ID A0A0Q5LYV4_9BURK Unreviewed; 122 AA.
AC A0A0Q5LYV4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=ASF94_04755 {ECO:0000313|EMBL:KQR55704.1};
OS Acidovorax sp. Leaf160.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=1736280 {ECO:0000313|EMBL:KQR55704.1, ECO:0000313|Proteomes:UP000051403};
RN [1] {ECO:0000313|EMBL:KQR55704.1, ECO:0000313|Proteomes:UP000051403}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf160 {ECO:0000313|EMBL:KQR55704.1,
RC ECO:0000313|Proteomes:UP000051403};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQR55704.1, ECO:0000313|Proteomes:UP000051403}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf160 {ECO:0000313|EMBL:KQR55704.1,
RC ECO:0000313|Proteomes:UP000051403};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KQR55704.1}.
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DR EMBL; LMOV01000012; KQR55704.1; -; Genomic_DNA.
DR RefSeq; WP_056664685.1; NZ_LMOV01000012.1.
DR AlphaFoldDB; A0A0Q5LYV4; -.
DR STRING; 1736280.ASF94_04755; -.
DR OrthoDB; 9796121at2; -.
DR Proteomes; UP000051403; Unassembled WGS sequence.
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:KQR55704.1};
KW Protease {ECO:0000313|EMBL:KQR55704.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051403}.
FT DOMAIN 39..116
FT /note="Adaptor protein ClpS core"
FT /evidence="ECO:0000259|Pfam:PF02617"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 122 AA; 13568 MW; 800E484A04686EC9 CRC64;
MKFMATNPPP KTPAPPTRAP ARDDGGSVVL ERRTQRTQPP QMFQVVMLND DYTPMEFVIV
VLQEFFSKDR EAATQIMLKI HLDGKGVCGV YSRDVAATKV EQVFEAAHKA GHPLQCVSEP
VE
//
