ID D3MSZ1_9FIRM Unreviewed; 864 AA.
AC D3MSZ1;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:EFD04688.1};
GN ORFNames=HMPREF0631_1011 {ECO:0000313|EMBL:EFD04688.1};
OS Peptostreptococcus anaerobius 653-L.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Peptostreptococcus.
OX NCBI_TaxID=596329 {ECO:0000313|EMBL:EFD04688.1, ECO:0000313|Proteomes:UP000004206};
RN [1] {ECO:0000313|EMBL:EFD04688.1, ECO:0000313|Proteomes:UP000004206}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=653-L {ECO:0000313|EMBL:EFD04688.1,
RC ECO:0000313|Proteomes:UP000004206};
RA Dodson R., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Strausberg R.L., Nelson K.E.;
RL Submitted (JAN-2010) 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:EFD04688.1}.
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DR EMBL; ADJN01000057; EFD04688.1; -; Genomic_DNA.
DR RefSeq; WP_002844048.1; NZ_ADJN01000057.1.
DR AlphaFoldDB; D3MSZ1; -.
DR GeneID; 79843064; -.
DR eggNOG; COG0542; Bacteria.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000004206; 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, 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 3..153
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 419..533
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 864 AA; 97547 MW; 908A5C1B45C8A24A CRC64;
MNADKMTLRV QNALNEAFNI AVSNNNQQLE PIHLLSALMV QEDGLIGSII DKMGIDRTSI
QNDIDDEVSK LPKVTGDGVN VTASVKINKI LIEAEKISGE FKDSYISVEH LFLAMINLES
SKGLSTSNVG KILKKYRIDK QSFLAVLHEI RGNQRVDSQD PEGTYDALSK YGTNLVKRAM
NNKLDPVIGR DDEIRRAIRI LSRRTKNNPV LIGEPGVGKT AIVEGLAQRI VKGDVPEGLK
DKIVFSLDMG SLIAGAKYRG EFEERLKAVL KEVEASEGKI ILFIDEIHTI VGAGKTEGSV
DAGNLIKPML ARGELNCIGA TTFDEYRKYI EKDKALERRF QPVIVDEPSV EDTISILRGL
KEKFEIHHGI RIHDNAIVAA AKLSDRYIQD RFLPDKAIDL IDEAGAMIRT EIDSLPTELD
IVRRRLFTLE TEREALKLEN DDKSKARLEE LEKELVTLRE ENDDMTAKYE KEKSRLTGAK
DIKQDLDDAK ALAEKYEREG DFNKAAELKY GKIPKLEEEL RLIEENIDSN EEYSLLKQEV
TEEEIADIIS KWTGIPIKKL VESEKEKLLR LEDKLHERVI GQDEPVRAVS DAILRSRAGL
SDQNRPLGSF IFLGPTGVGK TELAKTLARE LFDSEDSIIR LDMSEYMEKH SVSRLVGPPP
GYVGYEEGGQ LTEAVRRKPY SVILFDEIEK AHDDVFNMFL QILDEGRLTD NKGKTVDFKN
TLIIMTSNIG SDILLESKGK IDESVQKSVM DIMKFKFKPE FLNRVDDIIM FKPLMKEEVK
KIIDIFFESI KSKLKERDIE IEITDEAKDF IVDIAYDPVY GARPLKRYIN SNLETKLAKA
IISGQIKAHT KVKVDKLGED IQIV
//
