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Database: UniProt
Entry: A0A1Q5KI39_9ACTN
LinkDB: A0A1Q5KI39_9ACTN
Original site: A0A1Q5KI39_9ACTN 
ID   A0A1Q5KI39_9ACTN        Unreviewed;       844 AA.
AC   A0A1Q5KI39;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   SubName: Full=AAA family ATPase {ECO:0000313|EMBL:OKJ81251.1};
GN   ORFNames=AMK31_22750 {ECO:0000313|EMBL:OKJ81251.1};
OS   Streptomyces sp. TSRI0107.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1703942 {ECO:0000313|EMBL:OKJ81251.1, ECO:0000313|Proteomes:UP000185813};
RN   [1] {ECO:0000313|EMBL:OKJ81251.1, ECO:0000313|Proteomes:UP000185813}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TSRI0107 {ECO:0000313|EMBL:OKJ81251.1,
RC   ECO:0000313|Proteomes:UP000185813};
RX   PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA   Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA   Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA   Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT   "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL   MBio 7:e02104-e02116(2016).
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:OKJ81251.1}.
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DR   EMBL; LIVZ01000008; OKJ81251.1; -; Genomic_DNA.
DR   RefSeq; WP_073942524.1; NZ_LIVZ01000008.1.
DR   AlphaFoldDB; A0A1Q5KI39; -.
DR   STRING; 1703942.AMK31_22750; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000185813; 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; 2.
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   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          77..114
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          165..198
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          446..485
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   844 AA;  92530 MW;  BC0507FDDCBF6FD6 CRC64;
     MTSGFTGSEG YDAFGEFLAR FFGGPRPGPR QIDIGRLLSQ PARELVRGAA QYAAEHGSRD
     LDTQHLLRAA LSAEPTRSLL SRSGADPDSL ASEIDERSGP VQFPEGSAPP PTSLSLTPAV
     KRALLDAHDL ARATGAGHIG PEHVLSALAN NPDSAAGHIL NAARFSPGGL SPETAEAGPA
     PRAERPRQTG TPTLDKYGRD LTDQARRGRI DPVIGRDDEI EQTIEVLSRR GKNNPVLIGD
     AGVGKTAIVE GLAQRIAEAD VPDVLLGRRV VALDLTGVVA GTRYRGDFEE RMNNIVEEIR
     THSDQLIIFI DELHTVVGAG GGGEGGSMDA GNILKPALAR GELHIVGATT LEEYRRIEKD
     AALARRFQPI LVPEPTTEDA LEILRGLRDR YEAHHQVRYS DEALVAAVEL SDRYLTDRRL
     PDKAIDLIDQ AGARVRLRAR TKGTDVRAME REAEQLAADK DQAVADEQYE EAMRLRDRIT
     EIKQRITEAA GDGEADEGQH LEVTAEAIAE VVSRLTGIPV SRLTEEEKDR LLGLEEHLRE
     RVVGQEEAVR VVSDAVLRSR AGLSSPDRPI GSFLFLGPTG VGKTELARAL AEALFGSEDR
     MVRLDMSEYQ ERHTVSRLVG APPGYVGHEE AGQLTEVVRR HPYSLLLLDE VEKAHPDVFN
     ILLQVLDDGR LTDSQGRTVD FTNTVIVMTS NLGSEAIIRR GASIGFGPGG GDADEEARRE
     QILRPLREHF RPEFLNRIDE IVVFRQLTAD QLHQITNLLL EHTRRLLTAQ GVSVEFTDAA
     VDWLSRQGYQ PEYGARPLRR TIQREVDNRL SRLLLDGRVK EGDRVTVDVS DGRLDFRPER
     TPVG
//
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