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Database: UniProt
Entry: G1WC31_9BACT
LinkDB: G1WC31_9BACT
Original site: G1WC31_9BACT 
ID   G1WC31_9BACT            Unreviewed;       826 AA.
AC   G1WC31;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   24-JAN-2024, entry version 65.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=HMPREF9431_01382 {ECO:0000313|EMBL:EGV31047.1};
OS   Prevotella oulorum F0390.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=702438 {ECO:0000313|EMBL:EGV31047.1, ECO:0000313|Proteomes:UP000005141};
RN   [1] {ECO:0000313|EMBL:EGV31047.1, ECO:0000313|Proteomes:UP000005141}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0390 {ECO:0000313|EMBL:EGV31047.1,
RC   ECO:0000313|Proteomes:UP000005141};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Ganesan A.,
RA   Baranova O.V., Blanton J.M., Tanner A.C., Dewhirst F.E., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA   Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA   Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T.,
RA   Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA   Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Prevotella oulorum F0390.";
RL   Submitted (JUL-2011) 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:EGV31047.1}.
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DR   EMBL; ADGI01000048; EGV31047.1; -; Genomic_DNA.
DR   RefSeq; WP_004380422.1; NZ_JH114216.1.
DR   AlphaFoldDB; G1WC31; -.
DR   PATRIC; fig|702438.4.peg.1424; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_1_10; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000005141; 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:UP000005141};
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          410..487
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   826 AA;  93172 MW;  D4FEB1227C7A648F CRC64;
     MTLDKYTIKA QEAVQAGVQA AQAAQQQSVE PIHLLKGILE KAQDITHFIF QKLGVNAQAV
     DMALHNELQH LPKVSGGQPY LSNDSVQVLN KAEELSQKMG DEFVSVEPIL LALMQGNHTA
     GRILKDAGCT EEGVRKAIES LRQGQQVKSQ SGDENYQALS KYATNLVEKA RQGKLDPVIG
     RDEEIRRVLQ ILSRRTKNNP ILVGEPGTGK TAIVEGLAER IMKGDVPENL KNKQLYSLDM
     GQLVAGAKYK GEFEERLKGV IKEVTNAHGE IILFIDEIHT LVGAGGGEGA MDAANLLKPA
     LARGELRAIG ATTLNEYQKY FEKDKALERR FQMVKVDEPD ELDAISILRG LKEKYENHHH
     VRIQDDACIA AVQLSERYIS DRFLPDKAID LMDEAAAKLR MERDSVPEEL DEMERSLKQK
     EIERQAILRE NDTEKIALLE KEIAELKDKV NAFRARWQAQ KAEVDQISQL KQKKEGLKLE
     AERAEREGDY QRVAEIRYGE MKQIDDDIAH RREEIRKQQG ESLIREEVTS DDIAEVVSRW
     TGIPVSRMLQ SERDKLLHLE AELHRRVIGQ NEAIEAVSNA VRRSRAGLQD PNRPIASFIF
     LGTTGVGKTE LAKALAEYLF NDENMLTRID MSEYQEKFSV TRLIGAPPGY VGYDEGGQLT
     EAVRRKPYSV VLFDEIEKAH PDVFNTLLQV LDDGRLTDNK GRLVNFKNTI IIMTSNATRE
     QLTKLMRPEF LNRIDDIITF HALTKEEIGE VVELQMKRVQ KMLAAQGFTL HWTKETIDDL
     AELGYDPEFG ARPVKRAIQD YVLNDLSRKI LEGKVGKEIT LGHIEA
//
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