ID D6Z5B9_DESAT Unreviewed; 874 AA.
AC D6Z5B9;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN OrderedLocusNames=DaAHT2_0063 {ECO:0000313|EMBL:ADH84776.1};
OS Desulfurivibrio alkaliphilus (strain DSM 19089 / UNIQEM U267 / AHT2).
OC Bacteria; Thermodesulfobacteriota; Desulfobulbia; Desulfobulbales;
OC Desulfobulbaceae; Desulfurivibrio.
OX NCBI_TaxID=589865 {ECO:0000313|EMBL:ADH84776.1, ECO:0000313|Proteomes:UP000001508};
RN [1] {ECO:0000313|Proteomes:UP000001508}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19089 / UNIQEM U267 / AHT2
RC {ECO:0000313|Proteomes:UP000001508};
RG US DOE Joint Genome Institute;
RA Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Mikhailova N., Sorokin D.Y., Muyzer G.,
RA Woyke T.;
RT "Complete sequence of Desulfurivibrio alkaliphilus AHT2.";
RL Submitted (FEB-2010) 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. {ECO:0000256|RuleBase:RU362034}.
CC -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent.
CC {ECO:0000256|ARBA:ARBA00026057}.
CC -!- SUBUNIT: Homohexamer; The oligomerization is ATP-dependent.
CC {ECO:0000256|RuleBase:RU362034}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU362034}.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
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DR EMBL; CP001940; ADH84776.1; -; Genomic_DNA.
DR RefSeq; WP_013162307.1; NC_014216.1.
DR AlphaFoldDB; D6Z5B9; -.
DR STRING; 589865.DaAHT2_0063; -.
DR KEGG; dak:DaAHT2_0063; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_1_7; -.
DR InParanoid; D6Z5B9; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000001508; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0042026; P:protein refolding; IEA:UniProtKB-UniRule.
DR GO; GO:0009408; P:response to heat; IEA:UniProtKB-UniRule.
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; IPR017730; Chaperonin_ClpB.
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 NCBIfam; TIGR03346; chaperone_ClpB; 1.
DR PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR PANTHER; PTHR11638:SF18; HEAT SHOCK PROTEIN 78, MITOCHONDRIAL; 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|ARBA:ARBA00023054, ECO:0000256|RuleBase:RU362034};
KW Cytoplasm {ECO:0000256|RuleBase:RU362034};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Reference proteome {ECO:0000313|Proteomes:UP000001508};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..148
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 414..542
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 874 AA; 97756 MW; 5CDE4BE68C7E9F3A CRC64;
MKFDKFTMKS QEAVQEAQSL ALERQHQELQ PEHLAKVLLD QTDGVIAPVL QKMGVSREKL
AAEMEALVSK LPQVSGAGAT QLYASTAFQR LLDRAFKVAS GMQDEYVSQE HLVLALLEDK
DAAAARVLTA QGVTKDAFLK ALESVRGSQR VTDPNPEDKY QALEKYARNL TDVARQGKLD
PVIGRDDEVR RVVQVLSRRT KNNPVLIGEP GVGKTAIVEG LAQRIVNGDV PDTLRNKQVI
ALDMGALVAG AKYRGEFEDR LKAVLKEIQQ RQGEVVLFID EIHTLVGAGA AEGSMDASNM
LKPALARGEL HCVGATTLNE YRKYIEKDAA LERRFQQVLV KEPSVEDTIA ILRGIKEKYE
VHHGVRIKDS ATVAAATLSN RYITDRFLPD KAIDLVDEAA SRLRIEIDSM PTEIDEVERK
KIMLEIEREA LKKESDKSSQ ERLSKVEAEL ADCNEALQAM KGHWSLEKEI IQEIRDIKAK
IDEARIEEQQ AERQGDLSRV AEIRYGRIVE LEKQLAAKNE RLAEIQQDRK MLKEEVDEED
VAAVVAKWTG IPTDRLLEGE KEKLVNADAK LSERVVGQQE AIAAVANAVR RARAGLQDPN
RPLGSFIFLG PTGVGKTELA RSLAAFLFDT EKAMIRLDMS EFMEKHSVAR LIGAPPGYVG
YEEGGYLTEA VRRRPYSVIL FDEIEKAHPD VFNVLLQILD DGRMTDGQGR TVDFKNTILI
MTSNLGSQLI MDLGEERRQE MKARIDEILH AQFKPEFLNR VDEIIIFHAL NREHLSRIVD
IQLQLLTQRL LEQHFKIELT PAAREFVIEV GYDPNYGARP LKRAIQRHIQ DALAMKILEG
AFVEGDTIRI DRPEGSDALS FSRVAGDEAG LDSA
//
