ID   B1Z6M0_BURA4            Unreviewed;       889 AA.
AC   B1Z6M0;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   24-JAN-2024, entry version 87.
DE   SubName: Full=Type VI secretion ATPase, ClpV1 family {ECO:0000313|EMBL:ACB69097.1};
GN   OrderedLocusNames=BamMC406_6693 {ECO:0000313|EMBL:ACB69097.1};
OS   Burkholderia ambifaria (strain MC40-6).
OG   Plasmid pBMC401 {ECO:0000313|EMBL:ACB69097.1,
OG   ECO:0000313|Proteomes:UP000001680}.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=398577 {ECO:0000313|EMBL:ACB69097.1, ECO:0000313|Proteomes:UP000001680};
RN   [1] {ECO:0000313|Proteomes:UP000001680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC40-6 {ECO:0000313|Proteomes:UP000001680};
RC   PLASMID=Plasmid pBMC401 {ECO:0000313|Proteomes:UP000001680};
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Ramette A.,
RA   Konstantinidis K., Tiedje J., Richardson P.;
RT   "Complete sequence of plasmid 1 of Burkholderia ambifaria MC40-6.";
RL   Submitted (APR-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}.
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DR   EMBL; CP001028; ACB69097.1; -; Genomic_DNA.
DR   RefSeq; WP_012367331.1; NC_010553.1.
DR   AlphaFoldDB; B1Z6M0; -.
DR   KEGG; bac:BamMC406_6693; -.
DR   HOGENOM; CLU_005070_1_1_4; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000001680; Plasmid pBMC401.
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; 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; 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   Plasmid {ECO:0000313|EMBL:ACB69097.1};
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   889 AA;  95560 MW;  8E81061ECECEA4B6 CRC64;
     MTISRQALFG KLSHSLFRSV ESATTFCKLR GNPYVELVHW LHQLLQAPDG DLQRIVRHCD
     IDAETLDRDV LRALAALPAG ASSISDFSHH VETTIERAWV LASLNFGDRR IRGAWLVAAL
     VKTPELRRVL LSISPAFGKI PLDSLAEMLP AWIDGSPEAG DAPYDGTDFG GAVPGEVAGA
     LAPSMAGGSP LEQYCSDLTA RARAGEIDPV VGRELEIRTM IDVLLRRRQN NPLLTGDAGV
     GKTAVVEGLA RAVVDGDVPP KLADVRLLSL DVGALLAGAS MKGEFEARLK GVLEAATKST
     VPVILFVDEI HTLIGAGGHA GTGDAANLLK PALARGTLRT IGATTWSEYK RYIEKDPALT
     RRFQVLQVPE PEEAAAIDMV RGLARTFSRH HGVVLLDEAI RAAVTLSHRY IPSRQLPDKA
     ISLLDTACAR VALSQHAPPG ELQDVRQRLQ AARVECDLID HEWRIGLGDG DALARSRARI
     ADLEREADGV EARWRAQADA AQALLSAREA AAEAQGDVPD AGLHAFERAL ADLQGETALV
     FPEVNEVIVA EIVSDWTGIP VRRMVTDEVT AVLALPDTLS ARVIGQSDAL LQIGERVQTA
     RAGLTDPKKP LGVFLLAGPS GVGKTETALA LAEALYGGEQ NLITINMSEY QEAHTVSGLK
     GAPPGYVGYG EGGVLTEAVR RRPYSVVLLD EIEKAHGDVH EMFFQVFDKG YMEDGDGRYI
     DFRHTTILLT SNAGSDLIAS LCADEMLVPD ADALRTALVP ELLKTFPAAF LGRVTVVPYR
     PLAQATLSQI VRLHLDRVVA RMADGHGVAF SYAPAVLDYI VDRCLVQETG ARLLIGFLEQ
     HVLPRLAAQW LDALESKRTL TRVELDLADA GAAPAEAFVF HASGAQADE
//