ID C5AA71_BURGB Unreviewed; 889 AA.
AC C5AA71;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE SubName: Full=Putative type VI secretion system protein TssH {ECO:0000313|EMBL:ACR27594.1};
GN OrderedLocusNames=bglu_1g03950 {ECO:0000313|EMBL:ACR27594.1};
OS Burkholderia glumae (strain BGR1).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=626418 {ECO:0000313|EMBL:ACR27594.1, ECO:0000313|Proteomes:UP000002187};
RN [1] {ECO:0000313|EMBL:ACR27594.1, ECO:0000313|Proteomes:UP000002187}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGR1 {ECO:0000313|EMBL:ACR27594.1,
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; CP001503; ACR27594.1; -; Genomic_DNA.
DR RefSeq; WP_012734485.1; NC_012724.2.
DR AlphaFoldDB; C5AA71; -.
DR STRING; 626418.bglu_1g03950; -.
DR GeneID; 58136623; -.
DR KEGG; bgl:bglu_1g03950; -.
DR PATRIC; fig|626418.3.peg.3145; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_2_0_4; -.
DR Proteomes; UP000002187; Chromosome 1.
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 Reference proteome {ECO:0000313|Proteomes:UP000002187};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 9..150
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
SQ SEQUENCE 889 AA; 95580 MW; 53311EF21D21018B CRC64;
MSTPLKTLIA KLNPTCRKAA ERAASQCLAR GHYEVDLEHL FVALLDETSG DMPVVLRASG
VDPHALRRDL ERELDTLKSG NTRTPVFSVH LSELFQQAWL IASLDAQIGR IRSGHLLLAL
LSAPDLAQFA QRMSPQFAQV RVTDLKHKFD EITAGSHEAE PRGAEAGHDG APEAAALAGA
AGGPSKTPAL DTYTTNLTQR ARDGKIDPVI GRDAEIRQAI DILMRRRQNN PIMTGEAGVG
KTAVVEGLAL RIAAADVPPP LAGVALHVLD MGLLQAGASV KGEFENRLKS VIDEVKQSPH
PIILFIDEAH TIIGAGGQAG QNDAANLLKP ALARGELRTI AATTWSEYKK YFEKDAALAR
RFQVVKIEEP SEPLAAAMLR GMAALMERHF NVRILDDAIT EAVRLSHRYI SGRQLPDKAI
SVLDTACAKV ALAQSATPAA IDDLKKRLER TAAEIAALER EVAGGAAHDE RLAALGAARD
ADLAALAAAE ARYAEEQAIV AEIVALRAQI DASREASADG ERIDADAVRA QLAERVAALK
AVQGGEPMVP LQVDAHVVAE IVAAWTGIPL GRMVKDEIET VMNLKALLGA RVIGQDHALD
AVAQRVRTAT AGLEDPNKPR GVFLFVGPSG VGKTETALAL ADVLYGGERK MVTINMSEYQ
EAHSVSGLKG SPPGYVGYGE GGVLTEAVRR NPYSVVLLDE IEKAHPDVLE MFFQVFDKGV
MDDAEGREID FRNTLIILTS NVGSSAVMQA CLNQPAEALP DPDALAETLR PALYKAFKPA
FLGRMKVVPY YPISDDVLAE IIELKLERIA RRIEANHKAR FEWDESLVDA VLARCTEVDS
GARNVDHILN GTLLPEIAGH VLERLAEGSA IERIAVRASE AGEFEYTVK
//
