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Database: UniProt
Entry: A0A1C3NTR4_9ACTN
LinkDB: A0A1C3NTR4_9ACTN
Original site: A0A1C3NTR4_9ACTN 
ID   A0A1C3NTR4_9ACTN        Unreviewed;       878 AA.
AC   A0A1C3NTR4;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB2 {ECO:0000313|EMBL:SBW18175.1};
GN   Synonyms=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=FDG2_0557 {ECO:0000313|EMBL:SBW18175.1};
OS   Candidatus Protofrankia californiensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae;
OC   Protofrankia.
OX   NCBI_TaxID=1839754 {ECO:0000313|EMBL:SBW18175.1, ECO:0000313|Proteomes:UP000199013};
RN   [1] {ECO:0000313|Proteomes:UP000199013}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Wibberg D.;
RL   Submitted (FEB-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; FLUV01000215; SBW18175.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C3NTR4; -.
DR   Proteomes; UP000199013; 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:UP000199013};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          3..151
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          87..114
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
FT   COILED          417..531
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   878 AA;  97620 MW;  0D0739C41533342A CRC64;
     MDMNRLTQKS QEALAAAQAK ATALGHTEVD GEHLLIALLE APDGLVPRLI GQVGADTATL
     HAAVEADLAR RPKVTGPGAQ PGQVFVTQRL SGLLDAAERE AGRLKDEYVS VEHLLLALAE
     ESTSTAAGRR LAEHGITRES FLSALTRVRG HQRVTSTTPE AAYEALEKYG RDLVGQARTG
     TLDPVIGRDA EIRRVIQILS RKTKNNPVLL GDPGVGKTAI VEGLAQRIVR RDVPEGLRDK
     SIFALDLGSL VAGAKYRGEF EERLKAVLAE VKAAQGRILL FVDELHTVVG AGAGEGAMDA
     GNMLKPMLAR GELHMIGATT LDEYRKRVEA DAALERRFQP VMVDEPTVED TISILRGLRE
     RFEIYHGVKI QDGALVAAAT MSNRYITDRF LPDKAIDLVD EACARLRTEI DSMPAELDEI
     TRRVTRLEIE EAALAKETDP ASRARLEELR RELVDLRADA DAKRAQWDAE RQAIRRVQEL
     REELERVRRE AEEAERSYDL NRAAELRYGR LRELERRLTA EEEQLAAKQG EHRLLREVVT
     EEEIAEIVAV WTGIPVARLR ETERDKLLRL DEILRERVVG QDVAVALVAD AIIRARSGIR
     DLRRPIGSFV FLGPTGVGKT ELARTLAAAL FDTEESMIRL DMSEYQERHT VSRLVGAPPG
     YVGYEEGGQL TEAVRRKPYS VVLFDEIEKA HTDVFNVLLQ VLDDGRVTDA QGHRVDFRNT
     VIIMTSNIGS EYLLDGLDTE GRIRPEAETR VMAELRGHFR PEFLNRIDDI ILFRPLSLPQ
     LEKIVDLQVD DLRRRLAERR ITLELTGAGR RHIAQAGFDP VYGARPLRRY ISHEVETRIG
     RALLRGEVSE GGVVQVDAHD GELAVSYQAA DAQHGLAA
//
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