GenomeNet

Database: UniProt
Entry: A0A1I4TWW8_9BURK
LinkDB: A0A1I4TWW8_9BURK
Original site: A0A1I4TWW8_9BURK 
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}.
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; 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
//
DBGET integrated database retrieval system