ID   A0A1G7EPF8_9BURK        Unreviewed;       890 AA.
AC   A0A1G7EPF8;
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:SDE65509.1};
GN   ORFNames=SAMN05444679_12725 {ECO:0000313|EMBL:SDE65509.1};
OS   Variovorax sp. CF079.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Variovorax.
OX   NCBI_TaxID=1882774 {ECO:0000313|EMBL:SDE65509.1, ECO:0000313|Proteomes:UP000198763};
RN   [1] {ECO:0000313|EMBL:SDE65509.1, ECO:0000313|Proteomes:UP000198763}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CF079 {ECO:0000313|EMBL:SDE65509.1,
RC   ECO:0000313|Proteomes:UP000198763};
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; FMZU01000027; SDE65509.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G7EPF8; -.
DR   STRING; 1882774.SAMN05444679_12725; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000198763; 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:UP000198763};
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   REGION          161..180
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   890 AA;  97595 MW;  59448AB536D274CB CRC64;
     MSEISRTALF GKLNSLAYKA IEGATVFCKM RGNPYVELEH WFAQLLQSQD SDLHRVIQHY
     QLDISVIAKD MTAALDRLPR GATAISDFSP HIENAIERAW TYATLQFGEA QVRTGYLLVG
     MLKTPSLRNP LLGLSKQFDK VKVEDLADNF AKICDASPES KMRAQDGTGM GSGAPGEESG
     AMAPAAMGKG DALKKFAVDL TEKAKKGEMD PVTGRDEEIR QIVDILMRRR QNNPLLTGEA
     GVGKTAVVEG FAQRLARGDV PPQLKDVKLL TLDIGLLQAG ASMKGEFEQR LRQVIDEVQA
     SPTPIILFID EIHTLVGAGG AAGTGDAANL LKPALARGNL RTIGATTWAE YKKYIEKDPA
     LTRRFQVVQV PEPDETKAIL MLRGVASVLE KHHRVQLLDE AIEAAVKLSH RYIPARQLPD
     KAVSLLDTAC ARVAVSQHAM PPEVEDCQRR IEALTVESEI IGREEAIGID VSKRAPQVQA
     LLAESNAELE KLNARWKEEK GLVDRLLELR GKLRAGNKPV DASTPGDGDR AALLAELHEL
     QTQISSVQGE SPLILPSVDS QAVSSVVADW TGIPVGRMQR NEIETVLNLP KLLGQRVIGQ
     DHAMEMIAKR IQTSRAGLDN PSKPIGVFML AGTSGVGKTE TAIALAEALY GGEQNMIVIN
     MSEYQEAHTV SSLKGAPPGY VGYGEGGVLT EAVRRRPYSV VLLDEVEKAH SDVHELFFQV
     FDKGFMEDGE GRSIDFKNTL ILLTTNAGTD MIASMCKDPE LMPEPEGMAK ALREPLLKIF
     PPALLGRLVT IPYYPLSDEM LGKIVELQLK RIKKRVEARY QIPFDYSDEV VKLVVSRCTE
     SESGGRMIDA ILTNTMLPDI SREFLNRMME GKPIERVQVT VDNGAFDYRF
//