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Database: UniProt
Entry: C9Z164_STRSW
LinkDB: C9Z164_STRSW
Original site: C9Z164_STRSW 
ID   C9Z164_STRSW            Unreviewed;       105 AA.
AC   C9Z164;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   27-MAR-2024, entry version 70.
DE   RecName: Full=ATP-dependent Clp protease adapter protein ClpS {ECO:0000256|HAMAP-Rule:MF_00302};
GN   Name=clpS {ECO:0000256|HAMAP-Rule:MF_00302,
GN   ECO:0000313|EMBL:CBG72674.1};
GN   OrderedLocusNames=SCAB_56481 {ECO:0000313|EMBL:CBG72674.1};
OS   Streptomyces scabiei (strain 87.22).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=680198 {ECO:0000313|EMBL:CBG72674.1, ECO:0000313|Proteomes:UP000001444};
RN   [1] {ECO:0000313|EMBL:CBG72674.1, ECO:0000313|Proteomes:UP000001444}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=87.22 {ECO:0000313|EMBL:CBG72674.1,
RC   ECO:0000313|Proteomes:UP000001444};
RX   PubMed=20064060; DOI=10.1094/MPMI-23-2-0161;
RA   Bignell D.R., Seipke R.F., Huguet-Tapia J.C., Chambers A.H., Parry R.J.,
RA   Loria R.;
RT   "Streptomyces scabies 87-22 contains a coronafacic acid-like biosynthetic
RT   cluster that contributes to plant-microbe interactions.";
RL   Mol. Plant Microbe Interact. 23:161-175(2010).
CC   -!- FUNCTION: Involved in the modulation of the specificity of the ClpAP-
CC       mediated ATP-dependent protein degradation. {ECO:0000256|HAMAP-
CC       Rule:MF_00302}.
CC   -!- SUBUNIT: Binds to the N-terminal domain of the chaperone ClpA.
CC       {ECO:0000256|HAMAP-Rule:MF_00302}.
CC   -!- SIMILARITY: Belongs to the ClpS family. {ECO:0000256|HAMAP-
CC       Rule:MF_00302}.
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DR   EMBL; FN554889; CBG72674.1; -; Genomic_DNA.
DR   RefSeq; WP_013003244.1; NC_013929.1.
DR   AlphaFoldDB; C9Z164; -.
DR   STRING; 680198.SCAB_56481; -.
DR   GeneID; 85838650; -.
DR   KEGG; scb:SCAB_56481; -.
DR   eggNOG; COG2127; Bacteria.
DR   HOGENOM; CLU_153743_1_0_11; -.
DR   Proteomes; UP000001444; Chromosome.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
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_bL12_C/ClpS-like.
DR   PANTHER; PTHR33473; ATP-DEPENDENT CLP PROTEASE ADAPTER PROTEIN CLPS1, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR33473:SF20; ATP-DEPENDENT CLP PROTEASE ADAPTER PROTEIN CLPS1, CHLOROPLASTIC; 1.
DR   Pfam; PF02617; ClpS; 1.
DR   SUPFAM; SSF54736; ClpS-like; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:CBG72674.1};
KW   Protease {ECO:0000313|EMBL:CBG72674.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001444}.
FT   DOMAIN          28..99
FT                   /note="Adaptor protein ClpS core"
FT                   /evidence="ECO:0000259|Pfam:PF02617"
SQ   SEQUENCE   105 AA;  11847 MW;  08790D7057B9CA44 CRC64;
     MGGVTAAVPM EIEKTESAEE TFAVPEPDVP WLTIVHNDPV NLMSYVTYVF QAYFGYSKEK
     ANKLMLDVHH KGRAVVSSGS REEMERDVQA MHGYGLWATL QQDRK
//
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