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Database: UniProt
Entry: F6ES65_HOYSD
LinkDB: F6ES65_HOYSD
Original site: F6ES65_HOYSD 
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}.
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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
//
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