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Database: UniProt
Entry: S4XT10_SORCE
LinkDB: S4XT10_SORCE
Original site: S4XT10_SORCE 
ID   S4XT10_SORCE            Unreviewed;       682 AA.
AC   S4XT10;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 55.
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=SCE1572_11140 {ECO:0000313|EMBL:AGP35015.1};
OS   Sorangium cellulosum So0157-2.
OC   Bacteria; Myxococcota; Polyangia; Polyangiales; Polyangiaceae; Sorangium.
OX   NCBI_TaxID=1254432 {ECO:0000313|EMBL:AGP35015.1, ECO:0000313|Proteomes:UP000014803};
RN   [1] {ECO:0000313|EMBL:AGP35015.1, ECO:0000313|Proteomes:UP000014803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=So0157-2 {ECO:0000313|EMBL:AGP35015.1,
RC   ECO:0000313|Proteomes:UP000014803};
RX   PubMed=23812535; DOI=10.1038/srep02101;
RA   Han K., Li Z.F., Peng R., Zhu L.P., Zhou T., Wang L.G., Li S.G.,
RA   Zhang X.B., Hu W., Wu Z.H., Qin N., Li Y.Z.;
RT   "Extraordinary expansion of a Sorangium cellulosum genome from an alkaline
RT   milieu.";
RL   Sci. Rep. 3:2101-2101(2013).
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; CP003969; AGP35015.1; -; Genomic_DNA.
DR   RefSeq; WP_020734202.1; NC_021658.1.
DR   AlphaFoldDB; S4XT10; -.
DR   STRING; 1254432.SCE1572_11140; -.
DR   KEGG; scu:SCE1572_11140; -.
DR   PATRIC; fig|1254432.3.peg.2490; -.
DR   eggNOG; COG0515; Bacteria.
DR   HOGENOM; CLU_025729_0_0_7; -.
DR   OrthoDB; 5489674at2; -.
DR   Proteomes; UP000014803; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd14014; STKc_PknB_like; 1.
DR   Gene3D; 3.40.50.10140; Toll/interleukin-1 receptor homology (TIR) 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; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR000157; TIR_dom.
DR   InterPro; IPR035897; Toll_tir_struct_dom_sf.
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; PF00069; Pkinase; 1.
DR   Pfam; PF13676; TIR_2; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SMART; SM00255; TIR; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF52200; Toll/Interleukin receptor TIR domain; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS50104; TIR; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}.
FT   DOMAIN          1..143
FT                   /note="TIR"
FT                   /evidence="ECO:0000259|PROSITE:PS50104"
FT   DOMAIN          231..478
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   COILED          162..196
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         261
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   682 AA;  73989 MW;  EC629F4DD6D340AC CRC64;
     MAVNVFISYA PADRPHLEAL EAHLAALKRQ GLVSTWHRGR IGAGAVRDAS IAAELSAAEV
     VLLLVSEAFL ASDSCYEREL GAALERHRRG EARVVPILVR ACDREGTALA DLEALPRDGG
     AVTSWANPDE AWRDVVRGVR AAVEEAAASA RPEAAPARAA PASALAATLR EAEEAIRAID
     KQIAAAQKRR VRLKAAGAST VEVDQEIVDL RRKRREGGQL HVGEELSEGR YLLLERIGRG
     GFATVWRALD AGRGDQPVAI KVLHPNLAGD EGRRERFFRG ARAMAELDHP GVVRILEPKG
     EDGGWHYFVM ELVHGEDVQS AVVGKRLPAE GVIPMILRAG EAISFAHGRG LVHRDVKPAN
     ILLDGEGLPR ITDFDLVWAR DTTGGTRSGA LGTFLYAAPE LMHRPQDADA RADVYGLGMT
     AVFCLHGGEL PPIMMRYPGR VIERLPCGDA VRKVLERAIE FEASERYPDV AAFCEALRGA
     AESEGGPARE GSSGTGILQG EAGLQAHERS RRLPGGLVEA FERELGEGGP IRRTLKQIMV
     AGEQLELAVP PASPVAGTNK TRHSLGTSTL RFHVSRDEEH VRIEAVWGDG ARQLGELTAF
     YALLLLARER RKDAAVCLPE DEQGWIHEAD LAEQLGVEKK HLNVLIYRAR RAFADAGLGT
     EIVERRRQAI RIATGRVEEL KA
//
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