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Database: UniProt
Entry: L0FT13_ECHVK
LinkDB: L0FT13_ECHVK
Original site: L0FT13_ECHVK 
ID   L0FT13_ECHVK            Unreviewed;       870 AA.
AC   L0FT13;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 62.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   OrderedLocusNames=Echvi_0754 {ECO:0000313|EMBL:AGA77029.1};
OS   Echinicola vietnamensis (strain DSM 17526 / LMG 23754 / KMM 6221).
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC   Echinicola.
OX   NCBI_TaxID=926556 {ECO:0000313|EMBL:AGA77029.1, ECO:0000313|Proteomes:UP000010796};
RN   [1] {ECO:0000313|Proteomes:UP000010796}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17526 / LMG 23754 / KMM 6221
RC   {ECO:0000313|Proteomes:UP000010796};
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Teshima H.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA   Woyke T., Wu D., Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Echinicola vietnamensis DSM 17526.";
RL   Submitted (FEB-2012) 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; CP003346; AGA77029.1; -; Genomic_DNA.
DR   RefSeq; WP_015264595.1; NC_019904.1.
DR   AlphaFoldDB; L0FT13; -.
DR   STRING; 926556.Echvi_0754; -.
DR   KEGG; evi:Echvi_0754; -.
DR   PATRIC; fig|926556.3.peg.755; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_2_10; -.
DR   OMA; SKMMQGE; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000010796; 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:UP000010796};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          3..144
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          397..522
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   870 AA;  97619 MW;  65B24209B319EA99 CRC64;
     MDFKQFTIKS QEAIQKAAEL CMAEQQQAIE PAHVLKGILS EDESVVDFVF KKLGVNKKLV
     SQKLEEIIQS FPKVSGQQPY LSNAGNQALT KAKSYLKTFG DEFVAVEHLL LGILSGSDKS
     AQLLKDQGVT EKGLIEAIKE LRQGNKVTDQ NAEAKYRSLE KYSKNLNELA KKGKIDPVIG
     RDEEIRRVLQ ILARRTKNNP ILLGEPGVGK TAIVEGLAQR IVSGDVPENL KSKTLISLDM
     GLLVAGAKYK GEFEERLKAV IKEVTDSDGE IILFIDEIHT LIGAGGGGEG AMDAANLLKP
     ALARGELHAI GATTLKEYQK YVEKDKALER RFQAVMVDEP DAADAISILR GIKDKYELHH
     GVRIKDDAVI SAVELSQRYI SDRFLPDKAI DLMDEAAAKL RMEIDSLPQE LDELNRRIMQ
     LEIEREAIRR EKNKDKEAVL SKELAELSEK RQAVKAKWES EKAVIMGIQR EKENIDKFKL
     EAEQAERAGD FGKVAEIRYG KISESEQKLE SFKQQLQEMQ EGSPLLKEEV DAEDVAAVVA
     KWTGIPLSRM LESEREKLLH LEDELGKRVA GQQEAIAALS DAVRRSRAGL QDPKRPIGSF
     IFMGTTGVGK TELAKALAEY LFNDDNAMVR IDMSEYQERH AVSRLVGAPP GYVGYDEGGQ
     LTEAVRRKPY SVILLDEIEK AHPDVFNILL QVLDDGRLTD NKGRMANFKN TIIILTTNIG
     SQLIQERFAA IEDWNKEQVM EDTKKEVFEL LKQSVRPEFL NRIDETIMFE PLSREITRKI
     VDIQWKEIQH RLADSGIEID ATKEVLDYLG EVGFDPQFGA RPLKRTMQRL VLNELSKQIL
     SGYIKNDAAV LVDLDADKQV YFKNVEGVEV
//
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