ID C9LEY7_9BACT Unreviewed; 895 AA.
AC C9LEY7;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 24-JAN-2024, entry version 77.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:EEX72307.1};
GN ORFNames=GCWU000325_00769 {ECO:0000313|EMBL:EEX72307.1};
OS Alloprevotella tannerae ATCC 51259.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Alloprevotella.
OX NCBI_TaxID=626522 {ECO:0000313|EMBL:EEX72307.1, ECO:0000313|Proteomes:UP000003460};
RN [1] {ECO:0000313|EMBL:EEX72307.1, ECO:0000313|Proteomes:UP000003460}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51259 {ECO:0000313|EMBL:EEX72307.1,
RC ECO:0000313|Proteomes:UP000003460};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (SEP-2009) 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:EEX72307.1}.
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DR EMBL; ACIJ02000016; EEX72307.1; -; Genomic_DNA.
DR AlphaFoldDB; C9LEY7; -.
DR STRING; 626522.GCWU000325_00769; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_1_10; -.
DR Proteomes; UP000003460; 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:UP000003460};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 32..173
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 432..550
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 895 AA; 100381 MW; 7557B9C896CB982D CRC64;
MDANCQFVRL ITCGIKFGQR VVKLKKKDDM KFDNFTIKAQ EAVQQALNKA ERGGQQAVGT
IHLLLGVLEV GENVTQFLFG KMGVNLQQVA QNATQEAARL PRVSGGEPYL DREANAALTK
AVDIAKQMGD SFVGLEPMLL ALLITPSSTA QLLRDAGLTE DGLKKAIGEL RGGRKATSAS
SEETYQALAK FARNLVEEAR SGKLDPVIGR DEEIRRVLQI LSRRTKNNPI LIGEPGTGKT
AIVEGIAERI VRGDVPENLR EKQLFSLDMG ALLAGAKYKG EFEERLKSVV NEVVGSDGRI
ILFIDEIHTL VGAGKGEGAM DAANILKPAL SRGEIRTIGA TTLEEYQKYF EKDKALERRF
QTVTVDEPST EDAISILRGL KERYENHHKV RIQDDAIIAA VQLSHRYISD RFLPDKAIDL
MDEAAAKLRM ERDSQPEELD EITRRLRQLE IEREAIKREN DENKLAQLNK EIATLEEREK
NFRAKWEGER ELLNKIQENK KEMERLKFEA DRAEREGNYE RVAEIRYGKL QALQAEIDKI
QEDLKQRQGN EALVKEEVTA DDIADVVSRW TGIPVSRMLQ SEREKLVHLE AELHQRVIGQ
DEAITAVADA VRRSRAGLQD PKRPIGSFIF LGTTGVGKTE LAKALAEYLF NDESLMTRID
MSEYQEKFSV SRLVGAPPGY VGYEEGGQLT EAVRRKPYSV VLFDEIEKAH PDVFNILLQV
LDDGRLTDNK GRVVNFKNTI IIMTSNLGSG FIQSKFDEMR GKSESEQEHL LDETKEGVFE
MLKKTIRPEF LNRIDDIIMF QPLKKEEIRL IVRLQVAAIV NRLAEQGISL QVDDDAIAQI
AEAGFDPEFG ARPVKRSLQR LLLNDLSKSL LSGAIDKSRP IRVRAAGDAL SFSND
//