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
//