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Database: UniProt
Entry: A0A5D0NZI5_9ACTN
LinkDB: A0A5D0NZI5_9ACTN
Original site: A0A5D0NZI5_9ACTN 
ID   A0A5D0NZI5_9ACTN        Unreviewed;       865 AA.
AC   A0A5D0NZI5;
DT   13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2019, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034,
GN   ECO:0000313|EMBL:TYB49499.1};
GN   ORFNames=FXF69_10600 {ECO:0000313|EMBL:TYB49499.1};
OS   Actinomadura chibensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Thermomonosporaceae; Actinomadura.
OX   NCBI_TaxID=392828 {ECO:0000313|EMBL:TYB49499.1, ECO:0000313|Proteomes:UP000323380};
RN   [1] {ECO:0000313|EMBL:TYB49499.1, ECO:0000313|Proteomes:UP000323380}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 14158 {ECO:0000313|EMBL:TYB49499.1,
RC   ECO:0000313|Proteomes:UP000323380};
RA   Songsumanus A., Kuncharoen N., Kudo T., Yuki M., Igarashi Y.,
RA   Tanasupawat S.;
RT   "Actinomadura sp. nov. CYP1-5 isolated from mountain soil.";
RL   Submitted (AUG-2019) 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:TYB49499.1}.
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DR   EMBL; VSFG01000001; TYB49499.1; -; Genomic_DNA.
DR   RefSeq; WP_067902117.1; NZ_VSFG01000001.1.
DR   AlphaFoldDB; A0A5D0NZI5; -.
DR   STRING; 1220554.GCA_001552135_07044; -.
DR   Proteomes; UP000323380; 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   Reference proteome {ECO:0000313|Proteomes:UP000323380};
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          412..492
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   865 AA;  95122 MW;  6F385C6174EA4A07 CRC64;
     MDYKLTQKSQ EALSVAIRRA AAEGHPEVEP EHLLVSLIGL ADGTAVPLLE AVGADWQAIR
     RRAEEQLAAK PKAQGSTVAT PRLSGQLQRS INTAANRAQQ LEDDYVSTEH LLVGLAADGG
     PAAGLLKEFG ATPQALLDAF GKVRGHARVT SENPEGTYQS LERYGVDLTA AARDGRLDPV
     IGRDSEIRRV VQVLSRRTKN NPVLIGEPGV GKTAVVEGLA QRIIAGDVPE SLRDKRLVSL
     DLGAMVAGAK YRGEFEERLK AVLNEIKESE GQVVTFIDEL HTVVGAGAAE GAMDAGNMLK
     PMLARGELRM IGATTLDEYR ERIEKDAALE RRFQQVFVGE PSVEDTIAIL RGLKGRYEAH
     HKVQINDSSL VAAATLSDRY ITSRYLPDKA IDLVDEAASR LRMEIDSRPV EIDELQRTVD
     RLKMEEMNLS KETDEASRQR LERLRADLAD KQEHLTGLVA RWDKEKAGLN RVGEIKERID
     QLRGEAERAQ RDGDLETSAR LTYGEIPALE KQLEEASEAA ENTTPMVKEE VGPDDVADVV
     ASWTGIPAGR LLEGETAKLL RMEDELGKRL IGQETAVRTV SDAVRRARAG ISDPDRPTGS
     FLFLGPTGVG KTELAKALAE FLFDDERAMT RIDMSEYSEK HSVARLVGAP PGYVGYEEGG
     QLTEAVRRRP YSVVLLDEVE KAHPEVFDIL LQVLDDGRLT DGQGRTVDFR NAILILTSNI
     GSQFLVDPTL ENGAKREAVW NAVRNSFKPE FLNRLDDVIL FDALSTDELT RIVDLQVDKL
     ADRLADRQLT LDVTPAAREW LALTGYDPLY GARPLRRLVQ TAIGDQLARE LLSGEVRDGD
     EVTVDLDEQA DKLTVHPTRG LTLTK
//
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