ID A0A1I4TWW8_9BURK Unreviewed; 908 AA.
AC A0A1I4TWW8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Type VI secretion system protein VasG {ECO:0000313|EMBL:SFM81232.1};
GN ORFNames=SAMN05444747_10944 {ECO:0000313|EMBL:SFM81232.1};
OS Variovorax sp. OV329.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=1882825 {ECO:0000313|EMBL:SFM81232.1, ECO:0000313|Proteomes:UP000199688};
RN [1] {ECO:0000313|EMBL:SFM81232.1, ECO:0000313|Proteomes:UP000199688}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OV329 {ECO:0000313|EMBL:SFM81232.1,
RC ECO:0000313|Proteomes:UP000199688};
RA de Groot N.N.;
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; FOUG01000009; SFM81232.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I4TWW8; -.
DR STRING; 1882825.SAMN05444747_10944; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000199688; 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:UP000199688};
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"
SQ SEQUENCE 908 AA; 98748 MW; EF6385F7FCC60322 CRC64;
MSEISRTALF GKLNPLAYKA IEGATVFCKM RGNPYVELEH WFAQLLQSPD SDLHRVIQHY
GLDISVIAKD MTAALDRLPR GATAISDFSP HIENAVERAW TYATLQFGEA QVRTGYLLVG
MLKTPSLRNP LMGLSKQFEK VKVEDLADNF AKICDVSPEG KMRAQDGTGM GSGAPGEDTG
AIAPAAMGKG DALKKFAVDL TEKAKKGEMD PVTGRDEEIR QIVDILMRRR QNNPLLTGEA
GVGKTAVVEG FAQRLARGDV PPQLKDVKLL TLDIGLLQAG ASMKGEFEQR LRQVIDEVQA
SPTPIILFID EIHTLVGAGG AAGTGDAANL LKPALARGNL RTIGATTWAE YKKYIEKDPA
LTRRFQVVQV PEPDEVKAIL MLRGVASVLE KHHRVQLLDE AIEAAVKLSH RYIPARQLPD
KAVSLLDTAC ARVAVSQHAM PPEVEDCTRR IEALTVESEI IGREEAIGID VGKRSAQVQS
ALGEAQAELE KLNARWKEEK GLVDRLLELR GKLRDGNKPV DAPAAAASAA AAAEGGDLVS
NGAVAPDRAA MLAELNELQG KISAVQGESP LILPSVDAQA VSSVVADWTG IPVGRMQRNE
IETVLNLPKL LAQRVIGQDH AMEMIAKRIQ TSRAGLDNPQ KPIGVFMLAG TSGVGKTETA
IALAEALYGG EQNMIVINMS EYQEAHTVSS LKGAPPGYVG YGEGGVLTEA VRRRPYSVVL
LDEVEKAHPD VHELFFQVFD KGFMEDGEGR SIDFKNTLIL LTTNAGTDLI ASMCKDPELM
PEPEGMAKAL REPLLKIFPP ALLGRLVTIP YYPLSDVMLG QIVKLQLGRI KKRVESRYQI
PFEYGDDVVK LVVSRCTESE SGGRMIDAIL TNTMLPDISR EFLNRMMEGK PIERVRVGVG
ENDFSYEF
//