ID A0A118DT04_9BURK Unreviewed; 918 AA.
AC A0A118DT04;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=ClpV1 family T6SS ATPase {ECO:0000313|EMBL:KVE33801.1};
GN ORFNames=WS68_11580 {ECO:0000313|EMBL:KVE33801.1};
OS Burkholderia sp. TSV86.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=1385594 {ECO:0000313|EMBL:KVE33801.1, ECO:0000313|Proteomes:UP000066043};
RN [1] {ECO:0000313|EMBL:KVE33801.1, ECO:0000313|Proteomes:UP000066043}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TSV86 {ECO:0000313|EMBL:KVE33801.1,
RC ECO:0000313|Proteomes:UP000066043};
RA Sahl J., Keim P., Wagner D.;
RT "Expanding the genomic diversity of Burkholderia species for the
RT development of highly accurate diagnostics.";
RL Submitted (NOV-2015) 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:KVE33801.1}.
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DR EMBL; LOWB01000104; KVE33801.1; -; Genomic_DNA.
DR RefSeq; WP_059572161.1; NZ_LOWB01000104.1.
DR AlphaFoldDB; A0A118DT04; -.
DR Proteomes; UP000066043; 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; -; 2.
DR Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 4.10.860.10; UVR domain; 1.
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; PF02861; Clp_N; 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; 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}.
FT DOMAIN 221..365
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 598..754
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 769..859
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
FT COILED 473..500
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 918 AA; 99217 MW; DDCA2FD46F882840 CRC64;
MNRERIFNCL GRTTYAALVD ATALGRSRRH TFIDLDHWAL CLLQRERSDF AKLFAEWGHD
IGDVKRRLEK ALDAFDVSGE SLRDISGALE HSVGPAVIWS QVAAPSSKVR SGHLLLAWLN
DDLTRRWLQQ RVPGGITGAS TDEIVKRYEA LAASWPEAGE CVASSGDDAL ADDASADAAS
PDALAKWATC LTDQAARGEL DPVVGRDAEL RTVIDILSRR RQNNPILVGE AGVGKTAVVE
ALAQKIHAGD VPPGLLGAQV WALDLARLQA GAGVRGEFEQ RLKAVMDAVL AAPNPVILFC
DETHTLVGAG GAAGTGDAAN LIKPMLARGQ LRMVAATTWS EYKQYIEPDA ALVRRFQAVP
VEEPDDEAAV DMLRTIAPRF AEHHGVHIID AALRSAVALS RRYLPARQLP DKAIGLLDTA
CARVAMSQNC APAELDRLAQ QAFAIEQTLN WRANDRHMGV PTPGDEADLQ ARRGELVQQV
RTLEKAVEGE REEVRAWRAR LSAPPSAEQA DEADSNAWAA RIDAERWVRP WVDEHVIAEV
LSEWTGVPVT QLAQDEAQRI VELERSLNEC IHGQAHGLRS IAQVLQVSHS GLGDPERPLG
VMLLAGPTGT GKSQAAAKLA ELLFGGERNL VQFNMNEFQE AHTASTLKGA PPGYVGYGKG
GRLTEAIRKK PYSVLLLDEF DRAHPDIHEV FYQVFDQGWM EDGEGRRISF RNSLILLTTN
LGDADIEAAC EADPQTSQAN LESLVRERLQ GRFSAALLGR IQIVVFRPLD HDALAGIARQ
ALDEIGERLA QNGLAWRVDE GVADWIARAV ARHPSNGRAV RDLLRQHVMP AVARGVLAAR
AEDRSLQIVR LSAGDTLSLS FDDDAAVLND AAALPEAAPE AEAAHVAETA AATADVEGAV
CEGEFPADAG SKGETACV
//