ID C8VYG1_DESAS Unreviewed; 863 AA.
AC C8VYG1;
DT 03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 03-NOV-2009, sequence version 1.
DT 24-JAN-2024, entry version 93.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN OrderedLocusNames=Dtox_2007 {ECO:0000313|EMBL:ACV62842.1};
OS Desulfofarcimen acetoxidans (strain ATCC 49208 / DSM 771 / KCTC 5769 / VKM
OS B-1644 / 5575) (Desulfotomaculum acetoxidans).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC Desulfofarcimen.
OX NCBI_TaxID=485916 {ECO:0000313|EMBL:ACV62842.1, ECO:0000313|Proteomes:UP000002217};
RN [1] {ECO:0000313|EMBL:ACV62842.1, ECO:0000313|Proteomes:UP000002217}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49208 / DSM 771 / VKM B-1644
RC {ECO:0000313|Proteomes:UP000002217};
RX PubMed=21304664; DOI=10.4056/sigs.39508;
RA Spring S., Lapidus A., Schroder M., Gleim D., Sims D., Meincke L.,
RA Glavina Del Rio T., Tice H., Copeland A., Cheng J.F., Lucas S., Chen F.,
RA Nolan M., Bruce D., Goodwin L., Pitluck S., Ivanova N., Mavromatis K.,
RA Mikhailova N., Pati A., Chen A., Palaniappan K., Land M., Hauser L.,
RA Chang Y.J., Jeffries C.D., Chain P., Saunders E., Brettin T., Detter J.C.,
RA Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P., Han C.;
RT "Complete genome sequence of Desulfotomaculum acetoxidans type strain
RT (5575).";
RL Stand. Genomic Sci. 1:242-253(2009).
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}.
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DR EMBL; CP001720; ACV62842.1; -; Genomic_DNA.
DR AlphaFoldDB; C8VYG1; -.
DR STRING; 485916.Dtox_2007; -.
DR KEGG; dae:Dtox_2007; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_0_9; -.
DR OMA; GPEHILM; -.
DR Proteomes; UP000002217; Chromosome.
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:UP000002217};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 1..145
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 411..525
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 863 AA; 97253 MW; E7CCCFCAEA930DA2 CRC64;
MNRFTKKSAE ALSAAQQFTA SRHHQEITGK HLLAVLLTQE EGMIPRILEH AGVSTDLLST
KIEENLKKIP VIRGYDGTLH MGTGLARAIA RAEKEARDMK DDYVSVEHLL LGLLYEGEQD
TKEVLRQVGL TLDALLKSLR EVRGNQRVTS DSPEDTYEAL ERYGRDITKL AREGKLDPVI
GRDNEIRRLM EILSRRTKNN PVLIGEPGVG KTAIAEGLAR RIVTGDIPEG LKDKILIELD
MGALVAGAKY RGEFEERLKA VLKEVQNSQG RIIMFIDELH TVVGAGAAEG AMDAGNLLKP
MLARGELRTI GSTTLDEYRK HIEKDAALER RFQPVIVNPP SIEDTISILR GLKERYEIHH
GVRIKDSALV EAAVLSDRYI SDRFLPDKAI DLMDEAAAKL RTEIDSMPTD LDKITRRIMQ
LEVEEAALSK EKDQVSQERL EKLKEQLANL HSESDSMKAQ WQVEKQGISR LQQIKKEIEE
TKQEIERAER EYDLNRLAEL KYGRLNELER RLKSEEELLS GKQKYGMLLK EEVDEEDIAS
VVSRWTGIPV SKLMEGEKEK LIHLDEELHK RVIGQDEAVR AVADAVLRAR AGIKDPNRPI
GSFIFLGPTG VGKTELARSL AQALFDDEKN IIRLDMSEYM EKHTVSRLIG APPGYVGYDE
GGQLTEAIRR KPYSVILLDE IEKAHHDVFN VLLQLLDDGR LTDGQGRTVN FQNSVVIMTS
NLGSQEILNH QDQGGDYEQM KSGVLGILRQ HFRPEFLNRV DEVVVFHALN QPQVRKIAAI
LLEKLAERIN AGSGIKLEWS DDALNYLANK GYEPVYGARP LKRLIQQEVE TPFSRMLVKG
EIVPNQIVLL TIKEGELNFK IKS
//