ID R6GK42_9FIRM Unreviewed; 868 AA.
AC R6GK42;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=BN704_00108 {ECO:0000313|EMBL:CDB24840.1};
OS Firmicutes bacterium CAG:552.
OC Bacteria; Bacillota.
OX NCBI_TaxID=1263029 {ECO:0000313|EMBL:CDB24840.1, ECO:0000313|Proteomes:UP000018403};
RN [1] {ECO:0000313|EMBL:CDB24840.1, ECO:0000313|Proteomes:UP000018403}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:552 {ECO:0000313|Proteomes:UP000018403};
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:CDB24840.1}.
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DR EMBL; CBDH010000003; CDB24840.1; -; Genomic_DNA.
DR AlphaFoldDB; R6GK42; -.
DR STRING; 1263029.BN704_00108; -.
DR Proteomes; UP000018403; 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:UP000018403};
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 415..495
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 868 AA; 97150 MW; 022F303771E8F61A CRC64;
MDANKLTQKA LEALQSAQNI AIENNNVQIM PEHLLYALID QQNGLIGQLI KKMGKSPDAL
LSGLDALISK IPAVSGSGRE PDKVYVAPLT DKILTAAERL AKSMNDDYTS VEHIMLCIFD
YADDGIRSLF RERGITKDDF VTQLKKVKTD RITSDNPENT YDVLSKYGFD LVERAKQHKL
DPVIGRDSEI RNVIRILSRK TKNNPVLIGE PGVGKTAIAE GLAMRIVQGD VPEGLKDKTI
FALDMGALVA GAKFRGEFEE RLKAVLNEVK KSEGRILLFI DELHTIVGAG KTDGAMDAGN
LLKPLLARGE LHCIGATTLD EYRKYIEKDA ALERRFQPVM VDEPNVEDTI SILRGLKERY
EVYHGVTIHD SALVAAATLS NRYITDRFLP DKAIDLVDEA CAMIRTEIDS MPTEMDEISR
KIMQLEIEET ALKKETDELS AARLAEIRKE LADLREKFGA MKAQWENEKQ NIHRVSDLKS
EIEKVNADIE KAQRNADYEH AAFLKYSTLP DLTKKLEEAQ KTEKTDKNTL LRDTVTEEEI
TKVVSRWTGI PLSKLMEGER EKLLHLPEVL HRRVIGQDEA VTKVSEAIMR SRAGIADPDR
PIGSFMFLGP TGVGKTELAK ALAECLFDDE HNLIRIDMSE YMEKFSVSRL VGAPPGYVGY
EEGGYLTEAV RRKPYSVVLF DEIEKAHPDV FNILLQVLDD GRITDSQGRT VDFKNTIIIL
TSNLGSNIIL EGIDSESGEI NDEAKERVSA LLKQSFRPEF LNRLDEIVYY KPLTKANITG
IIDLLIKSLA HRIEERRLHL EVTDAAKDVI IEGGYDPVYG ARPLKRYLQS KVETLLAKKI
LESDLEPNST LIVDAKDGAL TVNVKNQS
//
