ID A0A512PC69_9CELL Unreviewed; 867 AA.
AC A0A512PC69;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:GEP68803.1};
GN ORFNames=CSO01_15180 {ECO:0000313|EMBL:GEP68803.1};
OS Cellulomonas soli.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Cellulomonas.
OX NCBI_TaxID=931535 {ECO:0000313|EMBL:GEP68803.1, ECO:0000313|Proteomes:UP000321798};
RN [1] {ECO:0000313|EMBL:GEP68803.1, ECO:0000313|Proteomes:UP000321798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 109434 {ECO:0000313|EMBL:GEP68803.1,
RC ECO:0000313|Proteomes:UP000321798};
RA Hosoyama A., Uohara A., Ohji S., Ichikawa N.;
RT "Whole genome shotgun sequence of Cellulomonas soli NBRC 109434.";
RL Submitted (JUL-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:GEP68803.1}.
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DR EMBL; BKAL01000004; GEP68803.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A512PC69; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000321798; 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:UP000321798};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 1..146
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 442..493
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 867 AA; 92587 MW; 3EA0F1ABF52188C9 CRC64;
MDAKFTTRSQ AALGDAIQQA SAAGNPQVEP AHVLNALLAQ DGGVAVGLLD AVGADRTALG
RAVRAALMNL PASSGDTVSQ PVASRQLNTA IQAASSEARA LGDDYVSTEH LLLGLAAGQS
GIADALRGAG ASRDALAAAL PAVRGSAKVD SPNPEGTYKA LEKYSIDLTQ SARDGKLDPV
IGRDAEIRRV IQVLSRRTKN NPVLIGEPGV GKTAVVEGLA QRIVAGDVPE SLRGKRLVSL
DLAAMVAGAK YRGEFEERLK SVLKEITESE GQIVTFIDEL HTVVGAGGGS EGAMDAGNML
KPMLARGELR LVGATTLDEY RERIEKDPAL ERRFQQVFVG EPSVEDTVAI LRGLKARYEA
HHKVTIADSA LVAAAALSDR YITGRQLPDK AIDLVDEAAS RLRMELDSSP VEIDALQRAV
TRLEMEEVVL SEATDPGSAE RLAKLRADLA DRREELAGLT ARWEKEKAGH NRVGDLRVRL
DQLRADAERA QREGDLAAAG RLLYGEIPTV EKEIAAAEAT EADADAVAET TPMIAENVGP
DEIAEVVSAW TGIPAGRLLE GESAKLLRME DVLGERLIGQ KPAVAAVSDA VRRARAGISD
PDRPTGSFLF LGPTGVGKTE LAKALADFLF DDERAMVRID MSEYSEKHTV ARLVGAPPGY
VGYEEGGQLT EAVRRRPYGV VLLDEIEKAH PEVFDILLQV LDDGRLTDGQ GRTVDFRNVI
LVLTSNLGSQ FLVDPLLDAT AKKDAVMAAV RGAFKPEFLN RLDDVVLFDP LSLAEIGEIV
ELQVAALGTR LADRRLTLEV SPAAREWLAL EGYDPAYGAR PLRRLVQREI GDQLARRLLA
GEIHDGQTVE VDLNADADAG GLVVSAR
//