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Database: UniProt
Entry: A0A2U3A770_9ACTN
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ID   A0A2U3A770_9ACTN        Unreviewed;       844 AA.
AC   A0A2U3A770;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=AAA family ATPase {ECO:0000313|EMBL:PWI20387.1};
GN   ORFNames=DI272_09670 {ECO:0000313|EMBL:PWI20387.1};
OS   Streptomyces sp. Act143.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=2200760 {ECO:0000313|EMBL:PWI20387.1, ECO:0000313|Proteomes:UP000245455};
RN   [1] {ECO:0000313|EMBL:PWI20387.1, ECO:0000313|Proteomes:UP000245455}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Act143 {ECO:0000313|EMBL:PWI20387.1,
RC   ECO:0000313|Proteomes:UP000245455};
RA   Valanrebinro G., Kumari S., Rameshkumar N.;
RT   "Actinomycin D producing novel Streptomyces isolated from the rhizosphere
RT   of saline tolerant kaipad rice and its draft genome analysis.";
RL   Submitted (MAY-2018) 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:PWI20387.1}.
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DR   EMBL; QFRX01000001; PWI20387.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2U3A770; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000245455; 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:UP000245455};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          34..184
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          169..196
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          446..492
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        180..196
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   844 AA;  91799 MW;  514EC48DDD6DDE55 CRC64;
     MTSGFSGPEG YDPFGEFLAR FFGGPRPGPR QINIGQLLSQ PARELVRGAA QYAAEHGSRD
     LDTQHLLRAA LSAEPTRSLL SRAGADPDEL ATEIDERSGP VLHPPGEAPP PTSLSLTPAA
     KRALLDAHDL ARARGAGCIG PEHVLSALAA NPDSAAGHIL NSAHFAPTGL PPEAAPDAGA
     ARAERPRDTG TPTLDKYSRD LTDLARRGGI DPVIGRDEEI EQTIEVLSRR GKNNPVLIGD
     AGVGKTAIVE GLAQRIADGD VPDVLIGRRV VALDLTGVVA GTRYRGDFEE RLNSIVSEIR
     AHSDQLIVFI DELHTVVGAG GGGEAASMDA GNILKPALAR GELHIVGATT LEEFRRIEKD
     AALARRFQPI LVPEPSVADA LEILRGLRDR YEAHHQVRYT DEALTAAVEL SDRYLPDRRL
     PDKAIDLIDQ AGARVRLRAR TKGTDVRALE REVEQLVRDK DQAVADEQYE KATQLRDRIA
     ELKERIGEAA GNGTADEGQH LEVTAEAIAE VVSRQTGIPV ASLTQEEKEK LLGLEEHLHQ
     RVVGQEEAVR VVSDAVLRSR AGLASPDRPI GSFLFLGPTG VGKTELARAL AEALFGSEER
     MVRLDMSEYQ ERHTVSRLVG APPGYVGHEE AGQLTEVVRR HPYSLLLLDE VEKAHPDVFN
     ILLQVLDDGR LTDSQGRTVD FTNTVVVMTS NLGSEAITRR GAGIGFGAGG AEADEEARRE
     QILRPLREHF RPEFLNRIDE IVVFRQLTEE QLRQITDLLL DRTRRMLHAQ GITVDVTEAA
     VDWLSRRGYQ PEYGARPLRR TIQREVDNEL SRLLLDGRVA AGGRITVDVQ EGSLTIQPTD
     AEAP
//
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