ID F6ES65_HOYSD Unreviewed; 102 AA.
AC F6ES65;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
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:AEF42069.1};
GN OrderedLocusNames=AS9A_3631 {ECO:0000313|EMBL:AEF42069.1};
OS Hoyosella subflava (strain DSM 45089 / JCM 17490 / NBRC 109087 / DQS3-9A1)
OS (Amycolicicoccus subflavus).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Hoyosellaceae;
OC Hoyosella.
OX NCBI_TaxID=443218 {ECO:0000313|EMBL:AEF42069.1, ECO:0000313|Proteomes:UP000009235};
RN [1] {ECO:0000313|EMBL:AEF42069.1, ECO:0000313|Proteomes:UP000009235}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45089 / DQS3-9A1 {ECO:0000313|Proteomes:UP000009235};
RX PubMed=21725023; DOI=10.1128/JB.05388-11;
RA Cai M., Chen W.M., Nie Y., Chi C.Q., Wang Y.N., Tang Y.Q., Li G.Y.,
RA Wu X.L.;
RT "Complete genome sequence of Amycolicicoccus subflavus DQS3-9A1T, an
RT actinomycete isolated from crude oil-polluted soil.";
RL J. Bacteriol. 193:4538-4539(2011).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002786; AEF42069.1; -; Genomic_DNA.
DR AlphaFoldDB; F6ES65; -.
DR STRING; 443218.AS9A_3631; -.
DR KEGG; asd:AS9A_3631; -.
DR eggNOG; COG2127; Bacteria.
DR HOGENOM; CLU_153743_1_0_11; -.
DR Proteomes; UP000009235; 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:AEF42069.1};
KW Protease {ECO:0000313|EMBL:AEF42069.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009235}.
FT DOMAIN 25..97
FT /note="Adaptor protein ClpS core"
FT /evidence="ECO:0000259|Pfam:PF02617"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 102 AA; 11372 MW; 5083BDFD9CF0226D CRC64;
METDPQTSPG VTPGGLSVAD EDEASQRPWV TIVWDDPVNL MQYVTYVLQK IFGYSRQKAT
ELMLKVHNDG KAVVSSGTRE KVEIDVRKLH AAGLWATMQH ES
//