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Database: UniProt
Entry: A0A0M4Q5E3_9PSEU
LinkDB: A0A0M4Q5E3_9PSEU
Original site: A0A0M4Q5E3_9PSEU 
ID   A0A0M4Q5E3_9PSEU        Unreviewed;       102 AA.
AC   A0A0M4Q5E3;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
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   ORFNames=WY02_22415 {ECO:0000313|EMBL:ALE80703.1};
OS   Pseudonocardia sp. AL041005-10.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Pseudonocardia.
OX   NCBI_TaxID=445576 {ECO:0000313|EMBL:ALE80703.1, ECO:0000313|Proteomes:UP000067245};
RN   [1] {ECO:0000313|EMBL:ALE80703.1, ECO:0000313|Proteomes:UP000067245}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AL041005-10 {ECO:0000313|EMBL:ALE80703.1,
RC   ECO:0000313|Proteomes:UP000067245};
RX   PubMed=26438860; DOI=10.1073/pnas.1515348112;
RA   Sit C.S., Van Arnam E.B., Ramadhar T.R.;
RT   "Variable genetic architectures produce virtually identical molecules in
RT   bacterial symbionts of fungus-growing ants.";
RL   Proc. Natl. Acad. Sci. U.S.A. 112:13150-13154(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; CP011862; ALE80703.1; -; Genomic_DNA.
DR   RefSeq; WP_060710877.1; NZ_CP011862.1.
DR   AlphaFoldDB; A0A0M4Q5E3; -.
DR   STRING; 445576.WY02_22415; -.
DR   KEGG; psea:WY02_22415; -.
DR   PATRIC; fig|445576.3.peg.4902; -.
DR   OrthoDB; 162238at2; -.
DR   Proteomes; UP000067245; 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:ALE80703.1};
KW   Protease {ECO:0000313|EMBL:ALE80703.1}.
FT   DOMAIN          27..98
FT                   /note="Adaptor protein ClpS core"
FT                   /evidence="ECO:0000259|Pfam:PF02617"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   102 AA;  10960 MW;  E7FE1C0B97313579 CRC64;
     MSAPSPAPSP APTEQVTPDL DESAGPDTPW QAIVWNDPVN LMSYVTYVLQ KVFHYPEAKA
     TALMLDVHHK GRAAVSAGDK DTVEGHVAQL HAAGLWATMQ RA
//
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