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Database: UniProt
Entry: A0A0F7JYT5_9GAMM
LinkDB: A0A0F7JYT5_9GAMM
Original site: A0A0F7JYT5_9GAMM 
ID   A0A0F7JYT5_9GAMM        Unreviewed;       106 AA.
AC   A0A0F7JYT5;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 24.
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:AKH19813.1};
GN   ORFNames=AAY24_04960 {ECO:0000313|EMBL:AKH19813.1};
OS   Sedimenticola thiotaurini.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Sedimenticola.
OX   NCBI_TaxID=1543721 {ECO:0000313|EMBL:AKH19813.1, ECO:0000313|Proteomes:UP000034410};
RN   [1] {ECO:0000313|EMBL:AKH19813.1, ECO:0000313|Proteomes:UP000034410}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SIP-G1 {ECO:0000313|EMBL:AKH19813.1,
RC   ECO:0000313|Proteomes:UP000034410};
RX   PubMed=26089430;
RA   Flood B.E., Jones D.S., Bailey J.V.;
RT   "Complete Genome Sequence of Sedimenticola thiotaurini Strain SIP-G1, a
RT   Polyphosphate- and Polyhydroxyalkanoate-Accumulating Sulfur-Oxidizing
RT   Gammaproteobacterium Isolated from Salt Marsh Sediments.";
RL   Genome Announc. 3:e00671-15(2015).
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; CP011412; AKH19813.1; -; Genomic_DNA.
DR   RefSeq; WP_046858749.1; NZ_CP011412.1.
DR   AlphaFoldDB; A0A0F7JYT5; -.
DR   KEGG; seds:AAY24_04960; -.
DR   PATRIC; fig|1543721.4.peg.1034; -.
DR   OrthoDB; 9796121at2; -.
DR   Proteomes; UP000034410; 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:AKH19813.1};
KW   Protease {ECO:0000313|EMBL:AKH19813.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034410}.
FT   DOMAIN          23..101
FT                   /note="Adaptor protein ClpS core"
FT                   /evidence="ECO:0000259|Pfam:PF02617"
SQ   SEQUENCE   106 AA;  11971 MW;  3A4ABFAC5BDD84D2 CRC64;
     MTDKSNPYDD GGLAVETSKP KLKRPPMYKV LLLNDDYTPM EFVVLVLETF FKMDHEKATQ
     IMLNVHTRGV GVCGVYTKDV AETKVAQVNE FSRSHQHPLL CALEEA
//
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