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Database: UniProt
Entry: W7Y6E4_9BACT
LinkDB: W7Y6E4_9BACT
Original site: W7Y6E4_9BACT 
ID   W7Y6E4_9BACT            Unreviewed;       823 AA.
AC   W7Y6E4;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   24-JAN-2024, entry version 49.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=JCM21142_41858 {ECO:0000313|EMBL:GAF03193.1};
OS   Saccharicrinis fermentans DSM 9555 = JCM 21142.
OC   Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Marinilabiliaceae;
OC   Saccharicrinis.
OX   NCBI_TaxID=869213 {ECO:0000313|EMBL:GAF03193.1, ECO:0000313|Proteomes:UP000019402};
RN   [1] {ECO:0000313|EMBL:GAF03193.1, ECO:0000313|Proteomes:UP000019402}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 21142 {ECO:0000313|EMBL:GAF03193.1,
RC   ECO:0000313|Proteomes:UP000019402};
RA   Starns D., Oshima K., Suda W., Iino T., Yuki M., Inoue J., Kitamura K.,
RA   Iida T., Darby A., Hattori M., Ohkuma M.;
RT   "Draft Genome Sequence of Cytophaga fermentans JCM 21142T, a Facultative
RT   Anaerobe Isolated from Marine Mud.";
RL   Genome Announc. 2:e00206-14(2014).
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:GAF03193.1}.
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DR   EMBL; BAMD01000019; GAF03193.1; -; Genomic_DNA.
DR   AlphaFoldDB; W7Y6E4; -.
DR   STRING; 869213.GCA_000517085_01425; -.
DR   eggNOG; COG0542; Bacteria.
DR   Proteomes; UP000019402; 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; 1.
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:UP000019402};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          1..105
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          364..489
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   823 AA;  92586 MW;  1B6DDDEEC57F7A9B CRC64;
     MIEVDDNVIP YLLNKLEASN FDSPLKAIID GYPRVSGGEP FLSRSTNEVL LKAKDYLKMF
     EDQYVSIEHI LLGLLKSKDP VANLLKDAGI SEKALIMSVK ELRNGAKVDS PTAEDSYNAL
     NRYAVNLIES ARSGKLDPVI GRDEEIRRVL QILSRRTKNN PILIGEPGVG KTAIGEGIAM
     RIVNGDVPDN LKSKLIYSLD MGALIAGAKY KGEFEERLKA VVKEVVASDG GIILFIDEIH
     TLVGAGKGEG AMDAANILKP ALARGDLRAV GATTLSEYQK YFEKDKALER RFQQVMVDEP
     DASSAISILR GLKERYETHH KVRIKDDAII AAVTLSKKYI TDRFLPDKAI DLIDEAAAKL
     RLEINSVPEE LDELDRKVKQ LEIEREAIKR EKDERKLELL SKELSELKDE RNNLRAKWQE
     EKSIVDEIQK YKSDIEQYKF DAEKAEREGL FEQVAELRYG KMKEAEERIE ELKNKLKDKQ
     SESAMIKEEV DSEDVAGVVS RWTGIPVTKM LKSEKEKLLS LEDELHKRVV GQEEAIAAVA
     DAIRRSRAGL QDEKRPVGSF IFLGMSGVGK TELAKTLASF LFDDENKMTR IDMSEFQERH
     SVSRLIGAPP GYVGYDEGGQ LTEAVRRKPY SVVLLDEIEK AHPDVFNVLL QVLDDGRLTD
     NKGRLVDFKN TIIIMTSNAG SHVIQQNYES LNVGNASEIM EKTKSEVFDL LRKTIRPEFL
     NRIDDIVMFA PLTKKEIEEI VLLQFNAIKK VLASKQVQIE ISKEAIQYIA NAGFDPLFGA
     RPIKRVLQKE VLNELSKRIL ADTIVKDKTI LVDCINNKLE FSN
//
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