ID S3BQP0_9ACTN Unreviewed; 852 AA.
AC S3BQP0;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE RecName: Full=Chaperone ClpB {ECO:0008006|Google:ProtNLM};
GN ORFNames=HMPREF1486_00717 {ECO:0000313|EMBL:EPD96542.1};
OS Streptomyces sp. HPH0547.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1203592 {ECO:0000313|EMBL:EPD96542.1, ECO:0000313|Proteomes:UP000014390};
RN [1] {ECO:0000313|EMBL:EPD96542.1, ECO:0000313|Proteomes:UP000014390}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HPH0547 {ECO:0000313|EMBL:EPD96542.1,
RC ECO:0000313|Proteomes:UP000014390};
RG The Broad Institute Genomics Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Schmidt T.M., Dover J., Dai D.,
RA 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. HPH0547.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent.
CC {ECO:0000256|ARBA:ARBA00026057}.
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:EPD96542.1}.
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DR EMBL; ATCE01000022; EPD96542.1; -; Genomic_DNA.
DR RefSeq; WP_016467612.1; NZ_KE150468.1.
DR AlphaFoldDB; S3BQP0; -.
DR PATRIC; fig|1203592.3.peg.726; -.
DR HOGENOM; CLU_005070_4_1_11; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000014390; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 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.
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:UP000014390};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 44..182
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT DOMAIN 460..495
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT REGION 169..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 456..502
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 852 AA; 93526 MW; 1042F1D632F3D29F CRC64;
MTSGYTGPGG FGRDPFEEFV ARFLGGAPSG GGGQRGDPRY FDFFRLLSEP ARQLVSEAAS
YAAQHGSTDL DTEHLLRAAL VSEPTHTMVA RAGADPDALA AEIDRVADEG PPRTSISVSP
AVKRALLDAH EIARSRGASY IGAEHVLVAL AANRDSTAGR ILNAARFDPG SAAPGGGPSG
GQGAPEAPPR GGTATRERGT PNLDKYGRDL TELAREGRID PVIGRDEQIE QTIEILARRG
KNNPVLIGEA GVGKTAVVEG LAQRIAEGDV PDNLLGRRVV QLDFGSIVAG TRYRGDFEER
LTGLIDEIRA RTDQLIVFID ELHTVVGAGG GGEGGSMDAS NMLKPALARG ELHVIGATTL
EEHRRHIEKD AALARRFQPV LVPEPTTADA IEILRGLRDR YEAHHQVRYT DEALVAAVEL
SDRYLTGRFL PDKAIDLLDQ AGARVRLRSA TRGTDVRALE REAEQVRRDK DQAVAAEDYE
RAKELRDRLG ELEEAIKQDG EREEQRHDHR IPEVTVEDIA DIISRQTGIP LSNLTQDEKD
RLLGLEEHLR HRVIGQDEAV TAVADAVLRS RAGLSSPDRP IGSFLFLGPT GVGKTELARA
LAEALFGSDE KMVRLDMSEY QERHTVSRLV GAPPGYVGHE EAGQLTETVR RNPYSLLLLD
EVEKAHPDVF NMLLQVLDDG RLTDSQGRTV DFTNTVIVMT SNLGSEAITG RGAVLGFGSG
ESADEEARRE RVLRPLREHF RPEFLNRIDE IVIFRRLDDV QLRQITDMLL EETRRRVHAQ
DLTIDFSSEA VDWLAHRGYQ PEYGARPLRR TIQREVDNRL SRMLLSGELE PHTRLLVDVA
GDELEFRTEA PA
//