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Database: UniProt
Entry: F1T6P6_9ACTO
LinkDB: F1T6P6_9ACTO
Original site: F1T6P6_9ACTO 
ID   F1T6P6_9ACTO            Unreviewed;       935 AA.
AC   F1T6P6;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 64.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034,
GN   ECO:0000313|EMBL:EGF22771.1};
GN   ORFNames=HMPREF0091_11097 {ECO:0000313|EMBL:EGF22771.1};
OS   Fannyhessea vaginae DSM 15829.
OC   Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC   Fannyhessea.
OX   NCBI_TaxID=525256 {ECO:0000313|EMBL:EGF22771.1, ECO:0000313|Proteomes:UP000005947};
RN   [1] {ECO:0000313|EMBL:EGF22771.1, ECO:0000313|Proteomes:UP000005947}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15829 {ECO:0000313|EMBL:EGF22771.1,
RC   ECO:0000313|Proteomes:UP000005947};
RA   Muzny D., Qin X., Buhay C., Dugan-Rocha S., Ding Y., Chen G., Hawes A.,
RA   Holder M., Jhangiani S., Johnson A., Khan Z., Li Z., Liu W., Liu X.,
RA   Perez L., Shen H., Wang Q., Watt J., Xi L., Xin Y., Zhou J., Deng J.,
RA   Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L., Villasana D., Johnson A.,
RA   Liu J., Liyanage D., Lorensuhewa L., Robinson T., Song A., Song B.-B.,
RA   Dinh H., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M.,
RA   Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N.,
RA   Okwuonu G., Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W.,
RA   Jakkamsetti A., Pham P., Ruth R., San Lucas F., Warren J., Zhang J.,
RA   Zhao Z., Zhou C., Zhu D., Lee S., Bess C., Blankenburg K., Forbes L.,
RA   Fu Q., Gubbala S., Hirani K., Jayaseelan J.C., Lara F., Munidasa M.,
RA   Palculict T., Patil S., Pu L.-L., Saada N., Tang L., Weissenberger G.,
RA   Zhu Y., Hemphill L., Shang Y., Youmans B., Ayvaz T., Ross M.,
RA   Santibanez J., Aqrawi P., Gross S., Joshi V., Fowler G., Nazareth L.,
RA   Reid J., Worley K., Petrosino J., Highlander S., Gibbs R.;
RL   Submitted (FEB-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:RU362034}.
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:EGF22771.1}.
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DR   EMBL; ACGK02000004; EGF22771.1; -; Genomic_DNA.
DR   AlphaFoldDB; F1T6P6; -.
DR   eggNOG; COG0542; Bacteria.
DR   Proteomes; UP000005947; 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; 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.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU362034};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU362034};
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:RU362034};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005947};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          9..152
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   REGION          869..935
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          418..532
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
FT   COMPBIAS        882..901
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        902..935
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   935 AA;  103430 MW;  840760776E485247 CRC64;
     MKEVVCMQLS MWSTTAQELL QQAIAAAQTA HASQVLPLHV LDALLSSRER NISAIIEKIG
     GDAGAIERSV KEKLAKLPAI TGQTVQTELS NQLIDVANKA EAYAHKLTDD YVTTEHILYA
     LASTSGDAQK ILQDFGITAQ RIAKVYEELR GNDRVTSADS KPQFQALEQY GRNVCALARA
     HKLDPVIGRV EEIRRTIQVL SRRTKNNPVL IGEPGVGKTA IVEGLAERIV AGDVPSSIKD
     KELIELDMSA LVAGAKYRGE FEDRLKAVLK EVEKSQGRII LFIDELHTIV GAGATDGAMD
     AGNILKPALA RGALHAIGAT TLDEYRKYIE KDQALARRFQ TVLVKEPSVE DTVSILRGLK
     QAYEQHHRVR ICDAALVSAA DLSNRYISER FLPDKAIDLV DEAASRLRME LDSMPADIDA
     KQRELTRMQI EEQALKKEDD DASKERLSAL QKEIADAREI LTTARAKWYN EKHAIDKVQD
     LKSKIEHAKR DMEYAAQTSD LARASELRYA TIPELEKRYQ EAEAALHDKQ ENGGLLKEEV
     TPEEIAAVVS SWTGIPVAKM MQGEMSKLRG LEAVLHKRVI GQDKAVSAVA AAVRRSRAGL
     ADPNKPLGSF FFLGPTGVGK TELAKTLVST LFDDERALVR IDMSEYMEKF SVQRLIGAPP
     GYVGYDEGGQ LTEAVRRHPY CVILLDEMEK AHPDVFNILL QLLDDGRLTD GQGRVVSFKN
     SIIIMTSNVG SQIISQATQA GSSLTSEDVK NRVTQALRDT FKPEFLNRID DIVMFDSLNA
     AAIEKIVDLQ LKSVRERLAR ERMSLVLTDA AHKQLATQGF DPAYGARPLK RLIQTQVVDT
     ISTLIIDGRV HEGDTLVVDV DAEHNFIAHP KMSDAHTDPA REASTQKGSS RLAQNISSRR
     GDSTIRAERE DDDGYDPYSD RAPSQEKLFE KNPWD
//
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