CLPS_XANCP
ID CLPS_XANCP Reviewed; 106 AA.
AC Q8P999;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 90.
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=XCC1966;
OS Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB
OS 528 / LMG 568 / P 25).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=190485;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25;
RX PubMed=12024217; DOI=10.1038/417459a;
RA da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT specificities.";
RL Nature 417:459-463(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; AE008922; AAM41255.1; -; Genomic_DNA.
DR RefSeq; NP_637331.1; NC_003902.1.
DR RefSeq; WP_011037130.1; NC_003902.1.
DR AlphaFoldDB; Q8P999; -.
DR SMR; Q8P999; -.
DR STRING; 340.xcc-b100_2265; -.
DR EnsemblBacteria; AAM41255; AAM41255; XCC1966.
DR KEGG; xcc:XCC1966; -.
DR PATRIC; fig|190485.4.peg.2101; -.
DR eggNOG; COG2127; Bacteria.
DR HOGENOM; CLU_134358_2_1_6; -.
DR OMA; NDDYTSM; -.
DR Proteomes; UP000001010; 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 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..106
FT /note="ATP-dependent Clp protease adapter protein ClpS"
FT /id="PRO_0000215763"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 106 AA; 12161 MW; 2BE8B41E2B47447B CRC64;
MPRKTSHEHD HGLVVETSKP EVAPPPRYQV LLLNDDYTPM DFVVTVLQQF FNLELERATQ
VMLHVHTRGR GVCGVYSREV AESKVAQVNE FSRMNQHPLL CTMEQA
