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Database: UniProt
Entry: A0A1W2GZ23_9BACT
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Original site: A0A1W2GZ23_9BACT 
ID   A0A1W2GZ23_9BACT        Unreviewed;       870 AA.
AC   A0A1W2GZ23;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=SAMN00777080_0395 {ECO:0000313|EMBL:SMD41861.1};
OS   Aquiflexum balticum DSM 16537.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC   Aquiflexum.
OX   NCBI_TaxID=758820 {ECO:0000313|EMBL:SMD41861.1, ECO:0000313|Proteomes:UP000192333};
RN   [1] {ECO:0000313|EMBL:SMD41861.1, ECO:0000313|Proteomes:UP000192333}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16537 {ECO:0000313|EMBL:SMD41861.1,
RC   ECO:0000313|Proteomes:UP000192333};
RA   Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA   Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL   Submitted (APR-2017) 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; LT838813; SMD41861.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1W2GZ23; -.
DR   STRING; 758820.SAMN00777080_0395; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000192333; Chromosome i.
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:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0042026; P:protein refolding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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   Hydrolase {ECO:0000313|EMBL:SMD41861.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SMD41861.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000192333};
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;  98222 MW;  793EF3D05165F56F CRC64;
     MDFKQFTIKS QEAIQKAVEL TSAEQQQVIE PAHLLKGIFS EDENVTDFLF KKLGVNKGLI
     IQKTDEIISN YPKVSGQQPY LSNAANQVLS KAKDYLKNFG DEFIAIEHLL LAILAGSEKT
     AQLLKDQGMS EKPLIEAIKE LRKGNKVTDQ NAESKYRALE KYSKNLNELA KKGKIDPVIG
     RDEEIRRVLQ ILARRTKNNP ILLGEPGVGK TAIVEGLAQR IISGDVPENL KSKILISLDM
     GLLVAGAKYK GEFEERLKAV IKEVTDSEGE IILFIDEIHT LIGAGGGGEG AMDAANLLKP
     ALARGELHAI GATTLKEYQK YIEKDKALER RFQAVMVNEP DSADAISILR GIKDKYELHH
     GVRIKDDAVI AAVELSQRYI SDRFLPDKAI DLMDEAAAKL RMEIDSLPQE LDELNRRIMQ
     LEIEREAIRR ENNKDKETVL SKEIAELSEK RQNVKAKWES EKAVITGIRT EKESIDRLKL
     EAEQAERAGD FGKVAEIRYG KIVEAEQKLD KYKSQLEEMQ QGSPLLKEEV DNEDIAAVVS
     KWTGIPLSKM IQSEREKLLH LEDELGKRVA GQREAITAIS DAVRRSRAGL QDPKRPIGSF
     IFMGTTGVGK TELAKALAEY LFNDENSMVR IDMSEYQERH AVSRLVGAPP GYVGYDEGGQ
     LTEAVRRKPY SVVLLDEIEK AHPDVFNILL QVLDDGRLTD NKGRIANFKN TIIILTTNIG
     SHLIQERFAE MEEWNKEEIL EKTKSEVYDL LKKSVRPEFL NRIDETIMFE PLNRKVIRKI
     VDIQWREIQQ RLAESNIEIE ATQEVLDFLG QVGFDPQFGA RPLKRTMQRL ILNELSKQIL
     SGYIKNDSAV LVDLDAENQV YFKNIESVEV
//
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