ID A0A1Q6YQV8_9CHLR Unreviewed; 1169 AA.
AC A0A1Q6YQV8;
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:OLB40115.1};
GN ORFNames=AUH05_09920 {ECO:0000313|EMBL:OLB40115.1};
OS Ktedonobacter sp. 13_2_20CM_53_11.
OC Bacteria; Chloroflexota; Ktedonobacteria; Ktedonobacterales;
OC Ktedonobacteraceae; Ktedonobacter.
OX NCBI_TaxID=1805233 {ECO:0000313|EMBL:OLB40115.1, ECO:0000313|Proteomes:UP000185646};
RN [1] {ECO:0000313|EMBL:OLB40115.1, ECO:0000313|Proteomes:UP000185646}
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:OLB40115.1}.
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DR EMBL; MNDA01000265; OLB40115.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q6YQV8; -.
DR Proteomes; UP000185646; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011009; Kinase-like_dom_sf.
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; IPR019734; TPR_repeat.
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; PF13401; AAA_22; 1.
DR Pfam; PF00196; GerE; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR00364; DISEASERSIST.
DR PRINTS; PR00038; HTHLUXR.
DR SMART; SM00421; HTH_LUXR; 1.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00028; TPR; 3.
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; 1.
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.
DR PROSITE; PS50005; TPR; 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}; TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339}.
FT DOMAIN 14..267
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REPEAT 832..865
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 1102..1167
FT /note="HTH luxR-type"
FT /evidence="ECO:0000259|PROSITE:PS50043"
FT BINDING 43
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1169 AA; 128043 MW; 0A0A54FBDA4CC81B CRC64;
MTMTERVGQH LGNYHISRLL GTGVFADVYL SEHLYLNTQA AMKILHTPLD VHAQDSFLTE
ARYLSHLIHP HIIRVLEFGM QDQVPYLLMD YAPWGNLRQQ HPQGTVVPLA TVVSYVTAIA
SALQYAHDQH VLHRDLKPEN LLLGARNEVL LSDFGLALLT SSADEAGVRE RFGTLAYMAP
EQIQGQPSPA SDQYALAVMV YEWLSGSRPF GGTAAELSSQ HLLAEPASLR EQHPEIPPEV
EQVVFKALSK DPALRYVDVL SFASAFEDAS HVASLPSNFS GRPVGVAIEA GEANTTLRKS
QAYVKKLPTP LTPLIGRKQE LQAAHARLSR PEVRLLTLTG PPGVGKTRLA LALGSEMLEE
FAQGVCFVSL APISDADLVI PTIIGTLGLP ESGDRSPFEH LEAYLRDKQL LLLLDNFEHL
LPAASWLSEL LVSCPLLKVL VTSRATLHVH GEYEFAVLPL AIPDLQALPA NETLSQLAAV
KLFVQCTEAV KPGFALTEGN AAVIAEICVR LEGLPLAIEL AAARCKLLPL QALLARLEHS
LAVLSGGKRD GPGHQQALGT TIGWSYDLLT TEEQTLFRQL CIFVGDFTLE AAEAVSTSAG
GRTTSILDGV ASLLDKSLVQ QREEEGREPR LHLLETIREY GIERMAALGE LEQCRDAHAA
YYLELVERAE PALDDDTQVT VLAVLEREYK NIRAAIAWLL KRGMAETALR IASALRQFWF
LRGRLSEGVS ELTLALEARE EGNMQMADQV RAKALYALGY LWFFLRDPKR PPVLFQESLE
LFLRMEDKRG IAACLHRLGA AIYILGEVER GLAMGEEGLS LSRESRDSTS CAETLLSIGV
SFLANGKYDR AYEVLDESLA LYRITGSVWG RATCLHYLAM AQLSLGAIAK AYSLSGESLA
LMQTLKTPYI VVEALTVCAF EATVLGEETG AHALLEEAQA VARETESAED QERVLWGLGH
LALRQGDLAQ ARELYTHCVK RTKGKFLIPR FKWVVASCLE GLAEIALARG QATWAVQLVG
AAEAVRRARG YYSPLCIEQP CYDRTLAEAR SRLSEKGFAV AWAAGQAMTP EQALAAEKHT
PLLVQNPSVP PARREPAPTP VAPDIPQPLT AREVEVLRLV ATGMSNHQIA EQLVVSPNTV
NAHVQSIYRK IDINSRSAAT RFALEHQLV
//
