ID C5AHX4_BURGB Unreviewed; 902 AA.
AC C5AHX4;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE SubName: Full=Type VI secretion ATPase, ClpV1 family {ECO:0000313|EMBL:ACR31504.1};
GN OrderedLocusNames=bglu_2g11100 {ECO:0000313|EMBL:ACR31504.1};
OS Burkholderia glumae (strain BGR1).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=626418 {ECO:0000313|EMBL:ACR31504.1, ECO:0000313|Proteomes:UP000002187};
RN [1] {ECO:0000313|EMBL:ACR31504.1, ECO:0000313|Proteomes:UP000002187}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGR1 {ECO:0000313|EMBL:ACR31504.1,
RC ECO:0000313|Proteomes:UP000002187};
RX PubMed=19329631; DOI=10.1128/JB.00349-09;
RA Lim J., Lee T.H., Nahm B.H., Choi Y.D., Kim M., Hwang I.;
RT "Complete genome sequence of Burkholderia glumae BGR1.";
RL J. Bacteriol. 191:3758-3759(2009).
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; CP001504; ACR31504.1; -; Genomic_DNA.
DR RefSeq; WP_012733891.1; NC_012721.2.
DR AlphaFoldDB; C5AHX4; -.
DR STRING; 626418.bglu_2g11100; -.
DR KEGG; bgl:bglu_2g11100; -.
DR PATRIC; fig|626418.3.peg.1377; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_1_0_4; -.
DR Proteomes; UP000002187; Chromosome 2.
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:SF181; ATPASE SUBUNIT OF ATP-DEPENDENT PROTEASE-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 Coiled coil {ECO:0000256|SAM:Coils};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000002187};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 10..150
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 453..519
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 902 AA; 97440 MW; EEE69291C2E68BFA CRC64;
MTLRDTTHLL RRLNPHCAKA LEAAASLCQG RLSDEITVEH WLLKLIEAGD GDIPAILLHY
RIGIDAVWDA LIAAIERQPR LLRGKPALSP QLAAVLHDAW LHATSEIDEQ AIRSGHLLQA
IADAPHVLRA QHAWPLLSIS STQIQRLLPR LGHRSCESQP ERVEAGADAE ALAAAGEVRP
AAAASDGART PAPRRTVEGD ALARFAIDLT DKARRGDIDP VFGRDREIQQ MVDVLARRRK
NNPILVGEPG VGKTALVEGL ALRVAQANVP NVIREVRILT LDLGLLQAGA GVKGEFEQRL
KNVIDEVQAS PVPIMLFIDE AHTLIGAGNA AGGADAANLL KPALARGELR TIAATTWSEY
KEFFERDAAL ERRFQIIKVD EPDDEAACLM LRGLRSRYAQ HHRVHIRDEA LVAAVRLSRR
YIPARQLPDK AVDLIDTAAA RVRMGLESPP AELQRARAAV SALELEYATL EDDARAGIDN
AQARRASLEA ALASAKSALA DLQQRYDTEL RLVQALHEQR EVEPCARDGA SFAQARQALA
GAQGKTPLIF ADVDAQAIAR VVAEWTGVPV GNLVEDELQG LLALEAQLAR RVVAQDDALA
ALAESLRTAK AGLRNEHAPL GVFLLAGPSG VGKTETALAL ADLLFGGEAA LTTINMSEYQ
ESHTVSQLKG SPPGYVGYGR GGILTEAVRQ RPYSVVLLDE VEKAHRDVLD IFYQVFDRGT
MRDGEGREID FRNCVILMTS NLGSAQIDEA ITDNPGIAQA ALLDAIHPQL VAHFQPALLA
RFQTLVYRPL DASALASIMR LKLAKLAGRL RRQHDVELRC DESLIGAMAE LCLARESGAR
SVDAFLDQRI LPTVSRELLT RMASGLAPAK IALSSSAEGN LTIDFVDRGE PVDAAASEPS
GA
//
