ID R9N6N5_9FIRM Unreviewed; 862 AA.
AC R9N6N5;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=C817_03249 {ECO:0000313|EMBL:EOS78728.1};
OS Dorea sp. 5-2.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Dorea.
OX NCBI_TaxID=1235798 {ECO:0000313|EMBL:EOS78728.1, ECO:0000313|Proteomes:UP000014211};
RN [1] {ECO:0000313|EMBL:EOS78728.1, ECO:0000313|Proteomes:UP000014211}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5-2 {ECO:0000313|EMBL:EOS78728.1,
RC ECO:0000313|Proteomes:UP000014211};
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 Dorea bacterium 5-2.";
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:EOS78728.1}.
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DR EMBL; ASTD01000063; EOS78728.1; -; Genomic_DNA.
DR RefSeq; WP_016219946.1; NZ_KE159794.1.
DR AlphaFoldDB; R9N6N5; -.
DR STRING; 1235798.C817_03249; -.
DR PATRIC; fig|1235798.3.peg.3419; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_0_9; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000014211; 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 Reference proteome {ECO:0000313|Proteomes:UP000014211};
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 411..525
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 862 AA; 97455 MW; 96AA1B376B74C40B CRC64;
MNINKFTQKS IQAVQGCERT AMEYGNQEIE QEHLLYALLT QEDSLILKLM EKMGIDKSLI
VNRTEEALRK RTKVQGGNQY IGQDLNKALI HAEDEAKQMG DEYVSVEHLF LSLLKHPNRE
LKAMFREMGI KRDDFLKALS TVRGNQRVTS DNPEDTYDTL NKYGSDLVER AREQKLDPVI
GRDSEIRNVI RILSRKTKNN PVLIGEPGVG KTAVAEGLAQ RIVRGDVPEG LKDKTIFSLD
MGALVAGAKY RGEFEERLKA VLEDVKNSDG RIILFIDELH TIVGAGKTDG AMDAGNMLKP
MLARGELHCI GATTLDEYRQ YIEKDAALER RFQPVLVDEP TVEDAISILR GLKERYEVFH
GVKITDSALV AAATLSERYI SDRFLPDKAI DLVDEACALI KTELDSMPTE LDELRRKIML
MEIEEAALKK EDDRLSRDRL EHLQQELAEY REEFAGKKAQ WDNEKIDVER VRKIREEIEQ
VNKDIEKAQQ SYDLNKAAEL QYGRLPQLQK QLEEQEVKVR DEDKSLVHEN VTDDEIGRIV
SRWTGIPVAK LNESERSKTL HLAEELHKRV IGQDEGVELV TEAIIRSKAG IKDPTKPIGS
FLFLGPTGVG KTELAKALAE SLFDDESNMV RIDMSEYMEK YSVSRLIGAP PGYVGYDEGG
QLTEAVRRKP YSVVLFDEVE KAHPDVFNVL LQVLDDGRIT DSQGRTVDFK NTILIMTSNI
GSSYLLEGID EQGNISGKSQ ELVMNDLRAH FRPEFLNRLD ETILFKPLTK ENIYHIIDLL
AADVNKRLAD REISIALTEE AKNYVVEGGY DPTYGARPLK RYLQKNVETL AARLMLRGDV
GAQDTILIDV ADGKLTALVK NR
//
