ID A0A133QQF3_9BACT Unreviewed; 868 AA.
AC A0A133QQF3;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=HMPREF3226_00066 {ECO:0000313|EMBL:KXA45099.1};
OS Prevotella corporis.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=28128 {ECO:0000313|EMBL:KXA45099.1, ECO:0000313|Proteomes:UP000070533};
RN [1] {ECO:0000313|Proteomes:UP000070533}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MJR7716 {ECO:0000313|Proteomes:UP000070533};
RA Mitreva M., Pepin K.H., Mihindukulasuriya K.A., Fulton R., Fronick C.,
RA O'Laughlin M., Miner T., Herter B., Rosa B.A., Cordes M., Tomlinson C.,
RA Wollam A., Palsikar V.B., Mardis E.R., Wilson R.K.;
RL Submitted (JAN-2016) 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:KXA45099.1}.
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DR EMBL; LRQG01000002; KXA45099.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A133QQF3; -.
DR STRING; 28128.HMPREF3226_00066; -.
DR PATRIC; fig|28128.5.peg.64; -.
DR eggNOG; COG0542; Bacteria.
DR Proteomes; UP000070533; 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 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:UP000070533};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 9..150
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 409..527
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 868 AA; 97619 MW; 1F253FAD2697B063 CRC64;
MKGDLIMTFD KFTIKAQEAI QSAVNTAQRN GQQTIEPVHI LAGVMDKGKD VVNYVFQKLG
MNSQMVETAV QNEINHLPKV SGGEPYFSPE ANKVMQRTLD ISQKLGDEFV SIEPLLLALL
NVNSMASRLL KDAGCTEKDL KAAINDLRQG QKVQSQSGDE NYQALKKYAR NLVEDARAGK
LDPVIGRDEE IRRVLQILSR RTKNNPILIG EPGTGKTAIA EGLAGRIVRG DVPENLKNKQ
LYSLDMGALL AGAKYKGEFE ERLKSVIKEV TSSDGNIILF IDEIHTLVGA GGGEGAMDAA
NILKPALARG ELRAIGATTL NEYQKYFEKD KALERRFQTV IVDEPSELDA ISILRGLKER
YENHHKVRIQ DDACIAAVQL SERYISDRFL PDKAIDLMDE AAAKLRMERD SVPEELDEIS
RRLKQLEIER EAIKRENDAE KIAQLDKEIA DLKDQERSFR AKWEGEKALV NKIQQDKQEM
ENLKYEAERA EREGNYERVA EIRYSRLKEL NDDIAQIQLQ LQATQGGQAM IREEVTSDDI
AEVVSRWTGI PVTKMLQSDR EKLLHLEDEL HKRVIGQDEA ITAVANAVRR SRAGLQDPKK
PIASFIFLGT TGTGKTELAK ALADYLFNDE TMMTRIDMSE YQEKFSVSRL IGAPPGYVGY
DEGGQLTEAV RRKPYSVVLF DEIEKANPDV FNILLQVLDD GHLTDNKGRT VNFKNTIIIM
TSNLGSQYIQ QEFEKLADDN RQEIIDLTKA TVMDMLKKTI RPEFLNRIDE TIMFLPLTKA
EIAGVVRLQL ERAKAMLSPQ GFNLEWTDKA VEYLSGVGYD PEFGARPVKR AIQRYVLNDL
SKSLLAETVS RDKPIIIDSL GDGLIFKN
//