ID A0A176L8G3_9ACTN Unreviewed; 879 AA.
AC A0A176L8G3;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=A6P39_10790 {ECO:0000313|EMBL:OAB00720.1};
OS Streptomyces sp. FXJ1.172.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=710705 {ECO:0000313|EMBL:OAB00720.1};
RN [1] {ECO:0000313|EMBL:OAB00720.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FXJ1.172 {ECO:0000313|EMBL:OAB00720.1};
RA Liu M., Liu N., Shang F., Huang Y.;
RT "Activation and identification of NC-1, a novel cryptic cyclodepsipeptide
RT from red soil-derived Streptomyces sp. FXJ1.172.";
RL Submitted (APR-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|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:OAB00720.1}.
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DR EMBL; LWRP01000057; OAB00720.1; -; Genomic_DNA.
DR RefSeq; WP_067043073.1; NZ_CP119133.1.
DR AlphaFoldDB; A0A176L8G3; -.
DR STRING; 710705.A6P39_10790; -.
DR OrthoDB; 9803641at2; -.
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 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; 98180 MW; 9FF200D50D2E7947 CRC64;
MDMNSLTQKS QEALQAAQSA AVGMGQTEVD GEHLLLALLD QEDGLIPRLL QQAGTEPKEL
RAAVREELSR RPKVTGPGAA PGQVFVTQRL SRLLDAAERE AKRLKDEYVS VEHLLLALAE
EGSATAAGRL LKEHGVTRDS FLSALTQVRG NQRVTSANPE VAYEALEKYG RDLVLEARSG
RLDPVIGRDA EIRRVTQILS RKTKNNPVLI GDPGVGKTAI VEGLAQRIVR GDVPEGLRDK
TVFALDMGSL VAGAKYRGEF EERLKAVLSE VKAAQGRILL FIDELHTVVG AGAAEGAMDA
GNMLKPMLAR GELHMIGATT LDEYRKHIEK DAALERRFQQ VLVDEPSVED TISILRGLRE
RLEVFHGVKI QDTALVSAAT LSHRYITDRF LPDKAIDLVD EACARLRTEI DSMPAELDEI
TRRVTRLEIE EAALSKETDP ASKTRLEELR KELADLRGEA DAKHAQWEAE RQAIRRVQEL
RQELEQVRHE AEEAERAYDL NRAAELRYGR LQDLERRLKA EEEQLVTKQG QNRLLREVVT
EEEIAEIVAA WTGIPVARLQ EGEREKLLRL DEILRERVIG QDEAVKLVAD AIIRARSGIR
DPRRPIGSFI FLGPTGVGKT ELAKTLAAAL FDSEENMVRL DMSEYQERHT VSRLMGAPPG
YVGYEEGGQL TEAVRRKPYS VVLFDEIEKA HTDVFNTLLQ VLDDGRITDS QGRTVDFRNT
VIIMTSNIGS EHLLDGATAE GEIKPDARAL VMGELRGHFR PEFLNRVDDI VLFKPLGERQ
IERIVELQFD ELRRRLAERR ITVELTDAAR EVIAHQGYDP VYGARPLRRY ISHEVETMVG
RALLRGDVQD GATVRVDAEH GELVVTYDQP EDVKGARAA
//
