ID A0A5D6W472_9FIRM Unreviewed; 857 AA.
AC A0A5D6W472;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 13-SEP-2023, entry version 13.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:TYZ21644.1};
GN ORFNames=FZ040_09590 {ECO:0000313|EMBL:TYZ21644.1};
OS Selenomonas sp. mPRGC5.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC Selenomonas.
OX NCBI_TaxID=2593411 {ECO:0000313|EMBL:TYZ21644.1, ECO:0000313|Proteomes:UP000323646};
RN [1] {ECO:0000313|EMBL:TYZ21644.1, ECO:0000313|Proteomes:UP000323646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=mPRGC5 {ECO:0000313|Proteomes:UP000323646};
RA Poothong S., Nuengjamnong C., Tanasupawat S.;
RT "Selenomonas sp. mPRGC5 and Selenomonas sp. mPRGC8 isolated from ruminal
RT fluid of dairy goat (Capra hircus).";
RL Submitted (AUG-2019) 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:TYZ21644.1}.
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DR EMBL; VTOY01000008; TYZ21644.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5D6W472; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000323646; 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:UP000323646};
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 857 AA; 95434 MW; BF1DA74E8737CCC8 CRC64;
MGQEKYTTKT MAALQSAQQL AAMRYHQEIT SAHVLLALAK EPEGLLATIF EDCQTDLPML
KASLEQVLNK IPSVKGSDRL GMGMDMVRVL GRAEALAGSM KDDYISTEHL LLAIVTDGSD
EVQAVCREFK LTKGGIQSSI KKNRKQNVTN ENPEEGYKSL EKYGRDLTEA ARHGKLDPVI
GRDEEIRRTV EILSRRTKNN PVLIGEPGVG KTAIVEGLAR RIVAGDVPES LKNKTLYSLD
MGALIAGAKF RGEFEERLKA VLGEIVKSDG QILLFIDEVH TVVGAGAGEG AMDAGNLLKP
MMARGELRCI GATTLNEYRK YIEKDSALER RFQPVMVGEP TVEDTISILR GLKERYEVHH
GVRIRDAALV SAAVLSDRYI SDRFLPDKAI DLVDEAAAKL RTEIESMPAP LDEIRRKIMQ
LEIEEQALKK ENDAASKEKL DSMAAEKAEL TQQEATLKSK WEGEKQAILR VRAIKKEIDE
VNSQMETAER SYDLNRLSEL KYGRLPELQK KLQEEEAAIG KQSKDEQLLK EEVGEEDIAK
VVSRWTGIPV AKMMTGEREK LLHLEEVLHT RVVGQDEAVS SVSEAILRAR AGIKDPNRPI
GSFIFLGPTG VGKTELAKTL AESLFDDERS MIRIDMSEYM EKHSVSRLIG APPGYVGYDE
GGQLTEAVRR RPYSVILLDE IEKAHRDVFN VLLQILDDGR LTDGKGRVVN FKNTVIIMTS
NLGSHEILNK DYEEAKKAVD GILKEYFRPE FLNRVDDIIV FKALAKEQVK NIAAILLQKL
GERLQKQVKI TLGWNEAALD ALAEQGFEPN FGARPLRRLL VHTVETALSK EIIKGEVQEG
DTVNIGFLNG TFTFEKA
//