ID R9IIB9_9FIRM Unreviewed; 861 AA.
AC R9IIB9;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 56.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=C806_04160 {ECO:0000313|EMBL:EOS21513.1};
OS Lachnospiraceae bacterium 3-1.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=397288 {ECO:0000313|EMBL:EOS21513.1, ECO:0000313|Proteomes:UP000014188};
RN [1] {ECO:0000313|EMBL:EOS21513.1, ECO:0000313|Proteomes:UP000014188}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3-1 {ECO:0000313|EMBL:EOS21513.1,
RC ECO:0000313|Proteomes:UP000014188};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A., Xavier R., Elson C., Duck W., Walker B., Young S., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Lachnospiraceae bacterium 3-1.";
RL Submitted (APR-2013) 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:EOS21513.1}.
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DR EMBL; ASST01000026; EOS21513.1; -; Genomic_DNA.
DR AlphaFoldDB; R9IIB9; -.
DR STRING; 397288.C806_04160; -.
DR PATRIC; fig|397288.3.peg.4537; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_0_9; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000014188; 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:UP000014188};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..145
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 404..498
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 861 AA; 97071 MW; 5A0AF90A8732603F CRC64;
MNIQKFTQKS IEAINGCEKL AYEYGNQEIE QEHLLVSLLF QEDGLIPKLI EKMEINLEHF
TENAKNHLSK RVKVSGGQVY MGQNLNKVLV SAEDEAKKMG DEYVSVEHLF LTLLKYPNQG
LKEIFKEYGI TRERFLQALA TVRGNQRVVS DNPEATYDTL EKYGYDMVER AREQKIDPVI
GRDNEIRNAV RILSRKTKNN PVLIGEPGVG KTAVVEGLAQ RIVRGDVPEG LKDKRLFALD
MGALVAGAKY RGEFEERLKA VLDEIKSSDG QIILFIDELH TIVGAGKTDG AMDAGQLLKP
MLARGELHCI GATTLDEYRE YIEKDAALER RFQPVLVAEP TVEDTISILR GLKERYEVFH
GVKITDAALV SAAVLSNRYI SDRFLPDKAI DLVDEACALI KTELDSMPTE LDELQRRVMQ
MEIEEAALKK EEDRLSKDRL KVLQKELADL KNDFQSRKAQ WDNEKSSVEK VQRLREELEA
LNKEIAMAQQ NYDLEKAAEL QYGKKPDLQR QLEMEEEQVK KKDLSLVHEN VSEEEIAKII
SRWTGIPVAK LTESERNKTL HLDEELHKRV IGQEEGVTKV TEAIIRSKAG IKDPTKPIGS
FLFLGPTGVG KTELAKALAA SLFDDENNMV RLDMSEYMEK YSVSRLIGAP PGYVGYEEGG
QLTEAVRRKP YSVVLFDEVE KAHPDVFHVL LQVLDDGRIT DSQGRTVDFK NTILIMTSNL
GSSYLLEGIE DNGEIKPECE AAVMGELQNN FRPEFLNRLD EIILFKPLNK NDIGAIIHLL
MADLNKRLVD REVSVELTQE AQEFAVEHGY DPVYGARPLK RYLQKTVETL AAKLILANEV
GAGDTILIDV KNGSLAAECK K
//