ID A0LEW2_SYNFM Unreviewed; 873 AA.
AC A0LEW2;
DT 12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT 12-DEC-2006, sequence version 1.
DT 24-JAN-2024, entry version 119.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN OrderedLocusNames=Sfum_0263 {ECO:0000313|EMBL:ABK15964.1};
OS Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB).
OC Bacteria; Thermodesulfobacteriota; Syntrophobacteria; Syntrophobacterales;
OC Syntrophobacteraceae; Syntrophobacter.
OX NCBI_TaxID=335543 {ECO:0000313|EMBL:ABK15964.1, ECO:0000313|Proteomes:UP000001784};
RN [1] {ECO:0000313|EMBL:ABK15964.1, ECO:0000313|Proteomes:UP000001784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10017 / MPOB {ECO:0000313|Proteomes:UP000001784};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.G.,
RA Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Kim E., Boone D.R., Brockman F., Culley D., Ferry J., Gunsalus R.,
RA McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J., Sieber J.,
RA Stams A.J.M., Worm P., Henstra A.M., Richardson P.;
RT "Complete sequence of Syntrophobacter fumaroxidans MPOB.";
RL Submitted (OCT-2006) 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}.
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DR EMBL; CP000478; ABK15964.1; -; Genomic_DNA.
DR RefSeq; WP_011697137.1; NC_008554.1.
DR AlphaFoldDB; A0LEW2; -.
DR STRING; 335543.Sfum_0263; -.
DR KEGG; sfu:Sfum_0263; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_0_7; -.
DR InParanoid; A0LEW2; -.
DR OMA; ERMKAVM; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000001784; 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:UP000001784};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..151
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 50..114
FT /evidence="ECO:0000256|RuleBase:RU362034"
FT COILED 417..497
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 873 AA; 98097 MW; AEA95B61F1120473 CRC64;
MDLNKLTIKS QEALKAAETK AIRYGHVEVD VEHLLLALLE QSQGLIPSLL RKMDVQVDRL
RERLEQELEK KPRVSGPGIE PGKVYITQRL NQLLIKAEEE AGRLKDEYVS VEHLLLAFIQ
EGGATPAGRL LQENRVGKDA FLQTLTSVRG NQRVTSASPE TTYEALQKYG RDLVQEARTN
KLDPVIGRDS EIRRVVRILS RKTKNNPVLI GEPGVGKTAI VEGLAHRIVR GDVPEGLKDK
AIFALDMGAL VAGAKYRGEF EERLKAVLQE IKESEGGILL FIDELHTIVG AGKAEGSMDA
GNMLKPMLAR GELHCIGATT LDEYRKYIEK DAALERRFQP VLVDQPTVED TISILRGLKE
RYEVHHGVKI QDSALVAAAV LSGRYITDRF LPDKAIDLVD EACAMIRTEI DSRPEELDEV
MRRVMQLEIE EVALKKEKDK ASQERLEALR KEIGELRART DAMSAQWEAE KQAIKKVQAI
REEIEKVRRD IEVAERQFDL QKVAELKHGL MPDLEKKLKT EEGGLSADPD GNRLLREEVT
EEEIAEIISR WTGIPVTRLV EGEREKLLRL DEVLHRRIVG QNEAVSLVAD AVIRARSGIK
DPRRPIGSFI FLGPTGVGKT ELGKALAEAL FDSEDNVVRI DMSEYMEKHA VSRLIGAPPG
YVGYEEGGQL TEAVRRKPYS VILFDEIEKA HPDVFNVLLQ LLDDGRLTDA QGRTVDFKNT
VVIMTSNIGS VYLLDGVTDD GQIKERAREQ VMSDLRRQFR PEFLNRVDDI VLFKPLTVGE
IEKIIDLLTK DLTRRLKDRR IELELTGQAR EFIARAGYDP VFGARPLKRF LQHNLETRIG
RALIAGDIPD GSTIRVDIQD GDLSVTHTVN ENE
//