ID   CLPS_PSEPK              Reviewed;         120 AA.
AC   Q88FS4;
DT   26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=PP_4009;
OS   Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS   / KT2440).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=160488;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX   PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA   Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA   Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA   Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA   Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA   Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA   Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA   Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA   Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT   "Complete genome sequence and comparative analysis of the metabolically
RT   versatile Pseudomonas putida KT2440.";
RL   Environ. Microbiol. 4:799-808(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}.
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; AE015451; AAN69603.1; -; Genomic_DNA.
DR   RefSeq; NP_746139.1; NC_002947.4.
DR   RefSeq; WP_003251220.1; NC_002947.4.
DR   AlphaFoldDB; Q88FS4; -.
DR   SMR; Q88FS4; -.
DR   STRING; 160488.PP_4009; -.
DR   EnsemblBacteria; AAN69603; AAN69603; PP_4009.
DR   GeneID; 49612957; -.
DR   KEGG; ppu:PP_4009; -.
DR   PATRIC; fig|160488.4.peg.4265; -.
DR   eggNOG; COG2127; Bacteria.
DR   HOGENOM; CLU_134358_2_0_6; -.
DR   OMA; NDDYTSM; -.
DR   PhylomeDB; Q88FS4; -.
DR   BioCyc; PPUT160488:G1G01-4276-MON; -.
DR   Proteomes; UP000000556; 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   3: Inferred from homology;
KW   Reference proteome.
FT   CHAIN           1..120
FT                   /note="ATP-dependent Clp protease adapter protein ClpS"
FT                   /id="PRO_0000215735"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..24
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   120 AA;  13602 MW;  D94629B43252C3EC CRC64;
     MHAPSEIRLT FNQDRPQSNE DDGSGLAVQE AKPILQAPPM YKVVLFNDDY TPMDFVVEVL
     ETFFSLNREL ATKIMLTVHT EGRAVCGLFT RDIAETKAMQ VNQYARESQH PLLCEIEKDG