ID A0A498DTT9_9ACTN Unreviewed; 875 AA.
AC A0A498DTT9;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:RLL67692.1};
GN ORFNames=D7M15_13525 {ECO:0000313|EMBL:RLL67692.1};
OS Streptomyces sp. Z26.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2500177 {ECO:0000313|EMBL:RLL67692.1, ECO:0000313|Proteomes:UP000288048};
RN [1] {ECO:0000313|EMBL:RLL67692.1, ECO:0000313|Proteomes:UP000288048}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Z26 {ECO:0000313|EMBL:RLL67692.1,
RC ECO:0000313|Proteomes:UP000288048};
RA Buchmann A., Cano-Prieto C., Baz M., Hassani L., Barakate M., Nafis A.,
RA Niedermeyer T.H.J., Gross H.;
RT "Draft Genome Sequence of the Novonestmycin-Producing Strain Streptomyces
RT sp. Z26, isolated from potato rhizosphere in Morocco.";
RL Submitted (OCT-2018) 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}.
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:RLL67692.1}.
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DR EMBL; RCHV01000002; RLL67692.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A498DTT9; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000288048; 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};
KW Cytoplasm {ECO:0000256|RuleBase:RU362034};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Reference proteome {ECO:0000313|Proteomes:UP000288048};
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 514..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 875 AA; 95734 MW; AEC3956A7567791E CRC64;
MDAELTNKSR DAISAANDKA VTGGHPDITP VHLLLALLEG EDNENVQDLI AAVDVDQAAL
RADAERRLAA LPSVRGSTVS RPQPDRALLA VIADAARHAK ELGDDYVSTE HLLIGVAAKG
GPVAELMRAQ GATDRKLLDA FEKSRGGQRV TNADPEGTYK ALEKFGTDFT AAAREGKLDP
VIGRDQEIRR VVQVLSRRTK NNPVLIGEPG VGKTAVVEGL AQRIVKGDVP ESLKNKRLVG
LDLGAMVAGA KYRGEFEERL KTVLAEIRSS DGRIITFIDE LHTVVGAGAG GDSAMDAGNM
LKPMLARGEL RMVGATTLDE YRERVEKDPA LERRFQQVLV AEPTVPDTIA ILRGLKGRYE
AHHKVQIADG ALVSAAALSD RYITSRFLPD KAIDLVDEAA SRLRMEIDSS PVEIDELQRA
VDRLRMEELA LANETDPGSV QRLERLRREL ADREEELRGL NARWEKEKQG LNRLGELKEK
LDELRGRAER AQRDGDFEGA SQLLYGEIPD LERELEEASA AEEEAAASQR GDDGHAAKQT
MVKEEVGPDD IADVVASWTG IPAGRLLEGE TQKLLRMEDE LGRRLIGQTE AVRAVSDAVR
RTRAGVADPD RPTGSFLFLG PTGVGKTELA KALADFLFDD ERAMVRIDMS EYGEKHSVAR
LVGAPPGYVG YEEGGQLTEA VRRRPYTVVL LDEVEKAHHD VFDILLQVLD DGRLTDGQGR
TVDFRNTILV LTSNLGSQFL VDQLEKPEAK KAKVLETVRA SFRPEFLNRL DDVVVFDALG
PDELGRIAAL QLKALQRRLA DRRLTLDVTP AALHWLAEEG NDPAYGARPL RRLVQTAIGD
QLAREILAGD VRDGDTVRVD RVDGWEGLSV ARAEG
//