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
//