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Database: UniProt
Entry: A0A118DT04_9BURK
LinkDB: A0A118DT04_9BURK
Original site: A0A118DT04_9BURK 
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
//
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