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
//