ID R7BPB7_9ACTN Unreviewed; 914 AA.
AC R7BPB7;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 57.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=BN629_01287 {ECO:0000313|EMBL:CDD67645.1};
OS Eggerthella sp. CAG:368.
OC Bacteria; Actinomycetota; Coriobacteriia; Eggerthellales; Eggerthellaceae;
OC Eggerthella.
OX NCBI_TaxID=1262877 {ECO:0000313|EMBL:CDD67645.1, ECO:0000313|Proteomes:UP000018088};
RN [1] {ECO:0000313|EMBL:CDD67645.1, ECO:0000313|Proteomes:UP000018088}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:368 {ECO:0000313|Proteomes:UP000018088};
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:CDD67645.1}.
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DR EMBL; CBHM010000064; CDD67645.1; -; Genomic_DNA.
DR AlphaFoldDB; R7BPB7; -.
DR STRING; 1262877.BN629_01287; -.
DR Proteomes; UP000018088; 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:UP000018088};
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 415..536
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 914 AA; 100550 MW; 01CD369C07841FEF CRC64;
MRFDKLALTA QEALQSAMSI AGEAEAGSVE PLHLLSALLA SGEHNMNAIV SRIGADPAYL
KTKTAEEISR MPKVSNGGFM GMAVPSPAFI KVMDNAVKIA EKLGDSYATS EHLLIALSEE
KGTAGKILND AGITRKNIEE AYEELRGDTR VTDAQNKAEF EVLEQYGNNL TQAAREGKLD
PVIGRSEEIR RTIQVLSRRT KNNPVLIGEP GTGKTAIVEG LAQRIVAGDV PSSLQDRELI
ALDLPAMLAG AKYRGEFEDR LKAVLREVKQ SDGQIILFID ELHTIVGAGS TGDSSMDAGN
MLKPALARGE LHAIGATTLD EYRKYIEKDA ALERRFQPVL VGEPSVEDTI AILRGLKEKY
EIHHGVRITD SALVAAAELS NRYISDRFLP DKAIDLMDEA ASRLRIEIDS MPEEVDLAER
KLTQMQIEEQ ALMKETDEPS KERLEALRKE ISQAREELDR QKAEWKNEKD VIVDVQSLKA
EIDSAQLEEE RATREGDLAR ASELRYGRIP ELQVKLKEAE ATLEARQEQG AILKEEVSEE
EIAEVVSTWT GIPVTKMMQG EMAKLVDLED RLHDRVVGQD EAVSAVAGAI RRNRAGLSDP
DRPIGSFLFL GPTGVGKTEL AKALAEYLFD SERAMVRIDM SEYMEKHSVA RLVGAPPGYV
GYDEGGQLTE AVRRKPYCVV LLDEIEKAHP DVFNILLQVL DDGRLTDGQG RVVSFKNAII
IMTSNVGSQS IRDFANANSN DSMGNVMEDL MKSDIATASK RLAELSNSIN DALRATFRPE
FLNRIDDVIT FNPLSIAAME PIVELQLKDV RHRLADRRVD LEVTPAAVER LAIDGYDPVY
GARPLRRLIQ REVVDRIATA IIEGKVNDGA HVVVDIDSDG NYATTIQSVS DHKAFEESVA
DVLDQADDIL GSAE
//