ID A0A6G4VJU3_9ACTN Unreviewed; 870 AA.
AC A0A6G4VJU3;
DT 12-AUG-2020, integrated into UniProtKB/TrEMBL.
DT 12-AUG-2020, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:NGO14047.1};
GN ORFNames=G5C60_42275 {ECO:0000313|EMBL:NGO14047.1};
OS Streptomyces scabichelini.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2711217 {ECO:0000313|EMBL:NGO14047.1, ECO:0000313|Proteomes:UP000472335};
RN [1] {ECO:0000313|EMBL:NGO14047.1, ECO:0000313|Proteomes:UP000472335}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HC44 {ECO:0000313|EMBL:NGO14047.1,
RC ECO:0000313|Proteomes:UP000472335};
RA Sahin N., Gencbay T.;
RT "Whole-genome analyses of novel actinobacteria.";
RL Submitted (FEB-2020) 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:NGO14047.1}.
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DR EMBL; JAAKZY010000230; NGO14047.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A6G4VJU3; -.
DR Proteomes; UP000472335; 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:UP000472335};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 1..147
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT REGION 515..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 414..494
FT /evidence="ECO:0000256|RuleBase:RU362034"
FT COMPBIAS 520..535
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 870 AA; 95383 MW; D91A8061C9E333B5 CRC64;
MDAELTNRSR DAINAASNRA VSEGHPDLTP AHLLLALLEG QDNENITDLL AAVEADQAAV
RAGTERVLST LPSVTGSTVA PPQPNRELLA VIADAAERAK ELGDEYLSTE HLLIGIAAKG
GQTGDVLSQQ GASAKKLLEA FQKARGGRRV TTADPEGQYK ALEKFGTDFT AAAREGKLDP
VIGRDQEIRR VVQVLSRRTK NNPVLIGEPG VGKTAVVEGL AQRIIKGDVP ESLKNKRLVA
LDIGAMIAGA KYRGEFEERL KTVLAEIKDS DGQIITFIDE LHTVVGAGAG GDSAMDAGNM
LKPMLARGEL RMVGATTLDE YRERIEKDPA LERRFQQVLV AEPTVEDTIA ILRGLKGRYE
AHHKVVIADS ALVAAATLSD RYITSRFLPD KAIDLVDESA SRLRMEIDSS PVEIDELQRV
VDRLKMEELA LERETDPASR ERLEKLRRDL ADKEEELRGL TARWEKEKQS LNRVGELKEK
LDELRGQAER AQRDGDFDTA SKLLYGEIPA VERDLEAASE EEEEASKSGS KSDTMVKEEV
GADDIADVVA AWTGIPAGRL LEGETQKLLR MEEELGRRLI GQTQAVRAVS DAVRRTRAGI
ADPDRPTGSF LFLGPTGVGK TELAKALADF LFDDERAMVR IDMSEYSEKH SVSRLVGAPP
GYVGYEEGGQ LTEAVRRRPY SVVLLDEVEK AHSEVFDILL QVLDDGRLTD GQGRTVDFRN
TILILTSNLG SQFLVDPITS EEEKKEQVLE VVRASFKPEF LNRLDDLVVF SALTKPELER
IARLQIDRLA KRLAERRLAL EVTDEALTWL ADEGMDPAYG ARPLRRLVQT TIGDRLAKEI
LAGEIKDGDT VRVDSFGDGL IVGPATGKTL
//
