ID B1FA78_9BURK Unreviewed; 897 AA.
AC B1FA78;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 24-JAN-2024, entry version 71.
DE SubName: Full=Type VI secretion ATPase, ClpV1 family {ECO:0000313|EMBL:EDT05533.1};
GN ORFNames=BamIOP4010DRAFT_0937 {ECO:0000313|EMBL:EDT05533.1};
OS Burkholderia ambifaria IOP40-10.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=396596 {ECO:0000313|EMBL:EDT05533.1, ECO:0000313|Proteomes:UP000005463};
RN [1] {ECO:0000313|EMBL:EDT05533.1, ECO:0000313|Proteomes:UP000005463}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IOP40-10 {ECO:0000313|EMBL:EDT05533.1,
RC ECO:0000313|Proteomes:UP000005463};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Larimer F., Land M.L., Hauser L.,
RA Tiedje J., Richardson P.;
RT "Sequencing of the draft genome and assembly of Burkholderia ambifaria
RT IOP40-10.";
RL Submitted (MAR-2008) 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:EDT05533.1}.
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DR EMBL; ABLC01000011; EDT05533.1; -; Genomic_DNA.
DR RefSeq; WP_006750146.1; NZ_ABLC01000011.1.
DR AlphaFoldDB; B1FA78; -.
DR PATRIC; fig|396596.7.peg.7014; -.
DR Proteomes; UP000005463; 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 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"
SQ SEQUENCE 897 AA; 96779 MW; F450629EDA1C9748 CRC64;
MTISRQALFG KLGVQLYRSI ESATQFCKLR GNPYVELIHW LHQLLQQPDS DLHRIVRHAG
IERDVLDRDF ARALAVLPAG ASSISDFSWH IETAIERAWV LATLSHGDRR VRGAWLVVAL
VSTPELRRVL LSISPAFGKI PVDGLGDELP AWIDGSPEAA DAPYDHGDLS AATPGEASGA
IPVASKRGSL DQYCADLTAR ARVGEIDPVI GRELEIRTMI DVLLRRRQNN PLVTGEAGVG
KTAVVEGLAR AIASGNVPPK LADVRLLSLD VGALLAGASM KGEFEARLKG LLEAAGKLPT
PVILFIDEIH TLIGAGGQAG TGDAANLLKP ALARGTIRTI GATTWAEYKR HIEKDPALTR
RFQVLQIAEP SEAAAIDMVR GLAQTFCRHH GVVVLDEAIR AAVTLSHRYI PSRQLPDKAI
SLLDTACARV ALSQHAAPRE LDDVRQRLAA ARAEEALLVQ EARIGLDTDR ALTGVRVRID
TLGAEAAAVE HRWRSQAAAA QALLVAREAI GPDDGKPPRD EVAALLKLRE LEHALVALQG
DAPLVFPEVD EAIVAEIVSD WTGIPVGRMV TDEVAAVRKL PETLEARVIG QADALRQIGE
RVQTARAGLT DPRKPVGVFL LAGPSGVGKT ETALALAEAL YGGEQNLITI NMSEYQEAHT
VSGLKGAPPG YVGYGEGGVL TEAVRRRPYS VVLLDEIEKA HRDVHEMFFQ VFDKGYMEDG
DGRYIDFRNT TILLTSNVGS ELSTSLCADP SLAPNQDGLR DALTPELLKV FPAAFLGRMT
VVPYRPLADS VLASIVRLYL ERIVKRMADG HGIALTYDDA VVNYIIGRCL VQETGARVLI
GFIEQHVLPR LSALWLDAFA SKRTLSHIVI GVADPSCMPA QALSFDAIDF HSDEPVL
//
