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Database: UniProt
Entry: A0A367ARI5_9ACTN
LinkDB: A0A367ARI5_9ACTN
Original site: A0A367ARI5_9ACTN 
ID   A0A367ARI5_9ACTN        Unreviewed;       860 AA.
AC   A0A367ARI5;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034,
GN   ECO:0000313|EMBL:RBY92042.1};
GN   ORFNames=DQ244_06925 {ECO:0000313|EMBL:RBY92042.1};
OS   Blastococcus sp. TBT05-19.
OC   Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC   Geodermatophilaceae; Blastococcus.
OX   NCBI_TaxID=2250581 {ECO:0000313|EMBL:RBY92042.1, ECO:0000313|Proteomes:UP000253254};
RN   [1] {ECO:0000313|EMBL:RBY92042.1, ECO:0000313|Proteomes:UP000253254}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TBT05-19 {ECO:0000313|EMBL:RBY92042.1,
RC   ECO:0000313|Proteomes:UP000253254};
RA   Ennis N., Dharumadurai D., Sevigny J., Hall J., Simpson S., Morris K.,
RA   Thomas W.K., Tisa L.S.;
RT   "Genome Sequence of Blastococcus sp. TF05-19.";
RL   Submitted (JUL-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:RBY92042.1}.
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DR   EMBL; QOHI01000002; RBY92042.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A367ARI5; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000253254; 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   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          1..146
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          413..493
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   860 AA;  93563 MW;  7E5FB8934AC7FBEE CRC64;
     MESKLTTRSQ EAVAGAQRLA VGRGQAALEP LHLLNALLEQ TDGIAGPLLT AVGADPVDVR
     SKAEAALRRM PSVSGATVSA PAPSREFLRV INAAGEQAGA LGDEYVSTEH LLVGLAGSEG
     EAGAVLTSAG ATRDALVAAF RTVRGTRKVT TPDPENTFQA LQKYAVDLTE RAREGKIDPV
     IGRDTEIRRV VQVLSRRTKN NPVLIGEPGV GKTAIVEGLA QRMVAGDVPE SLKGKRLMAL
     DLGAMVAGAK YRGEFEERLK AVLQEITEAE GQVVTFIDEL HTLVGAGATG DSSMDAGNMI
     KPMLARGELR MVGATTLDEY REHIEKDPAL ERRFQQVYVG EPSVEDTIGI LRGLKERYEV
     HHGVRITDTA IVAAATLSDR YVTSRFLPDK AIDLVDEAAS RLRMEIDSRP VEVDEVERAV
     RRMEIEEMAL AKEDDESSKA RLAALREDLA NRRQELAELT FRWQQDKTAI ERIQRIKEEL
     EHVRLEAERA ERDGDLARAA ELRYGRLPEL ERSLTSAEDS VASGDSMLKE EVGPDDIAEV
     VQAWTGIPAG RLLEGETQKL LRMEEGLTGR VVGQPDAVRA VADAVRRARS GVSDPDRPTG
     SFLFLGPTGV GKTELAKALA EYLFDDDRAM VRIDMSEYSE KHSVARLVGA PPGYVGYEAG
     GQLTEAVRRR PYTVVLLDEV EKAHPDVFDL LLQVLDDGRL TDGQGRTVDF RNTILILTSN
     LGSQIIADQS VPEAARRGAV LEVVRSHFKP EFLNRLDDVV VFRALGSEEL TGIVDIQVGV
     LARRLAARRL SLTVTDAARD WLALNGFDPV YGARPLRRLV QSAIGDQLAR ALLSGDIRDG
     DEVVVDWPAG DAEGLSVTRA
//
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