ID A0A1Y4I122_9FIRM Unreviewed; 876 AA.
AC A0A1Y4I122;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=B5F35_07505 {ECO:0000313|EMBL:OUP12730.1};
OS Anaeromassilibacillus sp. An200.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Anaeromassilibacillus.
OX NCBI_TaxID=1965587 {ECO:0000313|EMBL:OUP12730.1, ECO:0000313|Proteomes:UP000195336};
RN [1] {ECO:0000313|Proteomes:UP000195336}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An200 {ECO:0000313|Proteomes:UP000195336};
RA Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA Rychlik I.;
RT "Function of individual gut microbiota members based on whole genome
RT sequencing of pure cultures obtained from chicken caecum.";
RL Submitted (APR-2017) 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:OUP12730.1}.
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DR EMBL; NFJU01000011; OUP12730.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y4I122; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000195336; 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:UP000195336};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..150
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 87..114
FT /evidence="ECO:0000256|RuleBase:RU362034"
FT COILED 416..503
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 876 AA; 98964 MW; 91D196D068EC58B8 CRC64;
MNAQKFTQKS LEAIQEAQNL ALRHNSMQIE QEHLLAALLE QENGLIPQLM KKMEVDPAAL
QRELENRIDK MPGVTGPGRE PGKIYVSGDV DRALSEAEQQ ADRMKDEYVS VEHIFLSLLE
HANQGLREVF RTFGIDKNKF LSALSAVRGN TRVTSDTPEE TYDALTKYAQ DLVQLARNQK
LDPVIGRDSE IRNVIRILSR KTKNNPVLIG EPGVGKTAIA EGLALRIVRG DVPNNLKNRK
LFSLDMGALI AGAKFRGEFE ERLKAVLNEV KKSEGQIILF IDELHTIVGA GKTEGSMDAG
NLLKPMLARG ELHCIGATTL DEYHKYIEKD AALERRFQPV MVDEPTVADT ISILRGLKER
YEVFHGVKIQ DQALIAAATL SNRYITDRFL PDKAIDLVDE ACAMVRTEID SMPTELDEIS
RRIMQYEIEE AALKKETDHL SQEHLAEIQK EMAELRSQFN EMKAKWENEK DAIGKVQKLR
SEIEATNAEI EKAERTYDLN KAAELKYGKL PALTKELQEE ERIAEEGQKS GSLLRDRVTE
EEIARIIGRW TGIPVSRLME GEREKLLRLP EILHERVIGQ DEAVDRVADA ILRSRAGIQD
PDRPIGSFLF LGPTGVGKTE LAKALAQALF DDEKNMVRID MTEYMEKYSV SRLIGAPPGY
VGYEEGGQLT EAVRRHPYCV VLFDEVEKAH PDVFNVLLQV LDDGRITDSQ GRTVDFKNTI
IILTSNLGSQ IILDGIGDNG EINPEAREHV QALLKQQFRP EFLNRLDEIV FYKPLRREEI
FSIVDLMIRD LQRRLEEKQL TVELTDAAKD LIVEQGFDPV YGARPLKRYL QSHVETLIAK
LIIRDDPMPR THIVVDAENG ELTLHTVLPA EMVSTK
//
