GenomeNet

Database: UniProt
Entry: A0A2R7T744_9BURK
LinkDB: A0A2R7T744_9BURK
Original site: A0A2R7T744_9BURK 
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}.
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; 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
//
DBGET integrated database retrieval system