ID D1Y7Z7_9BACT Unreviewed; 869 AA.
AC D1Y7Z7;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:EFB89574.1};
GN ORFNames=HMPREF7215_0268 {ECO:0000313|EMBL:EFB89574.1};
OS Pyramidobacter piscolens W5455.
OC Bacteria; Synergistota; Synergistia; Synergistales;
OC Dethiosulfovibrionaceae; Pyramidobacter.
OX NCBI_TaxID=352165 {ECO:0000313|EMBL:EFB89574.1, ECO:0000313|Proteomes:UP000006462};
RN [1] {ECO:0000313|EMBL:EFB89574.1, ECO:0000313|Proteomes:UP000006462}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W5455 {ECO:0000313|EMBL:EFB89574.1,
RC ECO:0000313|Proteomes:UP000006462};
RA Shrivastava S., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Strausberg R.L., Nelson K.E.;
RL Submitted (DEC-2009) 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:EFB89574.1}.
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DR EMBL; ADFP01000127; EFB89574.1; -; Genomic_DNA.
DR RefSeq; WP_009165978.1; NZ_ADFP01000127.1.
DR AlphaFoldDB; D1Y7Z7; -.
DR STRING; 352165.HMPREF7215_0268; -.
DR eggNOG; COG0542; Bacteria.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000006462; 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 Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..149
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 50..106
FT /evidence="ECO:0000256|RuleBase:RU362034"
FT COILED 415..529
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 869 AA; 96296 MW; 5FBF478D612466E4 CRC64;
MNLNKLTQKS QEALSEAQNL AISHGHQEVD VEHLTLALLS QKDGLIPSIL EKLGANAAAL
GARLDQLLER KPRITGGYDK DRIYLSQNLS KVLTDAEKRA QALGDEYVSV EHLFAAILDL
PQHPVAKLLA ESGVGADAFL KALESVRGGA RVQSANPEET YEALKKYGVD LVEYARSDKL
DPVIGRDDEI LRVIQILSRK TKNNPVLIGE PGVGKTAIVE GLAQRILKGD VPEDLKNRTV
FSLDMGSLIA GAKYRGEFEE RLKAVINEVK RSEGRVILFI DEIHTIVGAG RTEGSMDAGN
LLKPMLARGE LHCIGATTID EYRKNIEKDA ALERRFQPVM VDPPSQEDAI SILRGLKDRF
QVYHGVRITD GAIVAAVTLS DRYISDRFLP DKAIDLIDEA CAMVRTEINS MPSELDGVSR
KVVRLEIEEA ALKKEKDDAS AARLAELQKE LSDLKDRQKE LTARYNSEKE KLTEVQQLRQ
KIEATKHDVE TAERQYDLNK AAELQHGVLP QLQKELKEKE AALRGASGDG SLLRESVTEN
EISRIVSDWT GIPVTKLMEG EREKLLHLDD ELHKGVIGQD EAVSLVADAI MRARAGIKDP
RRPIGSFIFL GPTGVGKTEL AKTLARTLFD SEDNMIRIDM SEYMEKYSVS RLLGAPPGYV
GYDEGGQLTE AVRSKPYSVI LFDEIEKAHP DVFNVMLQIL DDGRVTDSHG RTVDFKNTVI
IMTSNLGSEL LLEGVRDGTI PPDVRDGVMD LLKSRFRPEF LNRVDDIVLF SPLDKAQLHK
IVKLILNDLA KRLGERRIAL NVSDAALDFI TEHGYDPVFG ARPLKRYISH NVETLVARYL
IANSVVEGAT LSIDVQGDRL ALSAQPPRE
//
