ID A0A2A9D4P9_9MICO Unreviewed; 875 AA.
AC A0A2A9D4P9;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=ATL40_2444 {ECO:0000313|EMBL:PFG20829.1};
OS Serinibacter salmoneus.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Beutenbergiaceae;
OC Serinibacter.
OX NCBI_TaxID=556530 {ECO:0000313|EMBL:PFG20829.1, ECO:0000313|Proteomes:UP000224915};
RN [1] {ECO:0000313|EMBL:PFG20829.1, ECO:0000313|Proteomes:UP000224915}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21801 {ECO:0000313|EMBL:PFG20829.1,
RC ECO:0000313|Proteomes:UP000224915};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (OCT-2017) 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:PFG20829.1}.
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DR EMBL; PDJD01000001; PFG20829.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A9D4P9; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000224915; 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:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0042026; P:protein refolding; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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};
KW Cytoplasm {ECO:0000256|RuleBase:RU362034};
KW Hydrolase {ECO:0000313|EMBL:PFG20829.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:PFG20829.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000224915};
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 875 AA; 94072 MW; 02BB11FCF8FC4A9A CRC64;
MNDKLTTKSQ EAIAAALQSA TQAGNPHLEP VHLLGALLQQ ADGIAVALLR AVGADPQAIA
QRTAGALATL PSASGGTTAQ PTASRGLSNA LTQAGEEARA LGDDYVSTEH LLLALAASST
STGEILTHAG ASRDALAAAL PQVRGGRRVT SPDPEGTFQS LEKYGQDLTA RAREGKIDPV
IGRDSEIRRV VQVLSRRTKN NPVLIGEPGV GKTAVVEGLA QRIVDGDVPE SLRDKRLIAL
DLGSMIAGAK YRGEFEERLK AVLEEITQSD GEVVTFIDEL HTVVGAGASE GAMDASNMLK
PMLARGELRM IGATTLDEFR ENIEKDPALE RRFQQVFVGE PSVEDTVAIL RGIAPRYEAH
HKVTISDGAL VAAATLSDRY ITARQLPDKA IDLVDEAASR LRMELDSSPT EIDVLRRTVD
RLTMEEAYLA DGPGGGADDE ATAERLEKLR RDIADRSEEL AALNARWEQE KAGHNRVGDL
RVRLDELRTQ FEIAMRDGNY ETAGRLANGE IPAIEREIAE AERAEAEGSE SAEGALPHTA
PMIADKVGPD EIAEVVAAWT GIPAGRLLEG ETAKLLRMEE VLGERLIGQA GAVAAVSDAV
RRSRAGIADP DRPTGSFLFL GPTGVGKTEL AKSLADFLFD DERAMVRIDM SEYAEKHAVA
RLVGAPPGYV GYEEGGQLTE AVRRRPYSVV LLDEVEKAHP EVFDILLQVL DDGRLTDGQG
RTVDFRNVIL VLTSNLGSQA LVDPNLDEAT KRESVMAAVR AAFRPEFLNR LDDVVIFDAL
SVEELGSIVD LQVERLAARL ADRRIALEVT PAAREWLALE GYDPAYGARP LRRLVQREIG
DRLARRLLAG EVADGSRVLV DRAEGEAPGL EVRGA
//