ID R5CSG4_9FIRM Unreviewed; 859 AA.
AC R5CSG4;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=BN705_01703 {ECO:0000313|EMBL:CCX70870.1};
OS Firmicutes bacterium CAG:555.
OC Bacteria; Bacillota.
OX NCBI_TaxID=1263030 {ECO:0000313|EMBL:CCX70870.1, ECO:0000313|Proteomes:UP000018402};
RN [1] {ECO:0000313|EMBL:CCX70870.1, ECO:0000313|Proteomes:UP000018402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:555 {ECO:0000313|Proteomes:UP000018402};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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:CCX70870.1}.
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DR EMBL; CAWW010000016; CCX70870.1; -; Genomic_DNA.
DR AlphaFoldDB; R5CSG4; -.
DR STRING; 1263030.BN705_01703; -.
DR Proteomes; UP000018402; 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:UP000018402};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..146
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 411..525
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 859 AA; 96002 MW; 30511B9622C985C0 CRC64;
MNAQNFTQKT IETIQTAQSM AQENQNQYIT PEHILYALVD QDGGLIPSLL GKMGVDCNTV
LAELDTAIAA LPKVTGDTDV YLSREADRVM QAAEKSAKSL GDEYLSVEHL MIGIFAAATP
AVKRILADHG ITKSAFTAEL AKVKNGPVTS DNPENTYDAL KKYGTDLVER ARKQELDPVI
GRDNEIRNVV RILSRKTKNN PVLIGEPGVG KTAIAEGLAQ RIVRGDVPEG LKDKTIFSLD
MGALIAGAKY RGEFEERLKA VLEEIKQSEG KIILFIDELH TIVGAGKTEG SMDAGNLLKP
MLARGELHCI GATTLDEYRK YIEKDAALER RFQPVMVDEP TVEDTISILR GLKERYEVYH
GVRIHDNALV AAATLSDRYI TDRFLPDKAI DLVDEACALI RTEIDSMPAE LDDVRRKIMQ
LEIEEMALKK ETDRLSMERL EKLSEELANL KDKFKEQKSR WESEKSSVDE VKNLKAEIEK
MHADIENAQL RYEYETAAKL KYSDLPALER KLQEAEKNSE ERKSNSMVHD TVTEEEIAGI
VAKWTGIPVA KLMEGEREKL LHLDDVLHRR VIGQDEAVQK VTEAIWRSRA GIADPNRPIG
SFMFLGPTGV GKTELAKALA ECLFDDEHNI VRIDMTEYME KFSVSRLIGA PPGYVGYDEG
GQLTEAVRRK PYSVVLFDEI EKAHPDVFNI LLQILDDGRI TDSQGRTVDF KNTIIIMTSN
LGSQYLLDGI DDDGNITEDA KNSVFGELRR QFRPEFLNRL DEIICFKPLT KTELNGIIDI
LTESLKKRLA DKTLGLEITD AAKQLIIERG FDPVFGARPL KRYLQASVET LIAKTILSGE
MEAGHVITID VENGELVCK
//
