ID R6MQE5_9FIRM Unreviewed; 864 AA.
AC R6MQE5;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=BN515_02119 {ECO:0000313|EMBL:CDB88002.1};
OS Firmicutes bacterium CAG:170.
OC Bacteria; Bacillota.
OX NCBI_TaxID=1263006 {ECO:0000313|EMBL:CDB88002.1, ECO:0000313|Proteomes:UP000018279};
RN [1] {ECO:0000313|EMBL:CDB88002.1, ECO:0000313|Proteomes:UP000018279}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:170 {ECO:0000313|Proteomes:UP000018279};
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:CDB88002.1}.
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DR EMBL; CBEH010000286; CDB88002.1; -; Genomic_DNA.
DR AlphaFoldDB; R6MQE5; -.
DR Proteomes; UP000018279; 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:UP000018279};
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 416..503
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 864 AA; 96963 MW; F55CBFE12AF5C20F CRC64;
MNAEKYTQKS LEAVKAAQEL TIQNQNQQIE QAHLLAALLR QDGGLVPQLL KKMGVTVESL
DAAVGKELEK LPRVTGSGRE ADKFYVSRAV DTALNQAEKI AADMKDDYVS VEHLLLALIE
TADSTLKELF RTYRITKESC LQALQTVRGS QRVTTDSPED TYEALEKYGT DLVKRAREQK
MDPVIGRDDE IRNVIRILSR KTKNNPVLIG EPGVGKTAIV EGLAQRIVAN EVPKSLQDKS
VFSLDMGALI AGAKYRGEFE ERLKAVLNEV KKSEGRIILF IDELHTIVGA GKTEGSMDAG
NLLKPMLARG ELHCIGATTL DEYRQYIEKD PALERRFQTV LVQEPTVEDT IAILRGLESR
YEVFHGVKIT DNAIIAAATL SNRYITDRYL PDKAIDLIDE ACAMIRTEMD SMPTELDVIN
RKIIQMEIEE AALKNEEDEL SKGRLAELQK ELADQREKFS TMKAQWENEK NAIGRVQQLR
ERIESLNREI EAAQQNYDLE KAAKLMYGDL PEAKKQLEHE EKLAQSSKES SLLRNKVTEE
EIARIIERWT GIPTSRLMEG EREKLLRLPE ILHKRVIGQD EAVQCVSDAI LRSRAGIQDP
NRPLGSFLFL GPTGVGKTEL AKTLAEALFD DEKNLVRIDM SEYMEKFSVS RLIGAPPGYV
GYEEGGQLTE AVRRRPYSVI LFDEIEKAHP DVFNVLLQVL DDGRITDSQG RTVDFKNTII
ILTSNLGSQQ LLDGIGPDGE ITQSAKDAVE ALLHHTFRPE FLNRLDEIVF YKPLTKENIT
GIIDLQIAAL NKRLADKQLR CELTPAAKQY VIDAAYDPQF GARPLRRYVQ HTVETLLAKK
IVEGNIQPGA KITVDVENGE LALR
//