ID A0A143XS64_9FIRM Unreviewed; 862 AA.
AC A0A143XS64;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB1 {ECO:0000313|EMBL:CVI70734.1};
GN Synonyms=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=BN3660_02000 {ECO:0000313|EMBL:CVI70734.1};
OS Eubacteriaceae bacterium CHKCI004.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae.
OX NCBI_TaxID=1780380 {ECO:0000313|EMBL:CVI70734.1, ECO:0000313|Proteomes:UP000199324};
RN [1] {ECO:0000313|EMBL:CVI70734.1, ECO:0000313|Proteomes:UP000199324}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CHKC4 {ECO:0000313|EMBL:CVI70734.1};
RA Oliw E.H.;
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}.
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DR EMBL; FCNR01000048; CVI70734.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A143XS64; -.
DR STRING; 1780380.BN3660_02000; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000199324; 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:UP000199324};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..145
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 404..525
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 862 AA; 97062 MW; 91DA86115F955B72 CRC64;
MNINKFTQKS LEAVNQCEKL AYQYGNPEID QEHFLYSLLT IEDSLILKLI EKMEVNKEVF
LSQTQQLIEK KPKVSGGQVY ISKSLNEVLV SAEDESKAMG DEYVSVEHLF LSLLKHPNKE
IKKLFQAYGV TRERFLQALS TVRGNQKVVS DNPEATYETL EKYGYDLVER ARQQKLDPVI
GRDGEIRNVV RILSRKTKNN PVLIGEPGVG KTAVVEGLAQ RIVKGDVPES LKDKKVFALD
MGSLVAGAKY RGEFEERLKA VLEEIKASDG QILLFIDELH TIVGAGKTEG AMDAGNLLKP
MLARGELHCI GATTLNEYRQ YIEKDAALER RFQPVMVDEP TVEDTISILR GLKDRYEVYH
GVKITDSALV SAAVLSNRYI SDRFLPDKAI DLVDEACAMI KTELDSLPTE LDEVQRKIMQ
LEIEEAALKK ETDRLSQERL ADLQKELAQM REDFQIQKAT WDQEKSAVER VSKIKEEIEA
LNNEIQIAQR NYDLNKAAEL QYGKLPELQK QLAEEEEKAK RDDASLVHES VTDEEIAKII
SRWTGIPVAK LTESERNKTL NLDKELHKRV VGQDEGVEKV TEAIIRSKAG IKDPTKPIGS
FMFLGPTGVG KTELAKALAE SLFDNEQNMV RIDMSEYMEK YSVSRLIGAP PGYVGYEEGG
QLTEAVRRKP YSVVLFDEIE KAHPDVFNVL LQVLDDGRIT DSQGRTVDFK NTILIMTSNI
GSQYLLDGIG EDGSIRPEAE DMVMNDLRAH FRPEFLNRLD EIIMFKPLTK DNIGGIIELM
LSDVNKRLAD RELSIELSDA AKDFVIEHGY EPAYGARPLK RFLTKHVDTL AARLILEGNV
REGDVILIDE QGGKLMASVK GQ
//
