ID R6KLD3_9CLOT Unreviewed; 866 AA.
AC R6KLD3;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 55.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=BN573_02083 {ECO:0000313|EMBL:CDB75973.1};
OS Clostridium sp. CAG:265.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1262787 {ECO:0000313|EMBL:CDB75973.1, ECO:0000313|Proteomes:UP000018277};
RN [1] {ECO:0000313|EMBL:CDB75973.1, ECO:0000313|Proteomes:UP000018277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:265 {ECO:0000313|Proteomes:UP000018277};
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:CDB75973.1}.
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DR EMBL; CBEC010000094; CDB75973.1; -; Genomic_DNA.
DR AlphaFoldDB; R6KLD3; -.
DR Proteomes; UP000018277; 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:UP000018277};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..151
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 417..497
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 866 AA; 97352 MW; C7977DF5AF01B908 CRC64;
MNVEKMTLRV QQALNDANLT AVKYSHQQID IIHLFSALLE QEDGLVPNIF TKMGINIKMM
KLDVASALER MPKVSGSGSE GAGPYITRDI DRVLIAADEI AKEFKDSYIS VEHLMLAILD
VDKKGSTKEI LNKYGVNKKS FMKVLQEVRG SQRVDTQDPE GTYDALAKYG TNLVELAKKH
KLDPVIGRDD EIRRTVRILS RRTKNNPVLI GEPGVGKTAI VEGLAERIVR GDVPEGLKDK
IIFSLDMGSL IAGAKYRGEF EERLKAVLKE VQNSEGRIIL FIDEIHTIVG AGKTDGAMDA
GNLIKPLLAR GELHCIGATT FDEYRQYIEK DKALERRFQP VIVDEPSVED AISILRGLKE
RFEIHHGVRI HDSALVAAAK LSDRYISDRY LPDKAIDLID EAGAMIRTEI DSLPSELDVV
RRKLMQLEIE KEALTKEKDE GSKKKLEALE KEYAELKGKN DEMTAKFERE KGSIDKLKEL
KSRLDDARGN LEQAQRNYDY NKAAEIQYSE IPSLEEAIKQ MEVEVKENYE GALLKEEVTE
EEVSQILSKW TGIPVSNLLE GEREKLLRLE DEMEKRVIGQ SEAVTAVTSA ILRARAGLKD
INRPIGSFIF LGPTGVGKTE LAKTLARNLF DSEENIIRID MSEYMEKHTV SRLVGAPPGY
VGYEEGGQLT EAVRRKPYSV ILFDEIEKAH EDVFNIFLQI LDDGRLTDNK GKTVDFKNTI
IIMTSNIGSN YLLENTSEES IDPSIRASVM DELKMRFKPE FLNRVDDIIM FKPLSESGIT
KIIDIFVGEV ANRLKDRNIT LEITPAAKHI LAVEGYDPVY GARPLKRFIQ NTLENNLARK
IISGDVHYGS HVIVDGHDDE IVIKSE
//