ID A0A3A9GPC6_9FIRM Unreviewed; 862 AA.
AC A0A3A9GPC6;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:RKJ66800.1};
GN ORFNames=D7Y06_06550 {ECO:0000313|EMBL:RKJ66800.1};
OS Roseburia sp. 1XD42-69.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Roseburia.
OX NCBI_TaxID=2320088 {ECO:0000313|EMBL:RKJ66800.1, ECO:0000313|Proteomes:UP000279120};
RN [1] {ECO:0000313|EMBL:RKJ66800.1, ECO:0000313|Proteomes:UP000279120}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1XD42-69 {ECO:0000313|EMBL:RKJ66800.1,
RC ECO:0000313|Proteomes:UP000279120};
RA Liu C.;
RT "Murine metabolic-syndrome-specific gut microbial biobank.";
RL Submitted (SEP-2018) 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:RKJ66800.1}.
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DR EMBL; RAZG01000009; RKJ66800.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3A9GPC6; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000279120; 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:UP000279120};
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..498
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 862 AA; 97038 MW; 69CD10CBFF3FAC91 CRC64;
MNIHKFTQKS VEAINDCEKL AYEYGNQEIE QEHLLLALLR QQDGLIQKMI EKMEINKEHF
MDNAVRHLEK RVKVSGGQIY MGQALNKVLI SAEDEAKAMG DEYVSVEHLF LSMIKYPNPA
LKEIFKEYGI TRDRFLTALS TVRGNQRVTT DNPEATYDTL EKYAYDLVER ARNQKLDPVI
GRDGEIRNVV RILSRKTKNN PVLIGEPGVG KTAVVEGLAQ RIVRGDVPEG LKDKKLFALD
MGALVAGAKY RGEFEERLKA LLDEVKKSDG QIILFIDELH TIVGAGKTDG AMDAGNMLKP
MLARGELHCI GATTLDEYRQ YIEKDAALER RFQPVMVEEP TVEDTISILR GLKERYEVFH
GVKIADSALV SAAVLSNRYI SDRFLPDKAI DLVDEACALI KTELDSMPSE LDELNRRVMQ
LEIEETALKK EEDTLSKNRL ATLQKELAEL RDEFSSKKAQ WDNEKNSVEH VQKLREDLEN
VKNEIKQAQQ NYDLEKAAEL QYGKLPSIQK ALEAEETRVK SEEYSLVHEN VSEEEIARII
SRWSGIPVAK LTESERNKTL HLDEELHRRV VGQDDGVTKV SEAIIRSKAG IKDPGKPIGS
FLFLGPTGVG KTELAKALAE SLFDDESNMV RLDMSEYMEK YSVSRLIGAP PGYAGYDEGG
QLTEAVRRKP YSVVLFDEVE KAHPDVFNVL LQVLDDGRIT DSQGRTVDFK NTIIIMTSNL
GSAHLLEGMD ENGSIRPEAE EAVMQELRGS FRPEFLNRLD EIIMFKALTK DNIGNIIHLL
MEELNSRVKD KGIQVELSPA AEDYIVENGY DPVYGARPLK RFLQKYVETL SAKIILGDQV
KGGDTIYIDT VNGELSASVR NG
//
