ID A0A0U3MVT2_9BURK Unreviewed; 883 AA.
AC A0A0U3MVT2;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=ATPase AAA {ECO:0000313|EMBL:ALV07123.1};
DE SubName: Full=Type VI secretion system protein VasG {ECO:0000313|EMBL:REG20106.1};
GN ORFNames=DES44_2613 {ECO:0000313|EMBL:REG20106.1}, RD2015_2658
GN {ECO:0000313|EMBL:ALV07123.1};
OS Roseateles depolymerans.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Roseateles.
OX NCBI_TaxID=76731 {ECO:0000313|EMBL:ALV07123.1, ECO:0000313|Proteomes:UP000060699};
RN [1] {ECO:0000313|EMBL:ALV07123.1, ECO:0000313|Proteomes:UP000060699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 42856 {ECO:0000313|EMBL:ALV07123.1,
RC ECO:0000313|Proteomes:UP000060699};
RA Kim K.M.;
RT "Complete genome of Roseateles depolymerans KCTC 42856.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:REG20106.1, ECO:0000313|Proteomes:UP000256283}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11813 {ECO:0000313|EMBL:REG20106.1,
RC ECO:0000313|Proteomes:UP000256283};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (AUG-2018) 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}.
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DR EMBL; CP013729; ALV07123.1; -; Genomic_DNA.
DR EMBL; QUMT01000002; REG20106.1; -; Genomic_DNA.
DR RefSeq; WP_058935296.1; NZ_QUMT01000002.1.
DR AlphaFoldDB; A0A0U3MVT2; -.
DR STRING; 76731.RD2015_2658; -.
DR KEGG; rdp:RD2015_2658; -.
DR PATRIC; fig|76731.3.peg.2721; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000060699; Chromosome.
DR Proteomes; UP000256283; 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:UP000060699};
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"
FT COILED 440..498
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 883 AA; 96856 MW; 9E5DC02C6B061647 CRC64;
MSEISRTSLF GKLNPLAYKA IEGATVFCKL RGNPYVELQH WIYQILNTPD SDLHRIIKHY
GLDAAQLSAD LMASLDRLPR GASSVTDLSS WVENAVERGW VYGSLLYGDG QVRTGHLVVG
LLKTASMRNV LLSLSRQFER IPVEDLSENF AKVVEGSPEQ AMRAAEPGAA PGDASGAIAP
AAMGKQEALK RFAVDLTERA RQGEIDPVAG RDEEIRQIVD ILMRRRQNNP ILTGEAGVGK
TAVVEGFALR LAQGDVPPQL KDVSLYMLDI GLLQAGASMK GEFENRLRAV IDEVQASPKP
IILFIDEAHT LIGAGGAAGT GDAANLLKPA LARGKLRTIA ATTWAEYKKH IEKDPALTRR
FQVVQVPEPD EAKAVLMLRG VASVLEKHHR VALLDEGIEA AVRLSHRYIP ARQLPDKAVS
LLDTACARVA VSQHATPAEL EDTLRRIQAL EVEQEIIQRE AAIGMDVTER RQRVAVELDQ
AQTRRAELEA RHAREKALVD RVLELHALLR KEGEGAPAEA ERETLLAELK TLRAELADLQ
GDTPLILPTV DEQAVASVVQ DWTGIPVGRM VRNELQAVLQ LADTLNQRVI GQRHALEMIA
KRIEVSRARL DNPNKPIGVF LLAGTSGVGK TETALALAEA LYGGEQNVIT INMSEFQEAH
TVSTLKGSPP GYVGYGEGGV LTEAVRRRPY SVVLLDEVEK AHPDVHELFF QVFDKGWMED
GEGRYIDFKN TIILLTSNAG SDLIMKLCAD PELMPEPEGI AKALREPLLK VFPAALLGRL
VTIPYYPLNE EMLGQIIRLQ LGRIQRRVGE NLGVPFSFGE DVVKLVISRC NEVESGGRVI
DAILTNTVLP RISREYLTRL TQGHSITKVA LTVKDGDFEY GFD
//
