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
//