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Database: UniProt
Entry: A0A0Q8P985_9ACTN
LinkDB: A0A0Q8P985_9ACTN
Original site: A0A0Q8P985_9ACTN 
ID   A0A0Q8P985_9ACTN        Unreviewed;      2142 AA.
AC   A0A0Q8P985;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KRB70006.1};
GN   ORFNames=ASE03_25445 {ECO:0000313|EMBL:KRB70006.1};
OS   Kitasatospora sp. Root187.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Kitasatospora.
OX   NCBI_TaxID=1736486 {ECO:0000313|EMBL:KRB70006.1, ECO:0000313|Proteomes:UP000051829};
RN   [1] {ECO:0000313|EMBL:KRB70006.1, ECO:0000313|Proteomes:UP000051829}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root187 {ECO:0000313|EMBL:KRB70006.1,
RC   ECO:0000313|Proteomes:UP000051829};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRB70006.1, ECO:0000313|Proteomes:UP000051829}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root187 {ECO:0000313|EMBL:KRB70006.1,
RC   ECO:0000313|Proteomes:UP000051829};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001433};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
CC   -!- SIMILARITY: Belongs to the AfsR/DnrI/RedD regulatory family.
CC       {ECO:0000256|ARBA:ARBA00005820}.
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:KRB70006.1}.
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DR   EMBL; LMHX01000014; KRB70006.1; -; Genomic_DNA.
DR   RefSeq; WP_057241032.1; NZ_LMHX01000014.1.
DR   STRING; 1736486.ASE03_25445; -.
DR   Proteomes; UP000051829; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:UniProt.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd15831; BTAD; 2.
DR   CDD; cd14014; STKc_PknB_like; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 2.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR   InterPro; IPR005158; BTAD.
DR   InterPro; IPR002543; FtsK_dom.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR001867; OmpR/PhoB-type_DNA-bd.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR047738; SAV_2336-like_N.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR016032; Sig_transdc_resp-reg_C-effctor.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   NCBIfam; NF041121; SAV_2336_NTERM; 1.
DR   PANTHER; PTHR35807:SF1; TRANSCRIPTIONAL REGULATOR REDD; 1.
DR   PANTHER; PTHR35807; TRANSCRIPTIONAL REGULATOR REDD-RELATED; 1.
DR   Pfam; PF03704; BTAD; 2.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00486; Trans_reg_C; 2.
DR   SMART; SM01043; BTAD; 2.
DR   SMART; SM00220; S_TKc; 1.
DR   SMART; SM00862; Trans_reg_C; 2.
DR   SUPFAM; SSF46894; C-terminal effector domain of the bipartite response regulators; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF48452; TPR-like; 2.
DR   SUPFAM; SSF69322; Tricorn protease domain 2; 1.
DR   PROSITE; PS50901; FTSK; 1.
DR   PROSITE; PS51755; OMPR_PHOB; 2.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00289};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PROSITE-
KW   ProRule:PRU01091};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00289};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051829};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   DOMAIN          1071..1337
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          1345..1444
FT                   /note="OmpR/PhoB-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51755"
FT   DOMAIN          1597..1700
FT                   /note="OmpR/PhoB-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51755"
FT   DOMAIN          1910..2093
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   DNA_BIND        1345..1444
FT                   /note="OmpR/PhoB-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01091"
FT   DNA_BIND        1597..1700
FT                   /note="OmpR/PhoB-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01091"
FT   REGION          47..112
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          231..253
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          314..340
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         1927..1934
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ   SEQUENCE   2142 AA;  230773 MW;  690680833603E6DA CRC64;
     MDEREPDATA QAALREALAQ LLAPAGGDPL SQDLADVLWI SRLTGLAPLP AGGAAPHGDT
     PTRAEEPEPL TVDQPEPAAE PSGPAQPSAG PKAELHPRAA AEATGPVGSR GGEAVQVTRP
     AALPGALGLA RALRPLRRPL RNPVGRVERA GLDEEATADS TADVGVLLPV WRQEQQRRFS
     VDLLVDTGAT MAVWHGLAGE FATLLERHGA FVDVRCWSLD TDHAVPHLTP FRRRSRRPRA
     ASQPSGPARN WARPLADPLG RRILLVLTDG VGPAWYGEEL PAFLARALGG RPAAVLQVLP
     RRLWHRTALR PAPVEGRAAT HGQSAPVLRS DAALPGIPRG PRGSAARAAV RWLPVLEIDA
     EWLAPWAEVV AGRASGWTPM LAAPVRGVPR PQHPGRAVEE PVTAAERVAR FRAGSSPGAY
     RLACHVAAAP LSLPVMRLVQ QATLPGTGQQ ELAELFLSGL LELREEALDP DEVVYDFREA
     VREELLAELT RSESVRVLES VLAKVSGRVA ATFGGTLDFR ALAATAGAGG LALPSRSRPF
     AEVAVAVLAG AGGQHAALAR TLSAAVEAGA GAGAGVADGT SVRGAVIRHE LLGPAPIISP
     PDPLRMIGRQ HKLALLEQAA LADRHSTVVI EAVPGLGKRR LVQEYIQWHG ARHSFIHWID
     GDTVSVVAGL AQLRSALDPA DLPSASFPPL SQLLREHPGW LIVIDGLSQD SVLTSLGVRF
     GLADAGPGCL IVTTGLLDSS RARDDATVIT LGELTDDELL HELRLRLDEL SPGREQDEQL
     RQLLEILPRN PGLLMQWDLD AELTAIAGFS VQGGDLEASA TESAVRRVRT YRLREPAVAM
     AAIPSPAGQL RLAVYGRSGQ VHFYDLTDGS VVGEPITLRH AAEVVAMAAL SDEDGRVVLY
     TADRDGQLSC WSSEDGSLLA RHQGFPRRPV AMAGFGHADR SQSLWAVDDE GHTHLWDPIA
     LRATRPDIPL FDGRTATTVP RVAGPSALLV AESTGLVYRC ELDGSDRVVL SIIGPAAART
     IVGLSDSPYE CASLGDQDDL VQVWEMSVAP RRAAPHDRTG QDTGRIVADR YRLVRQIGRG
     GAGEVWKAVD ELGGSAVVVK LFDRSRGGRD SRRLSRFLSQ AETVRGLRHR GITTVRDAGV
     EDDTGYLVLD LIDGPDLRGV LAGGRLPLSR AVAVARRVAE ALDYLHDHGV VHHDIKPANI
     LIPAAGEAVL CDYGFDWAGP RWSGSDTTSV EISRELVTPR YMSPEQAGGA VAGPTSDLYS
     LGCVLYEMLT GAPPFTDRSE ALLTSRHIDT APAFPQQIEP EVPQALDVLV RELLQKDPDL
     RPQTAAEVAR RLASPGVLRR PDRPAESESE SPLRFTVLGP VRAWRGEDPV ELSPRQLAVL
     AVLILNHGRP VTTSELVDAV WQRAPRSAAE ELGTYLRQIR RALNAGSAEP DVLVSGNDGH
     TLRVGAGAVD VVLFEDQLHR ADEDLRNDDP RAALRHVRDA LAVWKGRPLE DVPGPFASAQ
     RARLQERHLD AQEVWFEAEL WLGQAAELVA ELQELTFEYP LRERLRAFLM LALYRSGRSA
     EAVDVYIDTQ RVLREEHGRR PGAELADLYG RILAQDPGLL LPGQGPRFLI LGPLKAWRDE
     PLSLGPPQQQ AVLAILLLNA GRTVTVQTLV DGIWGDRPPQ AVAAVRTYVS RLRAVIDPSH
     RVRQPHQVLM SVADGYALMV PPASIDLSEF DSRMAEATSA RAAGALDRAY ELLLSALSLW
     QGTPLAGIPG PYAERRRAEL AERRIAALEV LHTVALDLGR HEESAGELAL LAADHPLRER
     LRALQMLALH RCRRSAEARN VYRGARQLLV EELGVEPGPV LTALYRRIDA DDPDLLHGSV
     DDLFERLTAV EPVQPPTGGR LPLVLDKIAL PDGFEFPELG VAFGIDDTDL APVFIDFETD
     PLLIVLGESE SGKTALLRLL IEKITQRYAP DQAGIVVGDY RRSLLGVVPT AYLMDYAASA
     PRLAEIAETV RGACEQRLPG PDVTPEQLRN RSWYTGKDMF VIVDDYELVA TSSGNPLAPL
     AEYLPFARDL GLRIIIARNS NGAGRAMYEP IMQRMKELGG QGVLLSGDEQ EGELLHGVRL
     QPLPPGRGIY VSHRHRSGTL VQTALLPPSG PLAIEAAPSP PG
//
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