ID A0A101WTH1_9FIRM Unreviewed; 865 AA.
AC A0A101WTH1;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=APF81_18400 {ECO:0000313|EMBL:KUO78880.1};
OS Desulfosporosinus sp. BRH_c37.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfosporosinus.
OX NCBI_TaxID=1734396 {ECO:0000313|EMBL:KUO78880.1, ECO:0000313|Proteomes:UP000053148};
RN [1] {ECO:0000313|EMBL:KUO78880.1, ECO:0000313|Proteomes:UP000053148}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRH_c37 {ECO:0000313|EMBL:KUO78880.1};
RA Bagnoud A., Chourey K., Hettich R.L., De Bruijn I., Andersson A.F.,
RA Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT "Microbial metabolic network in the subsurface.";
RL Submitted (OCT-2015) 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:KUO78880.1}.
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DR EMBL; LOEW01000020; KUO78880.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A101WTH1; -.
DR Proteomes; UP000053148; 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 Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 5..149
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 414..528
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 865 AA; 97388 MW; 2F81B97CC5C0ABC5 CRC64;
MSFDTNRFTQ KSQEAITNAQ TISERNGNSL VEPEHLLLSL LEQGDGVVPQ VLTKLNMAVG
ALIQSIRQEI NRFPRISGGN VQISISPRLR TVLVSAHDEM ISFGDEYVST EHLLLALFEK
AGGATEQILK QAGLSREKLL QALREIRGTQ RVTSPNPEGT YAALEQFGLN LVQQARRGRL
DPVIGRDEEI RRVIQTLSRR TKNNPVLIGE PGVGKTAIVE GLAQRIVRGD VPEAIKDKQV
ISLDMGTLIA GAKYRGEFEE RLKAVLKEIQ GRDDVILFID ELHTVVGAGA AEGAMDASNM
LKPMLARGEL SMLGATTLAE YRKHIEKDAA LERRFQPIMV EAPSVEDTIS ILRGLKERYE
THHGVRITDG AIIAAAVLSD RYISDRFLPD KAIDLIDEAG ARMRMEITSD PYELDQIKRR
MMQLEIEREA LKKEKDDASK ERLAKIEEEL ANLKEERSGL DAQLLGEREI LARIQQLKEE
VDRSRTLMEQ AQQQLDYNKA AELQYGIIPN LEKDLKSIEQ TLQTKKNTLL KQEVVEQDIA
EIVATWTHVP VSKLMESEMQ KLVNMEDRIH QRVIGQEDAV RAVADAVRRA RAGLQDPNRP
LGSFLFLGPT GVGKTELARA LAEFLFDDEQ AMVRIDMSEY MEKHTVSRLI GAPPGYVGYE
EGGQLTEAVR RKPYSVILFD EVEKAHSDVT NVLLQLLDDG RLTDGQGRMI NFKNTVVILT
SNIASPSIQQ LTQRKAPLEE VRFSINEELR HHFRPEFLNR LDEVIIFHPL GREHIGQIVE
IQLGLLRQRL SERKLTLELS ARAREQIVNE GYDPVYGARP LKRVIQQRLQ NPLALKLLQG
EFKEGQQLRV DVDATGTYSF SSQKD
//