ID G2LGC4_CHLTF Unreviewed; 746 AA.
AC G2LGC4;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:AEP12637.1};
DE EC=2.7.11.1 {ECO:0000313|EMBL:AEP12637.1};
GN OrderedLocusNames=Cabther_A1891 {ECO:0000313|EMBL:AEP12637.1};
OS Chloracidobacterium thermophilum (strain B).
OC Bacteria; Acidobacteriota; Blastocatellia; Chloracidobacterium.
OX NCBI_TaxID=981222 {ECO:0000313|EMBL:AEP12637.1, ECO:0000313|Proteomes:UP000006791};
RN [1] {ECO:0000313|EMBL:AEP12637.1, ECO:0000313|Proteomes:UP000006791}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B {ECO:0000313|EMBL:AEP12637.1,
RC ECO:0000313|Proteomes:UP000006791};
RX PubMed=21951563; DOI=10.1111/j.1462-2920.2011.02592.x;
RA Garcia Costas A.M., Liu Z., Tomsho L.P., Schuster S.C., Ward D.M.,
RA Bryant D.A.;
RT "Complete genome of Candidatus Chloracidobacterium thermophilum, a
RT chlorophyll-based photoheterotroph belonging to the phylum Acidobacteria.";
RL Environ. Microbiol. 14:177-190(2012).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002514; AEP12637.1; -; Genomic_DNA.
DR RefSeq; WP_014100374.1; NC_016024.1.
DR AlphaFoldDB; G2LGC4; -.
DR STRING; 981222.Cabther_A1891; -.
DR KEGG; ctm:Cabther_A1891; -.
DR HOGENOM; CLU_372431_0_0_0; -.
DR OrthoDB; 111294at2; -.
DR Proteomes; UP000006791; Chromosome 1.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR43671:SF13; LD04361P; 1.
DR PANTHER; PTHR43671; SERINE/THREONINE-PROTEIN KINASE NEK; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF13432; TPR_16; 1.
DR Pfam; PF14559; TPR_19; 1.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50005; TPR; 2.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:AEP12637.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000006791};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:AEP12637.1};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW Transferase {ECO:0000313|EMBL:AEP12637.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 452..479
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 45..312
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REPEAT 576..609
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 698..731
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REGION 325..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 482..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..356
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..389
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 746 AA; 79873 MW; 07991474F2A24BE7 CRC64;
MKRCPTCGTE YPDNAQFCPH DGATLVSVTA APDDPFIGQV LAGRYEILSK LGEGGMGSVY
AARHRTLGRI DAVKVLRPEA AGTDAGRRFL REAKLAASIN HPNAVVIHDF GQTESGVTFL
AMEYIQGQSL TKLLQREGPL PLARVVNIIR QVASALDAAH HLGVIHRDLK PDNIMVMEGD
RVKVVDFGIA KAVGGQESVV PMTQVGFVVG TPHYMSPEQV MGSPLDARSD VYSLALVAYE
MLTGARAFAG DSMQAQMVAR LSEPPRPMSV AAPQVTVPAV IEEVVRQALA RQPAERPASA
GAFAAELEKA LLVAENAQAV AASRAGSVQT RQQEGKASTA SASSPVTAQP SSRDEQLRSP
AALGASPAPL PTVVQHPPSS PPLTPHPYSG AGFYPPATPG SAPGLPSTPA TVLQPGSLPP
PVAPVASAPL PSALLSASPA SVPASGKAKT NIWLIVGLVA AAGGVLLTLV IVAVFLAYVS
TSSSEPGTEP VSGAPAPRQK GRQPDKALVS ILEQSRALRE SGDYESALHV VDEALAVSPT
SPELRIEKAE ILFEQEHFVE SEDLVYGVLR SHPDYGPAYQ NLGVLQYRQR KLAEAIASLK
RCLELDPEPE YASYAHAGLA QIYAEQYFSD KRRFAARSNE AEMEARWALS TATRKSLEVY
PRLTLATLLI DRQQYALARE QVAKLLRDNA FRKDQARALA YYQLAVVAFS ERKYDEAAEA
AEYAAQLDPQ TEDYRKLAEN LRQYRR
//
