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Database: UniProt
Entry: A0A316AF18_9ACTN
LinkDB: A0A316AF18_9ACTN
Original site: A0A316AF18_9ACTN 
ID   A0A316AF18_9ACTN        Unreviewed;       909 AA.
AC   A0A316AF18;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=BXY45_102236 {ECO:0000313|EMBL:PWJ55868.1};
OS   Quadrisphaera granulorum.
OC   Bacteria; Actinomycetota; Actinomycetes; Kineosporiales; Kineosporiaceae;
OC   Quadrisphaera.
OX   NCBI_TaxID=317664 {ECO:0000313|EMBL:PWJ55868.1, ECO:0000313|Proteomes:UP000245469};
RN   [1] {ECO:0000313|EMBL:PWJ55868.1, ECO:0000313|Proteomes:UP000245469}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44889 {ECO:0000313|EMBL:PWJ55868.1,
RC   ECO:0000313|Proteomes:UP000245469};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): from individual species to whole genera.";
RL   Submitted (MAR-2018) 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:PWJ55868.1}.
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DR   EMBL; QGDQ01000002; PWJ55868.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A316AF18; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000245469; 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: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:PWJ55868.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:PWJ55868.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245469};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          1..147
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   REGION          863..909
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          441..495
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   909 AA;  96954 MW;  9B33371E22063DF0 CRC64;
     MELKLTTKSQ EALAAAASSA VEAGHAHVLP AHLALALLEQ DGVAAALLAA TGAQVAPVRE
     QLRAQLAALP SASGATVATP QLSRPALQAL TAARTASEAH GDSFVSADHL LVGLASVEGP
     ESVAPLLARA GATRDALIEA LPGVRGGAQV TTADPEGTFK ALEQYGVDLT ARAREGKIDP
     VIGRDAEIRR VVQVLARRTK NNPVLIGEPG VGKTAVVEGL AQRIVDGDVP ESLRGRRLIS
     LDLGAMLAGA KYRGEFEERL KSVLDEIKGS DGEVITFIDE LHTVVGAGAS GGEGGLDAGN
     MLKPMLARGE LRLVGATTLS EYRERIEKDA ALERRFQQVF VGEPSVEDTV AILRGLNERY
     EAHHGVEITD AALVAAATLS DRYITGRQLP DKAIDLVDEA ASRLRMEIDS SPEEIDALRR
     ATDRLRMEEM ALSAETDPAS LDRLERLRAD LADRTEQLAA LTARWEQQKA GLNRVGELKQ
     QLDDARSRFE RAYRDLDYAV ASRIQYEEIP SLERQLAEAQ AAEEDGGAAG GGAPLVGERV
     GPDDIAAVVA AWTGIPVGRL LEGETSKLLR MEEVIGQRLV GQRDAVRAVS DAVRRARAGI
     SDPDRPTGSF LFLGPTGVGK TELAKSLADF LFDDERAMVR IDMSEYGEKH SVARLVGAPP
     GYVGYEAGGQ LTEAVRRRPY SVVLLDEVEK AHPEVFDVLL QVLDDGRLTD GQGRTVDFRS
     TILVLTSNLG SQFLVDSSLS SERQRDGVMA AVRAAFKPEF LNRLDEVVVF DALSTEDLAH
     IVDLHVDALA RRLSDRRLQL HVTPAARELL ALEGWDPAYG ARPLRRLVQR EIGDALAREL
     LSGGIQDGDA VLVDTSAEPL GSGRDRRALS VRRLAPGEQV PDGSGVTPAT DGATGGAGDP
     GELKALPSA
//
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