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Database: UniProt
Entry: A0A1I5JKD6_9PSEU
LinkDB: A0A1I5JKD6_9PSEU
Original site: A0A1I5JKD6_9PSEU 
ID   A0A1I5JKD6_9PSEU        Unreviewed;       862 AA.
AC   A0A1I5JKD6;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, 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=SAMN05421805_12313 {ECO:0000313|EMBL:SFO73170.1};
OS   Saccharopolyspora antimicrobica.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Saccharopolyspora.
OX   NCBI_TaxID=455193 {ECO:0000313|EMBL:SFO73170.1, ECO:0000313|Proteomes:UP000199398};
RN   [1] {ECO:0000313|EMBL:SFO73170.1, ECO:0000313|Proteomes:UP000199398}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CPCC 201259 {ECO:0000313|EMBL:SFO73170.1,
RC   ECO:0000313|Proteomes:UP000199398};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; FOUP01000023; SFO73170.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I5JKD6; -.
DR   STRING; 455193.SAMN05421805_12313; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000199398; 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:SFO73170.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SFO73170.1};
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   COILED          414..494
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   862 AA;  93613 MW;  26CC9D8DE49E4E96 CRC64;
     MDAFNPTTKT QQAISSAVQA ATVAGNPDVS PAHLLGALLA QGDGLTAPLL TAVGADPTAV
     RRELEQLINA LPAASGSTVS APQLSRDAVR ALTHAQRMAT EMGDEYVSTE HLLVGLAAEG
     GRVADLLKKH GATPEALTDA FGNVRGSARV TSPDPEGTYK ALEKYGQDLT DRARKGDLDP
     VIGRDTEIRR VVQVLSRRTK NNPVLIGEPG VGKTAIVEGL AQRIIAGDVP ESLRGKRVVA
     LDLGSMVAGA KYRGEFEERL KAVLKEITDS AGQIITFIDE LHTIVGAGAS GEGAMDAGNM
     IKPMLARGEL RMVGATTLDE YRKHIETDAA LERRFQQVLV GEPSPEDTVA ILRGLKERYE
     VHHGVRITDG ALVAAATLSD RYITARFLPD KAIDLVDEAA SRLRMEIDSR PVEIDEVERA
     VRRLEIEEMA LSKEDDPASL ERLAALRAEL ADRREKLSGL TARWQQEKES IDKVRDLKTQ
     LEQLRGESER AERDGDLGKA AELRYGRIPQ LEKELDAATA AQSERKAMLQ EEVIADDVAD
     VVSSWTGIPA GRLLEGETAK LLRMEEALGA HVVGQAEAVR AVSDAVRRTR AGVADPDRPT
     GSFLFLGPTG VGKTELAKAL AGFLFDDERA MVRIDMSEYA EKHSVARLVG APPGYVGYDQ
     GGQLTESVRR RPYSVVLFDE VEKAHPDVFD VLLQVLDDGR LTDGQGRTVD FRNTILVLTS
     NLGSQAIADP NLSERERDDA VMSVVRKHFK PEFLNRLDDV VVFHSLSTDE LTSIVDIQVD
     HLGRRLAQRR LTLDVQPAAR DWLALNGFDP VYGARPLRRL VQSAIGDQLA RKLLAGEIRE
     GDKIKVDTTD DSQGLTVTAA ES
//
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