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Database: UniProt
Entry: A0A0Q6WPG0_9BURK
LinkDB: A0A0Q6WPG0_9BURK
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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}.
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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
//
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