ID A0A0Q6WPG0_9BURK Unreviewed; 911 AA.
AC A0A0Q6WPG0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=ClpV1 family T6SS ATPase {ECO:0000313|EMBL:KQV87782.1};
GN ORFNames=ASD15_27370 {ECO:0000313|EMBL:KQV87782.1};
OS Massilia sp. Root351.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=1736522 {ECO:0000313|EMBL:KQV87782.1, ECO:0000313|Proteomes:UP000051876};
RN [1] {ECO:0000313|EMBL:KQV87782.1, ECO:0000313|Proteomes:UP000051876}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root351 {ECO:0000313|EMBL:KQV87782.1,
RC ECO:0000313|Proteomes:UP000051876};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQV87782.1, ECO:0000313|Proteomes:UP000051876}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root351 {ECO:0000313|EMBL:KQV87782.1,
RC ECO:0000313|Proteomes:UP000051876};
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: Part of a stress-induced multi-chaperone system, it is
CC involved in the recovery of the cell from heat-induced damage, in
CC cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the
CC processing of protein aggregates. Protein binding stimulates the ATPase
CC activity; ATP hydrolysis unfolds the denatured protein aggregates,
CC which probably helps expose new hydrophobic binding sites on the
CC surface of ClpB-bound aggregates, contributing to the solubilization
CC and refolding of denatured protein aggregates by DnaK.
CC {ECO:0000256|ARBA:ARBA00025613}.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|ARBA:ARBA00008675}.
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:KQV87782.1}.
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; LMDJ01000005; KQV87782.1; -; Genomic_DNA.
DR RefSeq; WP_057154620.1; NZ_LMDJ01000005.1.
DR AlphaFoldDB; A0A0Q6WPG0; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000051876; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR CDD; cd00009; AAA; 1.
DR CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR017729; ATPase_T6SS_ClpV1.
DR InterPro; IPR019489; Clp_ATPase_C.
DR InterPro; IPR036628; Clp_N_dom_sf.
DR InterPro; IPR004176; Clp_R_dom.
DR InterPro; IPR001270; ClpA/B.
DR InterPro; IPR018368; ClpA/B_CS1.
DR InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR03345; VI_ClpV1; 1.
DR PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR PANTHER; PTHR11638:SF184; ATPASE WITH CHAPERONE ACTIVITY-RELATED; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF17871; AAA_lid_9; 1.
DR Pfam; PF10431; ClpB_D2-small; 1.
DR PRINTS; PR00300; CLPPROTEASEA.
DR SMART; SM00382; AAA; 2.
DR SMART; SM01086; ClpB_D2-small; 1.
DR SUPFAM; SSF81923; Double Clp-N motif; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51903; CLP_R; 1.
DR PROSITE; PS00870; CLPAB_1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000051876};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 10..151
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
SQ SEQUENCE 911 AA; 98712 MW; D4F38810752EC0B9 CRC64;
MAEISRVALF GKLNSLCYRA IESSTVFCKL RGNPYVELVH WMHQILQLQD SDLLRLVKHY
ELDAAGLARD LTAALDRLPR GSTSGIDLSS QLEESVERAW VYGTLMFGES QIRSGHIVVG
MLKTSSLRNA LYGMSPQFQK IKADDLSEKF ASLLKESPEA QMAATDGFQA GGGAAPGEAS
GAIAPAAMGK QEALKKFTVD LTEQARSGKM DPIVGRDDEI RQVVDILMRR RQNNPILVGE
AGVGKTAVVE GFAQRIARGD VPPSLKDVQL LTLDVGLLQA GASMKGEFEQ RLRSVIDEVQ
GSPKPIILFI DETHTLVGAG GAAGTGDAAN LLKPALARGT LRTIGATTFA EYKKHIEKDP
ALTRRFQTVQ VDEPSEERAI LMMRGVASTM EKHHKVQILD EALEAAVKLS HRYIPARQLP
DKSVSLLDTA CARVAVSLHA TPAEVDDARK RIEALETELG IIGRESAIGI DIGKRKSEAD
DLLGAERERL AGLETRWNAE RELVDELLAL RAKLRDGAQP VEGTGSSLEA GAEAAAATAA
TAPAIAPEER AALMEQLKAV QAKLSALQGE TPLILPTVDY QAVAAVVGDW TGIPVGRMAK
NEMETILKVA SLLSQRVIGQ DHAMEMIAKR IQTSRAGLDN PSKPIGVFML AGTSGVGKTE
TALALAEALY GGEQNLITIN MSEYQEAHTV STLKGAPPGY VGYGEGGVLT EAVRRKPYSV
VLLDEVEKAH PDVHEMFFQV FDKGFMEDGE GRFIDFKNTL IILTTNAGTD LIAGLCKDPD
LMPDPDGMAK ALRAPMLKVF PPALLGRIVT IPYYPLSDQM LGQIVKLQLN RIKKRVEARY
KIPFQYSEEV VKLVVSRCTE GESGGRMIDA ILTNTMLPDI SREFLNRMMQ GDAIAGVQVE
VKEGEFAYSF D
//