GenomeNet

Database: UniProt
Entry: A0A0Q6XG93_9BURK
LinkDB: A0A0Q6XG93_9BURK
Original site: A0A0Q6XG93_9BURK 
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}.
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; 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
//
DBGET integrated database retrieval system