ID R7B7D7_9ACTN Unreviewed; 918 AA.
AC R7B7D7;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=BN592_00074 {ECO:0000313|EMBL:CDD59916.1};
OS Eggerthella sp. CAG:298.
OC Bacteria; Actinomycetota; Coriobacteriia; Eggerthellales; Eggerthellaceae;
OC Eggerthella.
OX NCBI_TaxID=1262876 {ECO:0000313|EMBL:CDD59916.1, ECO:0000313|Proteomes:UP000018266};
RN [1] {ECO:0000313|EMBL:CDD59916.1, ECO:0000313|Proteomes:UP000018266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:298 {ECO:0000313|Proteomes:UP000018266};
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:RU362034}.
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:CDD59916.1}.
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DR EMBL; CBHI010000056; CDD59916.1; -; Genomic_DNA.
DR AlphaFoldDB; R7B7D7; -.
DR STRING; 1262876.BN592_00074; -.
DR Proteomes; UP000018266; 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; 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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU362034};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU362034};
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:RU362034};
KW Reference proteome {ECO:0000313|Proteomes:UP000018266};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 7..152
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 419..533
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 918 AA; 101369 MW; 851B1EB3C1C0E023 CRC64;
MDLQKMLEKL ALSAQEALQS AMSIAGEAKA GMVEPIHMLA ALLSSGEHNI DAIVKRLGAD
PKLLRDEVQA EIDRMPKVEG GGIMGMTAPS MALVSLLDKA VKIAEKLGDS YATSEHLLIA
LSEENDAAGK ILNNAGINKN DIQQAYEELR GDTRVTDQQS KTEFEVLDQY GNNLTKAARE
GKLDPVIGRN EEIRRTIQVL SRRTKNNPVL IGEPGTGKTA IVEGLAQRIV AGDVPSSLQD
RELIALDLPS MLAGAKYRGE FEDRLKAVLR EVKESDGQII LFIDELHTIV GAGSSGDSSM
DAGNMLKPAL ARGELHAIGA TTLDEYRKYI EKDAALERRF QPVMVGEPSV EDTIAILRGL
KEKYEIHHGV RVTDSAIVAA AELSNRYISD RFLPDKAIDL MDEAASRLRI EIDSMPEEVD
LAERKLTQMQ IEEQALMKES DEPSKERLEQ LRKDIAAAQE SLDKRKAEWK NEKDSIVSVQ
NLKADIEAAQ LEEERATREG DLARASELRF GRIPELQEQL KAATAALEAR QADGTILKEE
VTEDEIAEVV SSWTGIPITK MMQGEMEKLI DLEDRLHERV VGQDEAVSAV AGAIRRSRAG
LADPEQPIGS FLFLGPTGVG KTELAKALAE CLFDDEKAMI RIDMSEYMEK FSVQRLIGAP
PGYVGYDEGG QLTEAVRRKP YSVILLDEVE KAHPDVFNVL LQVLDDGRLT DGQGRVVSFK
NAIIIMTSNI GSQLIRERDK EETMGDMVED MQKMTPEAAA KRMAEFANRM QDALRNTFRP
EFLNRIDDII TFNELNIASI EPIVELQLAE VSARLKDRKI ELEITPAAKE RLAIDGYDPV
YGARPLKRLI QRQVVDRVAT GIIEGKIYDG STVTIDIDAE GNYDAQVDNH GKDVDLPDGA
AELLEEANSF LNEVEGEE
//