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Database: UniProt
Entry: A0A515EPV9_9BURK
LinkDB: A0A515EPV9_9BURK
Original site: A0A515EPV9_9BURK 
ID   A0A515EPV9_9BURK        Unreviewed;       900 AA.
AC   A0A515EPV9;
DT   16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2019, sequence version 1.
DT   13-SEP-2023, entry version 18.
DE   SubName: Full=Type VI secretion system ATPase TssH {ECO:0000313|EMBL:QDL54697.1};
GN   Name=tssH {ECO:0000313|EMBL:QDL54697.1};
GN   ORFNames=EXZ61_11240 {ECO:0000313|EMBL:QDL54697.1};
OS   Rhodoferax sediminis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Rhodoferax.
OX   NCBI_TaxID=2509614 {ECO:0000313|EMBL:QDL54697.1, ECO:0000313|Proteomes:UP000317365};
RN   [1] {ECO:0000313|Proteomes:UP000317365}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Gr-4 {ECO:0000313|Proteomes:UP000317365};
RA   Jin L.;
RT   "Complete genome sequence of Rhodoferax sp. Gr-4.";
RL   Submitted (FEB-2019) 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; CP036282; QDL54697.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A515EPV9; -.
DR   KEGG; rhg:EXZ61_11240; -.
DR   Proteomes; UP000317365; Chromosome.
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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          9..151
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          501..540
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   900 AA;  98038 MW;  93D2284AACAC8401 CRC64;
     MYIARKNLFG KLNLVLFRAI ESATAFAKIR GNPYVELVHW IHQLWQIPGN DLHLVLTRYG
     IESAQIERDL SLSLGTLPVG ASSLNDFSHH IEMAIERAWM VASLSAGDSR VRGAWLFAAL
     LQTPELRKVI LGICPALQKI PVAQLDSDLA AIIAASNEEG IQSHQEAQLP AAIPGEASSA
     LASQEDQKGA LGKYCADLTQ QAQEGKIDPV IGREHEIRTM IDILLRRRQN NPLLTGEAGV
     GKTAVVEGFA LAIAAGSVPP SLQHVRLLSL DVGALLAGAS MRGEFEARLK AVLKEVAESP
     QAIIMFIDEV HTLLGAGGQS GSGDAANLLK PALARGGLRT IGATTWAEYK RHIEKDPALT
     RRFQVLQIAE PDEASAIQMV RGMAHVFAKH HGVDILDEAI KAAVKLSHRY IPARQLPDKA
     ISLLDTACAR VAMSIHAAPS DVKALRTHLE AAQTEKNLLQ QEADYGRHNA NGLVGIQSSI
     ASAQEQLTIR TAQWQAERNV CQEILNTRKL LNATKDQAEK EIQLELLKQL EQTLAQLQGE
     SPCVYFQVDE QIVASIVADW TGIPVGRMVR DELATVMGLE GQLRERVVGQ DCALSLISER
     VKTAKAKLSD EGKPLGTFLL VGPSGVGKTE TALALAKAVY GGEQNLITIN MSEYQEAHTI
     STLKGSPPGY IGFGEGGVLT EAVRRRPHSV ILLDEVEKAH PDVHELFYQV FDKGWMEDGE
     GLVIDFKNTL ILLTSNTGAD LIDSLCDDPL LSPSSEELAD ALQPELRKVF PAAFLGRLQI
     VPYLPLHEEV LQRIVRLQMR KVADRLQAQH AIELVYTDQT VEHIVATCGT HETGARRISQ
     FIEQHIATQL AQLWLQAMDE RITLSQIQVR AASENSASDK GRDSLQLAPR AGLLVQAKVG
//
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