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Database: UniProt
Entry: A0A6B2SHS0_9ACTN
LinkDB: A0A6B2SHS0_9ACTN
Original site: A0A6B2SHS0_9ACTN 
ID   A0A6B2SHS0_9ACTN        Unreviewed;       843 AA.
AC   A0A6B2SHS0;
DT   17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=ATP-dependent Clp protease ATP-binding subunit {ECO:0000313|EMBL:NDZ87862.1};
GN   ORFNames=G3I23_20235 {ECO:0000313|EMBL:NDZ87862.1};
OS   Streptomyces sp. SID10115.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=2706016 {ECO:0000313|EMBL:NDZ87862.1, ECO:0000313|Proteomes:UP000475437};
RN   [1] {ECO:0000313|EMBL:NDZ87862.1, ECO:0000313|Proteomes:UP000475437}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SID10115 {ECO:0000313|EMBL:NDZ87862.1,
RC   ECO:0000313|Proteomes:UP000475437};
RA   Currrie C., Chevrette M., Carlson C., Stubbendieck R., Wendt-Pienkowski E.;
RT   "Insect and environment-associated Actinomycetes.";
RL   Submitted (JAN-2020) 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:NDZ87862.1}.
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DR   EMBL; JAAGLF010000714; NDZ87862.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A6B2SHS0; -.
DR   Proteomes; UP000475437; 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   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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   Hydrolase {ECO:0000313|EMBL:NDZ87862.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:NDZ87862.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000475437};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          33..175
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   DOMAIN          449..484
FT                   /note="UVR"
FT                   /evidence="ECO:0000259|PROSITE:PS50151"
FT   REGION          159..192
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          438..491
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        166..192
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   843 AA;  91681 MW;  74371B9D52A8D2A1 CRC64;
     MSSGFIGPEG FGQDPFGALF ARFLGSGRRQ IDIGRLMSGP ARELVAAAAS YAAEHGKSNL
     DTEHLLRAAL TIEPTRGLVA RSGADPEQIA EEIDRHSAET EGAVPTQAVA LTPAVKRALL
     DAHEVARAVG AGYIGPEHIV MALAANPDSA AGHILNAARF DPGTAPQQPQ GRTGPAEQRQ
     NGSSGTATPT LDQFGRDLTA RAAEGGVDPV IGREEEIEQT IEVLSRRGKN NPVLIGDAGV
     GKTAVVEGLA QRIADGDVPE TLADRRVIAL DLSGVVAGTR YRGDFEERLN GIIEEVRANS
     DEVIVFIDEL HTVVGAGGGG SEGGSMDAGN MLKPALARGE LHVIGATTLE EYRRYIEKDA
     ALARRFQPIL VAEPTAADAV EILRGLRDRY EAHHQVRYSD EALLAAVELS DRYLTERFLP
     DKAIDLMDQA GARVRLRAST KGTDVRALER EMEQLTRDKD QAVAAEQYER ATELRDRVAD
     LARRIEEGRS RAPGDGRIVE VNSEDIAEVV SRQTGIPVST LTQEERDRLL GLEEHLHERV
     VGQEEAVSAV AEAVLRSRSG LSSPDRPIGS FLFLGPTGVG KTELARALAE ALFGSEERMV
     RLDMSEFQER HTVSRLVGAP PGYVGHEEAG QLTEAVRRHP YSLLLLDEVE KAHPDVFNTL
     LQVLDDGRLT DAQGRTVNFT NTVIVMTSNL GSEALTGRGA TLGFRADGSE ADEEARREQV
     LRPLREHFRP EFLNRIDEIV IFRRLTGEQL RQVTDLLLEE TRRRLRAQDV TIEFTTEAVD
     WLARRGHQPE YGARPLRRTI QREVDNRLSR LLLDGGLTAG SRVTVDVVDD ALDMRVASGS
     AVG
//
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