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Database: UniProt
Entry: A0A0Q6W3D1_9BURK
LinkDB: A0A0Q6W3D1_9BURK
Original site: A0A0Q6W3D1_9BURK 
ID   A0A0Q6W3D1_9BURK        Unreviewed;       886 AA.
AC   A0A0Q6W3D1;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   SubName: Full=ClpV1 family T6SS ATPase {ECO:0000313|EMBL:KQV80582.1};
GN   ORFNames=ASD15_11565 {ECO:0000313|EMBL:KQV80582.1};
OS   Massilia sp. Root351.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Telluria group; Massilia.
OX   NCBI_TaxID=1736522 {ECO:0000313|EMBL:KQV80582.1, ECO:0000313|Proteomes:UP000051876};
RN   [1] {ECO:0000313|EMBL:KQV80582.1, ECO:0000313|Proteomes:UP000051876}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root351 {ECO:0000313|EMBL:KQV80582.1,
RC   ECO:0000313|Proteomes:UP000051876};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQV80582.1, ECO:0000313|Proteomes:UP000051876}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root351 {ECO:0000313|EMBL:KQV80582.1,
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:KQV80582.1}.
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DR   EMBL; LMDJ01000031; KQV80582.1; -; Genomic_DNA.
DR   RefSeq; WP_057156824.1; NZ_LMDJ01000031.1.
DR   AlphaFoldDB; A0A0Q6W3D1; -.
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; PF02861; Clp_N; 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   Coiled coil {ECO:0000256|SAM:Coils};
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          9..151
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   REGION          157..188
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          444..497
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   886 AA;  95969 MW;  DF8AE79DF82728F3 CRC64;
     MSINLKTLIG KLNDTCRVAA TRAAGICVSL GQFEVDIEHL FLALLEQPKS DLVVIARRSG
     ISVSMLEADL QAELSRFKNG NTRTPVFSAR LPKLMENAWL IASLDIQSGR AVQIRSAHLL
     QALLTDSELS QLAQRSSKLF AKFELEQIRH KLDEIADGSQ EAVPASQSGG AAQEGGDPVG
     EIAANAPGKT PALDQYTTNL TQRAADGKVD PVIGRDDEIR QAIDILMRRR QNNPILTGEA
     GVGKTAVVEG LALRIAEGDV PDVLKGVQVH TLDMGLLQAG ASVKGEFENR LKNVIDEVRK
     SPHAIILFID EAHTMIGAGG QAGQNDAANL LKPALARGEL RTIAATTWGE YKKYFEKDAA
     LARRFQVVKV EEPSEELACA MLRGMAPLME KHFNVRVYDE AITEAVRLSH RYIMGRQLPD
     KAISVLDTAC AKVALGQNAT PALLENLARR QERMNAEIAS LEREQAAGGG AVHGERLKQL
     REDCEAAGKQ HGELAARWEQ EKQLTEQIKA ARVVLEAGGE ADASQGKDVQ ALLAELKALQ
     GETPMVPVQV DGNVVAGIVA GWTGIPLGKM VKDEIKTVLK LKDMLEERVL GQPHALEAVA
     QRVRTSRANL DDPNKPKGVF LFVGPSGVGK TETALALADV LYGGERKLVT INMSEYQEAH
     SVSGLKGSPP GYVGYGEGGV LTEAVRRNPY SVVLLDEVEK AHPDVLELFF QVFDKGVMDD
     AEGREIDFRN TIIILTSNVA SSTLMQACLN KSAEELPKAD ALEEMIRPQL SKQFKPAFLG
     RLKVIPFYPI PDDVLAEIIE LKLGRIGQRV GANHKAEFSW DEALVDAVLA RCTEVDSGAR
     NVDHILNGTL LPEIAESVLA KMAEGAAIAK IKVGANKDGK FKYTIR
//
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