ID R6BCF8_9CLOT Unreviewed; 865 AA.
AC R6BCF8;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=BN491_00229 {ECO:0000313|EMBL:CDA51017.1};
OS Clostridium sp. CAG:138.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1262775 {ECO:0000313|EMBL:CDA51017.1, ECO:0000313|Proteomes:UP000017905};
RN [1] {ECO:0000313|EMBL:CDA51017.1, ECO:0000313|Proteomes:UP000017905}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:138 {ECO:0000313|Proteomes:UP000017905};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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}.
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:CDA51017.1}.
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DR EMBL; CBBZ010000022; CDA51017.1; -; Genomic_DNA.
DR AlphaFoldDB; R6BCF8; -.
DR STRING; 1262775.BN491_00229; -.
DR Proteomes; UP000017905; Unassembled WGS sequence.
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 104; 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:UP000017905};
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 443..501
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 865 AA; 96893 MW; E7A01444A4EB9663 CRC64;
MNANKMTQKT LETLQQAQSL AEERRNTQVG QIHVFHALLD DPDDLNAQLM ASMGISTDEL
RAAIDTELDK QATFGSSGGG QVYMTPELNS VLTRAEEEAK RMGDSFVSVE HIMLGLIERA
DYVVKPLLKR FGIVRDKYLE ALKAVRGNSR VNSDNPESTY DVLNKYGQDL TELARAQKLD
PVIGRDNEIR SVIRILSRKT KNNPCLIGEP GVGKTAIAEG LALRIVRGDV PDNLKDRRLF
ALDMGSLVAG AKYRGEFEER LKAVLNEIKR SEGRIIMFID ELHTIVGAGK TDGAMDAGNI
LKPMLARGEL HCIGATTLDE YRKYIEKDAA LERRFQPVTV AEPSVEDTIA ILRGLKERYE
VYHGVKIHDS ALIAAATLSD RYISDRFLPD KAIDLVDEAC ALIKTEMNSM PSEMDEISRE
IMRLEIEETA LTGDNDEHTQ EHLVEIRREL AEKRDKFNNM KARWDNERNA ISKVQQLRER
IEQVNADIAR AENEYDLNRA AQLKYGELPG LQKELQKEEA LAANRENSLL RDHVSSEEIA
KIVARWTGIP VSKLMESERK KLLRLDSQLH KRIVGQDDAV QRVCDAILRS RAGIQNPNRP
IGSFLFLGPT GVGKTELCKA LAEALFDDER SMVRIDMSEY MEQYSVSRLI GAPPGYVGYD
EGGQLTEAVR RKPYAVLLFD EVEKAHPDVL NVLLQVLDDG RITDGQGRTV DFKNTIIILT
SNIGSDLILN SMAKDGRITT ETEELLHKLL RTKFRPEFIN RLDEIVFFNA LSDADMHGIV
DLLIADLAKR LQANRLNLSV SESAKAAIIK NGADPLFGAR PLKRYIQGHI ESLLARFIIE
NSPEEGSTLT VDADEKGSFI IGQKQ
//