ID A0A261EQ67_9BIFI Unreviewed; 908 AA.
AC A0A261EQ67;
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 ORFNames=BOCO_1238 {ECO:0000313|EMBL:OZG49002.1};
OS Bombiscardovia coagulans.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bombiscardovia.
OX NCBI_TaxID=686666 {ECO:0000313|EMBL:OZG49002.1, ECO:0000313|Proteomes:UP000216004};
RN [1] {ECO:0000313|EMBL:OZG49002.1, ECO:0000313|Proteomes:UP000216004}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22924 {ECO:0000313|EMBL:OZG49002.1,
RC ECO:0000313|Proteomes:UP000216004};
RX PubMed=28764658; DOI=10.1186/s12864-017-3955-4;
RA Lugli G.A., Milani C., Turroni F., Duranti S., Mancabelli L.,
RA Mangifesta M., Ferrario C., Modesto M., Mattarelli P., Jiri K.,
RA van Sinderen D., Ventura M.;
RT "Comparative genomic and phylogenomic analyses of the Bifidobacteriaceae
RT family.";
RL BMC Genomics 18:568-568(2017).
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:OZG49002.1}.
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DR EMBL; MWWS01000007; OZG49002.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A261EQ67; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000216004; 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:UP000216004};
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 REGION 513..543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 883..908
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 398..492
FT /evidence="ECO:0000256|RuleBase:RU362034"
FT COMPBIAS 515..530
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 887..908
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 908 AA; 99179 MW; DD229746C2E531AA CRC64;
MEHNFTTMAQ EALGDAIQSA SAAGNPQVDT LHLLDSLIRQ QSGVVPSLLQ AVGADPQTIG
AAVRNALVAL PSASSASSAQ PSASRQLTKV LSDAEQEMRR MGDEYVSTEH LLIAIAEGDA
QASTILKQSG ATAETLRKAI PEIRGNAKVT SQDAEGTYKA LEKYSIDLTA QAKEGKLDPV
IGRDQEIRRV IQILSRRTKN NPVLIGEPGV GKTAVVEGLA QRIVAGDVPT GLEGKRLISL
DLSSMVAGSK YRGEFEERLK AVLNEIKAAN GQIITFIDEI HTIVGAGASE GSMDAGNMLK
PMLARGELRL IGATTLDEYR ENIEKDPALE RRFQQVFVGE PSVEDTIAIL RGLKQRYEAH
HKVTIGDDAL VAAATLSNRY ITGRQLPDKA IDLVDEAAAH LRMELDSQPE EIDELQRKVT
RLEMEEMQLK KADDLSSQDR LKKLQAELAD TKEKLSGLKS RWEQEKAGHN KVGDLRAQLD
ALRVEADKAT REGDLEKASR LLYGEIPTIR KQLAQAESEA DKDKTASGTE ADSSNEEQEP
MVPDHVDADS VAEIVADWTG IPVGRLMQGE NEKLLHMEDY LSKKVIGQSE AIQAVSDAVR
RSRAGISDPD RPTGSFMFLG PTGVGKTELA KALADFLFDD EKAMIRIDMS EYMEKASVSR
LIGAAPGYVG YEEGGQLTEA VRRRPYSVVL FDEVEKANPE VFDILLQVLD DGRLTDGQGR
TVDFKNTILI MTSNLGSQYL VDEQMDAEAQ HKAVMDMVHA SFKPEFINRL DDLIVFHPLT
REELGSIVDI QVQQVASRLT DRRITLDVSN SAREWLANMG YDPAYGARPL RRLVQTEVGD
QLARMLLAGK VHDGDTVLVD QTGGEHLELS AWSTDQLVAD DIQVDSVATD ESGQEQGGQQ
GATQHSQN
//