ID A0A1I5QLD9_9BURK Unreviewed; 898 AA.
AC A0A1I5QLD9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Type VI secretion system protein VasG {ECO:0000313|EMBL:SFP46917.1};
GN ORFNames=SAMN05443579_111278 {ECO:0000313|EMBL:SFP46917.1};
OS Variovorax sp. PDC80.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=1882827 {ECO:0000313|EMBL:SFP46917.1, ECO:0000313|Proteomes:UP000199369};
RN [1] {ECO:0000313|Proteomes:UP000199369}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PDC80 {ECO:0000313|Proteomes:UP000199369};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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; FOWG01000011; SFP46917.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I5QLD9; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000199369; 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; 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000199369};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 10..159
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
SQ SEQUENCE 898 AA; 98014 MW; 0050191499E6F536 CRC64;
MSEISRTALF GKLNSLAYKA IEGATVFCKM RGNPYVELEH WFAQLLQAQD SDLHRVIQHY
GLDVSVIAKD MTAALDRLPR GATAISDFSP HIENAIERAW TYATLQFGEA QVRTGYLLVG
MLKTQSLRNP LFGLSKQFEK VKVEDLAENF VKICDASPEA QMRAQDGTGM GSGAPGEDAG
AMAPAAMGKG DALKKFAVDL TEKAKKGEMD PVTGRDEEIR QIVDILMRRR QNNPLLTGEA
GVGKTAVVEG FAQRLARGDV PPQLKDVKLL TLDIGLLQAG ASMKGEFEQR LRQVIDEVQS
SPTPIILFID EIHTLVGAGG AAGTGDAANL LKPALARGNL RTIGATTWAE YKKYIEKDPA
LTRRFQVVQV PEPDETKAIL MLRGVASVLE KHHRVQLLDE AIEAAVKLSH RYIPARQLPD
KAVSLLDTAC ARVAVSQHAT PPEVEDCMRR IEGLTVEQEI IGREEAIGID VTKRAAQVST
LLAESKAQLE VLNARWQEEK GLVDRLLELR AKLRTGNKPV DAPAGTEAAP AEAAPDRAAL
LAELHELQAK IHAVQGESPL ILPSVDEQAV ASVVADWTGI PVGRMVKNEV EAVLKLADTL
NQRVIGQKHG LEMIARRIQT SRARLDNPQK PIGVFMLCGT SGVGKTETAL ALAEALYGGE
QNIITINMSE FQEAHTVSTL KGAPPGYVGY GEGGILTEAV RRRPYSVVLL DEVEKAHPDV
HEIFFQVFDK GWMEDGEGRM IDFKNTIILL TTNAGSELVM SMCRDPELLP DPNALADALK
APLMKVFPPA LLGRIVTIPY YPLSPEMMKK IVRLQLGRIK KRVETNHGVP FEYSDAVVDQ
VVARCQDPES GGRVIDAILT NTVLPTISVE YLQRLAAGGE IRRVALDVKD ADFTYAFD
//