ID A0A0K1F8U2_9MICO Unreviewed; 650 AA.
AC A0A0K1F8U2;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=ADJ73_05100 {ECO:0000313|EMBL:AKT50837.1};
OS Arsenicicoccus sp. oral taxon 190.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Arsenicicoccus.
OX NCBI_TaxID=1658671 {ECO:0000313|EMBL:AKT50837.1, ECO:0000313|Proteomes:UP000065578};
RN [1] {ECO:0000313|Proteomes:UP000065578}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0371 {ECO:0000313|Proteomes:UP000065578};
RA Holder M.E., Ajami N.J., Petrosino J.F.;
RL Submitted (JUL-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};
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DR EMBL; CP012070; AKT50837.1; -; Genomic_DNA.
DR RefSeq; WP_050347350.1; NZ_CP012070.1.
DR AlphaFoldDB; A0A0K1F8U2; -.
DR STRING; 1658671.ADJ73_05100; -.
DR KEGG; ars:ADJ73_05100; -.
DR PATRIC; fig|1658671.3.peg.1036; -.
DR OrthoDB; 9762169at2; -.
DR Proteomes; UP000065578; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR CDD; cd06577; PASTA_pknB; 3.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 3.30.10.20; -; 3.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR005543; PASTA_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR NCBIfam; NF033483; PknB_PASTA_kin; 1.
DR PANTHER; PTHR43289; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED; 1.
DR PANTHER; PTHR43289:SF6; SERINE_THREONINE-PROTEIN KINASE NEKL-3; 1.
DR Pfam; PF03793; PASTA; 3.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00740; PASTA; 3.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51178; PASTA; 3.
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}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 369..390
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 9..277
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 395..460
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 461..528
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 529..591
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 415..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 556..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 599..650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..582
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 605..650
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 650 AA; 67572 MW; F4D64CD5930AD845 CRC64;
MSRLIGGRYE LGEEIGRGGM ATVHAAYDTR LGRPVAIKML HAGRLGDRSF QGRFRREAQA
AASLSHPNIV AVFDSGEDVL TTSVGVQEVI PYIVMELVQG HTLSQLMHDH GPFAPDDAMR
IVEKVLAALG YSHDRGLVHR DVKPGNVMLT PAGDVKVMDF GIARGGAEAT ATMTQTQAVI
GTAQYLSPEQ ARGQDVDGRS DLYSAGCLLF ELVAGRPPFV GDSPLAIAYQ HVGEDPSLPS
SHEHSIPRSL DTVIMHALIK DRERRYQSAD SFRRDLEAAR AGRPLSDEAR ATASALFAPT
ESIQRTEAPP ASYADGARAG GGATAAGAGL GAAAGATAAG IRPGVEGPGR DGPVTSSYPA
VAEDDNRRYV AWIAVLVALL ALTGLGVWWL TRPDPIAYKT VPVLVGETEA TARSKLQSSG
LQGSFTTKTS RSPKGTVVET DPPAGSQQDP ANPVTVVLSS GPSEVVVPDV RKYTTASAQQ
RLTNASLAAG AVKVVDDKTI PEGQVVRTDP AIGQTVPVGS KVALFVSSGK MPVPNVVGQD
WEGAAKALTD AGFRVARQDK PSTQTPGTVL DQDINDGSQP PGTKITLTVA VVTPTTTVTV
TSTAPAPPPT TPAPAPPSPR PTSTPTPTPT GTAPPTTQPT PAPPTTPPTP
//
