ID I3TI38_TISMK Unreviewed; 114 AA.
AC I3TI38;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 46.
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:AFK52426.1};
GN OrderedLocusNames=TMO_0587 {ECO:0000313|EMBL:AFK52426.1};
OS Tistrella mobilis (strain KA081020-065).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Geminicoccales;
OC Geminicoccaceae; Tistrella.
OX NCBI_TaxID=1110502 {ECO:0000313|EMBL:AFK52426.1, ECO:0000313|Proteomes:UP000005258};
RN [1] {ECO:0000313|EMBL:AFK52426.1, ECO:0000313|Proteomes:UP000005258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KA081020-065 {ECO:0000313|EMBL:AFK52426.1,
RC ECO:0000313|Proteomes:UP000005258};
RX PubMed=22458477; DOI=10.1021/ja301735a;
RA Xu Y., Kersten R.D., Nam S.J., Lu L., Al-Suwailem A.M., Zheng H.,
RA Fenical W., Dorrestein P.C., Moore B.S., Qian P.Y.;
RT "Bacterial biosynthesis and maturation of the didemnin anti-cancer
RT agents.";
RL J. Am. Chem. Soc. 134:8625-8632(2012).
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; CP003236; AFK52426.1; -; Genomic_DNA.
DR AlphaFoldDB; I3TI38; -.
DR STRING; 1110502.TMO_0587; -.
DR KEGG; tmo:TMO_0587; -.
DR PATRIC; fig|1110502.3.peg.609; -.
DR eggNOG; COG2127; Bacteria.
DR HOGENOM; CLU_134358_0_0_5; -.
DR Proteomes; UP000005258; 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:AFK52426.1};
KW Protease {ECO:0000313|EMBL:AFK52426.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005258}.
FT DOMAIN 32..110
FT /note="Adaptor protein ClpS core"
FT /evidence="ECO:0000259|Pfam:PF02617"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 114 AA; 12950 MW; 3664B0653ED16599 CRC64;
MGMSGERRSD DDRPGFGTVT EVATRPKAAT RKPSMYKVLL LNDDYTPMEF VIDVLQRFFS
KGAEEATRIM LHVHNHGVGV CGVFPFEVAE TKVNQVMDYA RRNQHPLQCT MEKD
//
