ID A0A1Q7URY2_9CHLR Unreviewed; 1171 AA.
AC A0A1Q7URY2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OLE06439.1};
GN ORFNames=AUG82_03430 {ECO:0000313|EMBL:OLE06439.1};
OS Ktedonobacter sp. 13_1_20CM_4_53_11.
OC Bacteria; Chloroflexota; Ktedonobacteria; Ktedonobacterales;
OC Ktedonobacteraceae; Ktedonobacter.
OX NCBI_TaxID=1805225 {ECO:0000313|EMBL:OLE06439.1, ECO:0000313|Proteomes:UP000186213};
RN [1] {ECO:0000313|EMBL:OLE06439.1, ECO:0000313|Proteomes:UP000186213}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27843720;
RA Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA Banfield J.F.;
RT "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT heterotrophy are prevalent below the grass root zone.";
RL PeerJ 4:E2687-E2687(2016).
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 -!- 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:OLE06439.1}.
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DR EMBL; MNIY01000069; OLE06439.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q7URY2; -.
DR STRING; 1805225.AUG82_03430; -.
DR Proteomes; UP000186213; Unassembled WGS sequence.
DR GO; GO:0043531; F:ADP binding; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd06170; LuxR_C_like; 1.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
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 InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR002182; NB-ARC.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
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; IPR000792; Tscrpt_reg_LuxR_C.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR47691:SF3; HTH-TYPE TRANSCRIPTIONAL REGULATOR RV0890C-RELATED; 1.
DR PANTHER; PTHR47691; REGULATOR-RELATED; 1.
DR Pfam; PF00196; GerE; 1.
DR Pfam; PF00931; NB-ARC; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF17874; TPR_MalT; 1.
DR PRINTS; PR00364; DISEASERSIST.
DR PRINTS; PR00038; HTHLUXR.
DR SMART; SM00421; HTH_LUXR; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF46894; C-terminal effector domain of the bipartite response regulators; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF48452; TPR-like; 2.
DR PROSITE; PS00622; HTH_LUXR_1; 1.
DR PROSITE; PS50043; HTH_LUXR_2; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}.
FT DOMAIN 15..272
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1104..1169
FT /note="HTH luxR-type"
FT /evidence="ECO:0000259|PROSITE:PS50043"
FT BINDING 44
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1171 AA; 129872 MW; 8B62E7D970B2E6FA CRC64;
MSDLVTREGQ QIGAYQLIRL LGRGGSAEVY LGEHVYLKSK AALKLLPVVL QEEERAGFLR
EAQTLAHLEH PHIVRILDFA VEAGTPFLVM EYAPRGSLRL RHPGGTRLPL TTIISYVQQA
ASALQYAHNQ QLIHCDVKPE NLLLNERDEL LLSDFGLAVL AHHLHSYSTH VLERQVAGTA
LYEAPEQLQG NPVLASDQYA LGAVVYEWLC GTPPFHGSPI EIAVQHLSTP PSSLSKQIPD
LSPAVEEVVQ RALAKRPEQR FASVREFAHA LEQALQEASR SSYTSVLSVQ KTGSPLPGNG
RQSILASSKP VAIWKVPTPL TPLIGREGDV VAICALLRRP EVRLLTLLGT GGIGKTRLSL
QVAEQMRADF ADGVCFVPLA AITNPNLLVP TIAEVLEMRE IGEIKEQSLF GQVRMALRDK
HLLLILDNFE QIGMAAPQVE ELLAICPSLK IMVTSRAVLH TQGEHEFPVA PLTLPDLNQL
PGHEALTHYA AVALFLQRAR AVLPTFELTE TNARVIAEIC VRLDGLPLAI ELAAPRIKLL
PPQALLTRLA QPLRVLTGGL KTMPARQQTL RGTLEWSYKL LDDQEQQLFQ RLSVFVGGCS
LETAEATCFS GEDQADVLNM ISSLVDKSFL QQTEQEAKEP RFAMLETVRE YGLECLQASG
DIESVQRAHA EYFLRLAEEA EPHLMEAQLP VWLRQLNREQ ENLRAALRWF IEHEEADLAL
RLSGALWRYW FIRGYWAEEL HWLRAALQLS HPEEQTEARA KALSVAGMMT LYMDKNPETA
QRLVEESITF YRNVENKPGL AIALFYLGIV YKFRTDYVTA QSLMEQSAAF YREVGDKYML
AIVLNDSARV ARRQGDNVTA RALLEECAML IREVGVTWWL TRPLAQLASM ARTEGDYARA
ADLARECLAI AQEIGDMFLI VWSLTTLVEI ARFQGDYASA MAWGNQGLAI ARDKGNRQAV
TRLLCILGDV AQNQGNVAQA STHYYESLSL ALQAKDKKNT GWCLLGLARL ASAEGQFWKA
ALLAGAAEAQ LDVNRDMEPV VHEEYKRDLI AIRTRLGDEV FAGARAEGHS MTPEKALAVS
EETIISILAS VELPSTLPGE QPSTPAYPDD LTVREVEVLR LMAQGQTNVQ IAEQLVISPR
TVNSHLTSIY KKIQVTSRSA ATRYAIEHQL A
//
