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Database: UniProt
Entry: S2YZS0_9ACTN
LinkDB: S2YZS0_9ACTN
Original site: S2YZS0_9ACTN 
ID   S2YZS0_9ACTN            Unreviewed;       841 AA.
AC   S2YZS0;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   RecName: Full=Chaperone ClpB {ECO:0008006|Google:ProtNLM};
GN   ORFNames=HMPREF1211_01814 {ECO:0000313|EMBL:EPD67555.1};
OS   Streptomyces sp. HGB0020.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1078086 {ECO:0000313|EMBL:EPD67555.1, ECO:0000313|Proteomes:UP000014410};
RN   [1] {ECO:0000313|EMBL:EPD67555.1, ECO:0000313|Proteomes:UP000014410}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HGB0020 {ECO:0000313|EMBL:EPD67555.1,
RC   ECO:0000313|Proteomes:UP000014410};
RG   The Broad Institute Genomics Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Schmidt T.M., Dai D., Dover J.,
RA   Kim K., Walker B., Young S., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M., Berlin A.M.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA   Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Streptomyces sp. HGB0020.";
RL   Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent.
CC       {ECO:0000256|ARBA:ARBA00026057}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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:EPD67555.1}.
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DR   EMBL; AGER01000004; EPD67555.1; -; Genomic_DNA.
DR   RefSeq; WP_016431786.1; NZ_KE150426.1.
DR   AlphaFoldDB; S2YZS0; -.
DR   STRING; 1078086.HMPREF1211_01814; -.
DR   PATRIC; fig|1078086.3.peg.1845; -.
DR   HOGENOM; CLU_005070_4_1_11; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000014410; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   CDD; cd00009; AAA; 1.
DR   CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR   Gene3D; 1.10.8.60; -; 2.
DR   Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   Gene3D; 4.10.860.10; UVR domain; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
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   InterPro; IPR001943; UVR_dom.
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.
DR   PROSITE; PS50151; UVR; 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|SAM:Coils};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014410};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          34..183
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   DOMAIN          450..485
FT                   /note="UVR"
FT                   /evidence="ECO:0000259|PROSITE:PS50151"
FT   REGION          78..115
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          163..197
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          446..485
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        173..194
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   841 AA;  92033 MW;  D09CBEABAC016A55 CRC64;
     MTSGFSGPEG YDPFGEFLAR FFGGPRPGPR QIDIGRLLSQ PARELVRGAA QYAAEHGSRD
     LDTQHLLRAA LAAEPTRSLL SRAGADPDSL ATEIDERSGP AQHTAEEAPP PTSLSLTPAV
     KRALLDAHDM ARASGAGYIG PEHVLSALAA NPDSAAGHIL NSARFAPTGP QPEAPETGQS
     RGEQTRTTGT PTLDKYGRDL TDLARQGRID PVIGRDEEIE QTIEVLSRRG KNNPVLIGDA
     GVGKTAIVEG LAQRIADGDV PDVLIGRRVV ALDLTGVVAG TRYRGDFEER LNNIVDEIRS
     HSDQLIVFID EVHTVVGAGS GGESGGAMDA GNILKPALAR GELHIVGATT LEEYRRIEKD
     AALARRFQPI LVPEPSVPDT IEILRGLRDR YEAHHQVRYT DEALVAAVEL SDRYLTDRRL
     PDKAIDLIDQ AGARVRLRAR TKGTDVRALE REIEQLTCDK DQSVADEQYE RAMQLRDRIA
     ELKQRIADTG GGVKADEGQL EVTAEAIAEV VSRQTGIPVS SLTQEEKEKL LGLEEHLHER
     VVGQEEAVSV VSEAILRSRA GLASPDRPIG SFLFLGPTGV GKTELARALA EALFGSEERM
     IRLDMSEYQE RHTVSRLVGA PPGYVGHEEA GQLTEVVRRH PYSLLLLDEV EKAHPDVFNI
     LLQVLDDGRL TDSQGRTVDF TNTVIVMTSN LGSEAIGRSG AGIGFGPGDA DADEEARRER
     ILRPLREHFR PEFLNRIDET VVFRRLTGDQ LRRITNLLLE KTRRLTHAQG ITVEFTDAAV
     DWLAERGYQP EYGARPLRRT IQREVDNQLS RLLLNGQIQE GGRVTVDVTD GHLEFRTDEH
     P
//
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