ID H0UID6_9BACT Unreviewed; 868 AA.
AC H0UID6;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=JonanDRAFT_0219 {ECO:0000313|EMBL:EHM12644.1};
OS Jonquetella anthropi DSM 22815.
OC Bacteria; Synergistota; Synergistia; Synergistales;
OC Dethiosulfovibrionaceae; Jonquetella.
OX NCBI_TaxID=885272 {ECO:0000313|EMBL:EHM12644.1, ECO:0000313|Proteomes:UP000003806};
RN [1] {ECO:0000313|EMBL:EHM12644.1, ECO:0000313|Proteomes:UP000003806}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22815 {ECO:0000313|EMBL:EHM12644.1,
RC ECO:0000313|Proteomes:UP000003806};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Held B.,
RA Kyrpides N., Mavromatis K., Ivanova N., Markowitz V., Cheng J.-F.,
RA Hugenholtz P., Woyke T., Wu D., Gronow S., Wellnitz S., Brambilla E.,
RA Klenk H.-P., Eisen J.A.;
RT "The Noncontiguous Finished genome of Jonquetella anthropi DSM 22815.";
RL Submitted (NOV-2011) 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; CM001376; EHM12644.1; -; Genomic_DNA.
DR RefSeq; WP_008522437.1; NZ_CM001376.1.
DR AlphaFoldDB; H0UID6; -.
DR STRING; 885272.JonanDRAFT_0219; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_2_0; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000003806; 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:UP000003806};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..149
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 415..502
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 868 AA; 95757 MW; ADC6634179DF16E6 CRC64;
MDLNKLTQKS QEALAEAQNI AVTHGHQQVG LEHLALALVG AKDGLTPSLL DKCGADVRAL
PARLEELLAK RPKITGGYDI EKIYLSTDLS QLLLNAEKCA QSMKDEYVSV EHLFLALFDF
PTSPTGQALA AAGLTKEGFL KALTGVRGAT RVQSANPEET YEALKKYGTD LVAAARDGKL
DPVIGRDAEI LRVIQILSRK SKNNPVLIGE PGVGKTAIVE GLAARIVRGD VPEGLKNRTI
FALDMGSLIA GAKYRGEFEE RLKAVISEVK AAEGQIILFI DELHTIVGAG KTEGSMDAGN
LLKPMLARGE LHCIGATTLD EYRLHIEKDA ALERRFQPVR VEPPTPEDAI SILRGLKDRF
QVFHGVRIAD SAIVAAVTLS DRYISDRFLP DKAIDLVDEA CAMVKTEINS RPSELDAVSR
RVVRLEIEEA ALKKERDDAS ARRLAELQKE LADAREQQNE LTARYESEKS RLTDVQALRE
RIEAAKVELE KAERAYDLER MAELRHGELP KLTEELAKKE KALKEASGGE SLLRESVTED
EIARIVSDWT GIPVTKLVQS ERDKLLHLDD ELHKGVIGQD QAVQLVADAV LRARAGIRDP
KRPIGSFIFL GPTGVGKTEL ARVLARTLFD SENNMVRIDM SEYMEKYSVS RLLGAPPGYV
GYDEGGQLTE AIRRKPYCVL LFDEIEKAHP DVFNVLLQIL DDGRVTDSHG RTVDFKNTVI
IMTSNIGSQM LLDGVTDGGE IPQPVRDQVM AQLKGHFRPE FLNRIDDTVI FSPLSRENLR
QIAVLLLRGL TDRLAGQSTV LRVTDEALDL IIRQSYEPSY GARPLKRYIS HNLETLVARY
LIANGPAENA ALVVDASGDE LTLRTEKN
//
