ID A0A0Q6XG93_9BURK Unreviewed; 895 AA.
AC A0A0Q6XG93;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=ClpV1 family T6SS ATPase {ECO:0000313|EMBL:KQV96829.1};
GN ORFNames=ASC87_24865 {ECO:0000313|EMBL:KQV96829.1};
OS Rhizobacter sp. Root1221.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Rhizobacter.
OX NCBI_TaxID=1736433 {ECO:0000313|EMBL:KQV96829.1, ECO:0000313|Proteomes:UP000051465};
RN [1] {ECO:0000313|EMBL:KQV96829.1, ECO:0000313|Proteomes:UP000051465}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1221 {ECO:0000313|EMBL:KQV96829.1,
RC ECO:0000313|Proteomes:UP000051465};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQV96829.1, ECO:0000313|Proteomes:UP000051465}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1221 {ECO:0000313|EMBL:KQV96829.1,
RC ECO:0000313|Proteomes:UP000051465};
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:KQV96829.1}.
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DR EMBL; LMDI01000022; KQV96829.1; -; Genomic_DNA.
DR RefSeq; WP_056664123.1; NZ_LMDI01000022.1.
DR AlphaFoldDB; A0A0Q6XG93; -.
DR STRING; 1736433.ASC87_24865; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000051465; 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:UP000051465};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 10..156
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 442..500
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 895 AA; 98090 MW; 39224BD45A150D3A CRC64;
MAEISRTALF GKLNPLAYKA IEGATVFCKL RGNPYVELQH WLFQILQNQD SDLHRIVKHY
GIDAAVLVAD LQNSLDRLPR GASSITDLSS HIENAVERAW VYGSLMFKDS QVRTGYLLIG
LLKTQSSRNA LLAISKQFER VKLDDLTENF AALLAGSPEH GQAASDGSGA AQPGEASDAI
APAAMGKQEA LKRYAVDLTE KARNGEIDPI AGRDEEIRQI VDILMRRRQN NPILTGEAGV
GKTAVVEGFA LRLARGDVPP QLRDVSLMML DIGLLQAGAS MKGEFENRLR QVIDEVQSSA
KPIILFIDEA HTLIGAGGAA GTGDAANLLK PALARGKLRT IAATTWAEYK KYFEKDPALT
RRFQVVQVPE PSEEKAVLML RGVATILEKH HRVQLLDEAI EAAVKLSHRY IPARQLPDKA
VSLLDTACAR VAVSQHATPP EVEDVQRRIE ALTTEQQIID READVGIDVK VRHDRVAQHL
AEANASLEKL QARFQEEKVL VDQVLALRGK LRKAGDKADG KDAATETTLS PEERTRLLAD
LAELQTKLHH LQGDTPLILP SVDEIAVGAV VQDWTGIPVG RMVKNEVESV LRLADTLNER
VIGQKHALEM IARRIQTSRA KLDNPNKPIG VFMLAGTSGV GKTETALALA EALYGGEQNV
ITINMSEYQE AHTVSTLKGS PPGYVGYGEG GVLTEAVRRR PYSVVLLDEV EKAHPDVHEL
FFQVFDKGWM EDGEGRMIDF KNTIILLTSN AGSDLIMNLC KDPELMPEPD AIAKALREPL
LKVFPAALLG RIVTIPYYPL SEAMLAQIVK LQLNRIKKRV EANHGVPFTF DDDVVKLVVS
RCNEVESGGR VIDALLTNTV LPRISHEYLT RLASGQPLNR VALTVQAGDF AYAFD
//