ID A0A2R7T744_9BURK Unreviewed; 906 AA.
AC A0A2R7T744;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 13-SEP-2023, entry version 23.
DE SubName: Full=Type VI secretion system ATPase TssH {ECO:0000313|EMBL:PTT91572.1};
GN Name=clpV {ECO:0000313|EMBL:PTT91572.1};
GN ORFNames=DBR42_03610 {ECO:0000313|EMBL:PTT91572.1};
OS Pelomonas sp. HMWF004.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Pelomonas.
OX NCBI_TaxID=2056841 {ECO:0000313|EMBL:PTT91572.1, ECO:0000313|Proteomes:UP000244686};
RN [1] {ECO:0000313|Proteomes:UP000244686}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMWF004 {ECO:0000313|Proteomes:UP000244686};
RA Muscarella M.E.;
RL Submitted (APR-2018) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PTT91572.1}.
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DR EMBL; QAJF01000174; PTT91572.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2R7T744; -.
DR Proteomes; UP000244686; 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:UP000244686};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 10..156
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT REGION 154..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 906 AA; 97973 MW; CFCD2BF508D65B4B CRC64;
MAEINRVAVF GKLNALTYKA VEGATVFCKL RGNPYVELEH WVAQIVQNPD SDWHRILRHF
EIDSGLLAKD ITTALDRLPR GATAISDIAD NITNAVERGW VYGSLMYGDT AVRSGYVLLG
MLKTTYLRNA LFAISRQFER IKADDLADGM AKIVTGSPED GQTASDGSGA APGEASGAIA
PAAMGKQEAL KKFTVDLTEQ ARSGKMDPIV GRDDEIRQVV DILMRRRQNN PILVGEAGVG
KTAVVEGFAQ RIARGDVPPS LKDVELRALD VGLLQAGASM KGEFEQRLRS VIDEVQASAK
PIILFIDETH TLVGAGGAAG TGDAANLLKP ALARGTLRTV GATTFAEYKK HIEKDPALTR
RFQTVQVDEP DEVRAVLMMR GVAATMEKHH QVQILDEALE AAVKLSHRYI PARQLPDKSV
SLLDTACARV AVSLHATPAE VDDCRKRIEA LEGELGIIGR ESAVGVDVGS RETVAREHLA
NERTRLAALD ARWAAERELV DEVLSLRAKL RAAAQPVEGT GSALEAEAKS DAAVPADVPS
AEERAAWLAQ LKVAQDKLAE LQGESPLILP TVDYQAVAAV VGDWTGIPVG RMARNEIETI
LKIADHLGQR VIGQDHAMEM IAKRIQTSRA GLDNPSKPIG VFMLAGTSGV GKTETALALA
EALYGGEQNL ITINMSEYQE AHTVSTLKGA PPGYVGYGEG GVLTEAVRRK PYSVVLLDEV
EKAHPDVHEM FFQVFDKGFM EDGEGRFIDF KNTLILLTTN AGTDLIAGLC KDPELMPDPE
GMAKALREPL LKIFPPALLG RLVAIPYYPL SDEMLGRIVK LQLGRIKKRV EARYQIPFNF
GDDVVKLVVS RCTESESGGR MIDAILTNTM LPDISREFLN RMMRGDAIAG VDVGVADGGF
SYSFAD
//