ID A0A2T9XRR8_9CELL Unreviewed; 877 AA.
AC A0A2T9XRR8;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:PVU82778.1};
GN ORFNames=DDP54_06870 {ECO:0000313|EMBL:PVU82778.1};
OS Cellulomonas sp. WB94.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Cellulomonas.
OX NCBI_TaxID=2173174 {ECO:0000313|EMBL:PVU82778.1, ECO:0000313|Proteomes:UP000245142};
RN [1] {ECO:0000313|EMBL:PVU82778.1, ECO:0000313|Proteomes:UP000245142}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WB94 {ECO:0000313|EMBL:PVU82778.1,
RC ECO:0000313|Proteomes:UP000245142};
RA Anderson E., Ishii S., Jang J.;
RT "Cellulomonas - woodchip bioreactor.";
RL Submitted (APR-2018) 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|ARBA:ARBA00004496,
CC 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:PVU82778.1}.
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DR EMBL; QEES01000002; PVU82778.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T9XRR8; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000245142; 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};
KW Cytoplasm {ECO:0000256|RuleBase:RU362034};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Reference proteome {ECO:0000313|Proteomes:UP000245142};
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"
SQ SEQUENCE 877 AA; 94073 MW; C3C361F1C15C223D CRC64;
MDAKLTTKSQ EALGDAIQQA SAAGNPQLEP AHLLNALLAQ EGGVANGLLD AVGADRGALG
RAVRAALVAL PAASGSAVAQ PTASRATSTA IEAASSEARA LGDDYVSTEH LLLGVAAGRS
GVADALRTHG ASRDALLAVL PTVRGSGKVT SPNPEGTYKA LEQYGVDLTA AARDGKLDPV
IGRDAEIRRV VQVLSRRTKN NPVLIGEPGV GKTAVVEGLA QRIVAGDVPE SLRGKRLVSL
DLAAMVAGAK YRGEFEERLK AVLEEIKSSD GEIVTFIDEL HTVVGAGAAE GSMDAGNMLK
PMLARGELRL VGATTLDEFR QHIEKDPALE RRFQQVFVGE PSVEDTIAIL RGLKERYEAH
HKVAISDAAL VAAASLSDRY ISGRQLPDKA IDLIDEAASR LRMELDSSPV EIDQLRRAVD
RLKMEELALE NADDDASRER LGKLRADLAD RSEELASLTA RWENERAGHN RVGDLRAKLD
ELRIESDKAQ RDGDLATASR LLYGEIPAVE REIAEAEARE QRAGVEDAIG PVPEPMIAEK
VGPDEIAEVV SAWTGIPAGR LLEGESAKLL RMEDVLGQRL IGQRAAVASV SDAVRRARAG
ISDPDRPTGS FLFLGPTGVG KTELAKALAD FLFDDERAIV RIDMSEYSEK HSVARLVGAP
PGYVGYEEGG QLTEAVRRRP YSVVLFDEVE KAHPEVFDIL LQVLDDGRLT DGQGRTVDFR
NVILVLTSNL GSQFLVDPML DDAAKREAVM AAVHAAFKPE FLNRLDDVVL FDPLSLDELS
RIVEIQVKAL ADRLTDRRLT LDVTPAAREW LAIEGFDPAY GARPLRRLVQ REIGDRLARM
LLGGEARDGD TVRVDRAADG SGSLTLAVVA RPVASVA
//
