ID B9B5A7_9BURK Unreviewed; 956 AA.
AC B9B5A7;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=Negative regulator of genetic competence ClpC/mecB {ECO:0000313|EMBL:EEE00348.1};
GN ORFNames=BURMUCGD1_6015 {ECO:0000313|EMBL:EEE00348.1};
OS Burkholderia multivorans CGD1.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=513051 {ECO:0000313|EMBL:EEE00348.1, ECO:0000313|Proteomes:UP000005493};
RN [1] {ECO:0000313|EMBL:EEE00348.1, ECO:0000313|Proteomes:UP000005493}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGD1 {ECO:0000313|EMBL:EEE00348.1,
RC ECO:0000313|Proteomes:UP000005493};
RX PubMed=23105085; DOI=10.1128/JB.01306-12;
RA Varga J.J., Losada L., Zelazny A.M., Brinkac L., Harkins D., Radune D.,
RA Hostetler J., Sampaio E.P., Ronning C.M., Nierman W.C., Greenberg D.E.,
RA Holland S.M., Goldberg J.B.;
RT "Draft Genome Sequence Determination for Cystic Fibrosis and Chronic
RT Granulomatous Disease Burkholderia multivorans Isolates.";
RL J. Bacteriol. 194:6356-6357(2012).
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, ECO:0000256|RuleBase:RU004432}.
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:EEE00348.1}.
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DR EMBL; ACFB01000004; EEE00348.1; -; Genomic_DNA.
DR RefSeq; WP_006398864.1; NZ_ACFB01000004.1.
DR AlphaFoldDB; B9B5A7; -.
DR Proteomes; UP000005493; 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; 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; IPR028299; ClpA/B_CS2.
DR InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR PANTHER; PTHR11638:SF145; CLPA_B PROTEASE ATP BINDING SUBUNIT-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; 2.
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.
DR PROSITE; PS00871; CLPAB_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004432};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU004432};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 81..224
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT REGION 882..956
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 493..543
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 882..899
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 956 AA; 104425 MW; E17A64E01B402CEA CRC64;
MPALCDICHA RPAVARATVM QDGERKTISI CDYHFRQLMR HQSMLNPFDS LLGGGPSSLF
GGLGEASPLA AEIPRESVDP TDAFSEQTLE LLQRAAEKAH ELRRNELDTE HLLYALADTD
VCAALLKELK LSPQDIKAYI DEHAHTGNTD PDQSLEKLSI SPRVKKAVQY AFQASRDLGH
SYIGPEHLLI GLASVPDSIA GTLLKKYGVT PEALRQKVVK VVGKGAEDGR VDTPTGTPNL
DKFGRDLTAL ARQGKLDPVL GRAQEIESAI EVLARRKKNN PVLIGEPGVG KTAIVEGLAQ
RIVNGDVPEV LRGKRLVEVN INSMVAGAKY RGEFEERAKQ LIDEVTAKQD ELILFIDELH
TIVGAGQGGG EGGLDIANVL KPALARGELS LIGATTLNEY QKYIEKDAAL ERRFQPVFVP
EPSVEQTIVI LRGLRDSLEA HHQVTFSDDA FVAAAEFADR YITSRFLPDK AIDLIDQAAA
RVRIGATSRP VDIQEDEAQI AQLKREQDYA TSRKRFDEAK QFEEQINAKQ KALDEKMEAW
QRKTGSETLE VTVESVAEVV SRLTGIPVSE LTQEERQKLL KMEEQLRERV VGQNDAVVAV
SDAVRLSRAG LGQTHRPIAT FLFLGPTGVG KTELAKALAE SVFGDEQAII RIDMSEYMER
HAVARLIGAP PGYVGYDEGG QLTERVRRRP YSVILLDEIE KAHPDVYNVL LQVFDDGRLT
DGKGRVVDFS NTIIIATSNL GAAIIMDNLT QPEAARKTDK AIREELMQVL KGHFRPEFLN
RIDEVIVFHA LSKENIRSIV QIQLDRVVRT AAAQDIQLVM GESLIEHLTE AGYQPEFGAR
ELKRQVRQTI ETRLAKEILA DALKSGDRVE VDYDKDRGEV TFNKLPPAEA KDAKDAKDAK
AAQQAGNGSA KGNGSAAAAA GRPDGEAGAS DGAPAEAPPP AKKSGKKSSG AKKDAP
//
