.48 A; A/B=35-119.
DR PDB; 3GQ0; X-ray; 2.07 A; A/B=35-119.
DR PDB; 3GQ1; X-ray; 1.50 A; A/B=35-119.
DR PDB; 3GW1; X-ray; 2.36 A; A/B=35-119.
DR PDBsum; 3DNJ; -.
DR PDBsum; 3G19; -.
DR PDBsum; 3G1B; -.
DR PDBsum; 3G3P; -.
DR PDBsum; 3GQ0; -.
DR PDBsum; 3GQ1; -.
DR PDBsum; 3GW1; -.
DR AlphaFoldDB; Q9A5I0; -.
DR SMR; Q9A5I0; -.
DR DIP; DIP-48881N; -.
DR STRING; 190650.CC_2467; -.
DR EnsemblBacteria; AAK24438; AAK24438; CC_2467.
DR KEGG; ccr:CC_2467; -.
DR PATRIC; fig|190650.5.peg.2484; -.
DR eggNOG; COG2127; Bacteria.
DR HOGENOM; CLU_134358_0_0_5; -.
DR OMA; NDDYTSM; -.
DR BioCyc; CAULO:CC2467-MON; -.
DR EvolutionaryTrace; Q9A5I0; -.
DR Proteomes; UP000001816; Chromosome.
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 1: Evidence at protein level;
KW 3D-structure; Reference proteome.
FT CHAIN 1..119
FT /note="ATP-dependent Clp protease adapter protein ClpS"
FT /id="PRO_0000215698"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 41..46
FT /evidence="ECO:0007829|PDB:3DNJ"
FT STRAND 49..52
FT /evidence="ECO:0007829|PDB:3DNJ"
FT HELIX 53..64
FT /evidence="ECO:0007829|PDB:3DNJ"
FT HELIX 68..81
FT /evidence="ECO:0007829|PDB:3DNJ"
FT STRAND 82..89
FT /evidence="ECO:0007829|PDB:3DNJ"
FT HELIX 91..107
FT /evidence="ECO:0007829|PDB:3DNJ"
FT STRAND 114..118
FT /evidence="ECO:0007829|PDB:3DNJ"
SQ SEQUENCE 119 AA; 13413 MW; B255057D2EFD433C CRC64;
MICPPGENKS MAERKQGGQG NGVGSSVVTE VKPKTQKPSL YRVLILNDDY TPMEFVVYVL
ERFFNKSRED ATRIMLHVHQ NGVGVCGVYT YEVAETKVAQ VIDSARRHQH PLQCTMEKD
