ID A0A255H0I8_9ACTN Unreviewed; 882 AA.
AC A0A255H0I8;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:OYO21240.1};
GN ORFNames=CGZ93_10770 {ECO:0000313|EMBL:OYO21240.1};
OS Enemella dayhoffiae.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Enemella.
OX NCBI_TaxID=2016507 {ECO:0000313|EMBL:OYO21240.1, ECO:0000313|Proteomes:UP000216311};
RN [1] {ECO:0000313|EMBL:OYO21240.1, ECO:0000313|Proteomes:UP000216311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NML 130396 {ECO:0000313|EMBL:OYO21240.1,
RC ECO:0000313|Proteomes:UP000216311};
RA Bernier A.-M., Bernard K., Domingo M.-C.;
RT "Draft whole genome sequences of clinical Proprionibacteriaceae strains.";
RL Submitted (JUL-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:OYO21240.1}.
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DR EMBL; NMVQ01000019; OYO21240.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A255H0I8; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000216311; 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:UP000216311};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..147
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT REGION 857..882
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 413..500
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 882 AA; 95943 MW; 7EFE682CC5CBB932 CRC64;
MDTSKLTTMS RDAVSAAVRT ALTEGNPQAE PEHLLLALLS IPGNPSAALL SQVGADPKVV
ESAAQGAIKK LPSSQGSSVS NPTMSGALAR VHAEAENLAQ KLGDKFVSTE HLLIALAKVK
SNAQTILNQL GVTADKLTKA FNDARGDKRI TSPEAEGSSG ALDQYSIDLT EVARSGKLDP
VIGRDSEIRR VVQVLSRRTK NNPVLIGEPG VGKTAVVEGL AQRIVAGDVP DSLKGRKLVS
LDLGAMIAGA KYRGEFEERL KAVLTEIKEA EGQIITFIDE LHTVIGAGKA EGSMDAGNML
KPMLARGELR MIGATTLDEY RENIEKDPAF ERRFQQVYVG EPSVEDTIAI LRGLRERYEA
HHKVAITDGA LVAAASLSNR YITSRQLPDK AIDLIDEAAS RLRMEIDSSP EEIDQLRRNV
DRMTMQQLAL AKEDDPASKE RLARLEEELA NAQEELRALE ARWEAEKTGL NKVGELKQQI
DELRSEAERA QREGDLQRAS ELLYGQIPAL QKQLEKADAE EAEAKPMVSE EVTASDIAEV
VSAWTGVPVG RLMQGESEKL LSMESHLGQR LIGQKAAVAA VSDAVRRSRA GISDPNRPTG
SFLFLGPTGV GKTELAKSLA EFLFDDEQAM VRIDMSEYSE KHSVSRLVGA PPGYVGYEQG
GQLTEAVRRR PYTVVLLDEV EKANPEVFDI LLQVLDDGRL TDGQGRTVDF RNTILILTSN
LGSQFLADPK LDAKTKSDAV MEVVRKSFKP EFLNRLDEVV MFDPLGIEDL TSIVDINLKR
LNERMADRRI KVEVTDAGKE WLAMTGFDPV YGARPLRRLI QNTIEDALAR KVLAGEILEG
DTVTFDREAG DGDGLVIVGE SSGDGARAAT SDTNRADEMS DS
//