ID A0A2U3CAZ6_9ACTN Unreviewed; 879 AA.
AC A0A2U3CAZ6;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:PWI46198.1};
GN ORFNames=CK485_00110 {ECO:0000313|EMBL:PWI46198.1};
OS Streptomyces sp. ICBB 8177.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=563922 {ECO:0000313|EMBL:PWI46198.1, ECO:0000313|Proteomes:UP000245673};
RN [1] {ECO:0000313|EMBL:PWI46198.1, ECO:0000313|Proteomes:UP000245673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ICBB 8177 {ECO:0000313|EMBL:PWI46198.1,
RC ECO:0000313|Proteomes:UP000245673};
RX PubMed=29773836; DOI=10.1038/s41598-018-26179-w;
RA Pavlikova M., Kamenik Z., Janata J., Kadlcik S., Kuzma M., Najmanova L.;
RT "Novel pathway of 3-hydroxyanthranilic acid formation in limazepine
RT biosynthesis reveals evolutionary relation between phenazines and
RT pyrrolobenzodiazepines.";
RL Sci. Rep. 8:7810-7810(2018).
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|ARBA:ARBA00004496,
CC 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:PWI46198.1}.
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DR EMBL; NSKH01000001; PWI46198.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U3CAZ6; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000245673; 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 78, MITOCHONDRIAL; 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:UP000245673};
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..121
FT /evidence="ECO:0000256|RuleBase:RU362034"
FT COILED 417..531
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 879 AA; 98128 MW; C055ABD1FCB23BEF CRC64;
MDMNRLTQKS QEALQEAQSA AVGMGQTEVD GEHLLLALLD QEDGLIPRLL QQAGTEPKEL
RAAVREELSR RPKVTGPGAA PGQVFVTQRL SRLLDAADRE AKRLKDEYVS VEHLLLALAE
EGSATAAGRL LKEHGVTRDS FLSALTQVRG NQRVTSANPE VAYEALEKYG RDLVLEARSG
RLDPVIGRDA EIRRVTQILS RKTKNNPVLI GDPGVGKTAI VEGLAQRIVR GDVPEGLRDK
TVFALDMGSL VAGAKYRGEF EERLKAVLAE VKAAQGHILL FVDELHTVVG AGAAEGAMDA
GNMLKPMLAR GELHMIGATT LDEYRKHIEK DAALERRFQQ VLVDEPSVED TISILRGLRE
RLEVFHGVKI QDTALVSAAT LSHRYITDRF LPDKAIDLVD EACARLRTEI DSMPAELDEI
TRRVTRLEIE EAALSKETDA ASKNRLEELR RELADLRGEA DAKHAQWEAE RQAIRRVQEL
RQELEQVRHE AEEAERAYDL NRAAELRYGR LQDLERRLTA EEGQLAAKQG QNRLLREVVT
EEEIAEIVAA WTGIPVARLQ EGEREKLLRL DEVLRERVIG QDEAVKLVAD AIIRARSGIR
DPRRPIGSFI FLGPTGVGKT ELAKTLAAAL FDSEENMVRL DMSEYQERHT VSRLMGAPPG
YVGYEEGGQL TEAVRRKPYS VVLFDEIEKA HTDVFNTLLQ VLDDGRITDS QGRTVDFRNT
VIIMTSNIGS EHLLDGATAE GEIKPDARAL VMGELRGHFR PEFLNRVDDI VLFKPLGERQ
IERIVELQFD ELRHRLAERR ITVELTDDAR EVIAHQGFDP VYGARPLRRY ISHEVETMVG
RTLLRGDVQD GATVRVDAEH GELVVTYDQP EDVEGARAA
//
