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Database: UniProt
Entry: A0A0F0HL34_9PSEU
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Original site: A0A0F0HL34_9PSEU 
ID   A0A0F0HL34_9PSEU        Unreviewed;       871 AA.
AC   A0A0F0HL34;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 46.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=UK12_24255 {ECO:0000313|EMBL:KJK56170.1};
OS   Saccharothrix sp. ST-888.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Saccharothrix.
OX   NCBI_TaxID=1427391 {ECO:0000313|EMBL:KJK56170.1, ECO:0000313|Proteomes:UP000033409};
RN   [1] {ECO:0000313|EMBL:KJK56170.1, ECO:0000313|Proteomes:UP000033409}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ST-888 {ECO:0000313|EMBL:KJK56170.1,
RC   ECO:0000313|Proteomes:UP000033409};
RA   Ju K.-S., Doroghazi J.R., Metcalf W.;
RL   Submitted (FEB-2015) 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:KJK56170.1}.
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DR   EMBL; JYJF01000089; KJK56170.1; -; Genomic_DNA.
DR   RefSeq; WP_045305247.1; NZ_JYJF01000089.1.
DR   AlphaFoldDB; A0A0F0HL34; -.
DR   PATRIC; fig|1427391.3.peg.7457; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000033409; 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:UP000033409};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          3..147
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          414..494
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   871 AA;  94585 MW;  B7D3E0BE2583B30F CRC64;
     MDAGKFTSKT QDALSAAIRQ ASAAGNPDVK PVHILLALLE QPEGIARPLL EAVGADVAAV
     TAAARRQLGT LPSAQGSTVS APQLARDTMA VLGEAGKRAE DLDDQYLSTE HLLVGLAAEG
     GPVADLLKQH GAAAKALLAA FKDVRGSARV TSPDPEGTYK ALEKYGTDLT QAARDGKLDP
     VIGRDQEIRR VVQVLSRRTK NNPVLIGDPG VGKTAVVEGL AQRIVAGDVP ESLRGKRLVA
     LDLGAMVAGA KYRGEFEERL KAVLNDIKSS NGQVVTFIDE LHTMVGAGAG GDSAMDAGNM
     LKPMLARGEL RMVGATTLDE YRERIEKDAA LERRFQQVLV GEPSVEDTIA ILRGLKGRYE
     AHHKVQIADA ALVAAASLSN RYITARFLPD KAIDLVDEAA SRLRMEIDSS PVEIDQLQRS
     VDRLRMEELA LEKESDPASV ERLDRLRRDL ADKQEQLSTL NARWEQEKKS LNRVGELKER
     LDDLHGLLER AQRDGDFERA SKLMYAEIPA AEQELADAQA RAADEDAGTS MVKEEVGPDD
     VADVVASWTG IPAGRLLEGE SAKLLRMEEE LGHRLIGQTE AVRAVSDAVR RTRAGLADPD
     RPTGSFLFLG PTGVGKTELA KALADFLFDD ERAMVRIDMS EYGEKHSVSR LVGAPPGYVG
     YEEGGQLTEA VRRRPYSVVL LDEVEKAHPE VFDVLLQVLD DGRLTDGQGR TVDFRNAILI
     LTSNLGSQFL VDPSTPDERK KALVLDTVRS AFKPEFLNRL DDIVVFDALG TAELSRIVDL
     QVARLGERLR ERRLTLDVTA AARDWLALTG YDPAYGARPL RRLVQSAIGD QLARAILSGE
     VHDGDTVVVE RDEAGDRLTV RSQHPVTSLQ K
//
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