ID   Q820A8_ENTFA            Unreviewed;       718 AA.
AC   Q820A8;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 133.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   OrderedLocusNames=EF_3120 {ECO:0000313|EMBL:AAO82800.1};
OS   Enterococcus faecalis (strain ATCC 700802 / V583).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=226185 {ECO:0000313|EMBL:AAO82800.1, ECO:0000313|Proteomes:UP000001415};
RN   [1] {ECO:0000313|EMBL:AAO82800.1, ECO:0000313|Proteomes:UP000001415}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700802 / V583 {ECO:0000313|Proteomes:UP000001415};
RX   PubMed=12663927; DOI=10.1126/science.1080613;
RA   Paulsen I., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R., Read T.D.,
RA   Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA   Dodson R.J., Umayam L., Brinkac L., Beanan M., Daugherty S., DeBoy R.T.,
RA   Durkin S., Kolonay J., Madupu R., Nelson W., Vamathevan J., Tran B.,
RA   Upton J., Hansen T., Shetty J., Khouri H., Utterback T., Radune D.,
RA   Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT   "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT   faecalis.";
RL   Science 299:2071-2074(2003).
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; AE016830; AAO82800.1; -; Genomic_DNA.
DR   RefSeq; NP_816730.1; NC_004668.1.
DR   RefSeq; WP_002387383.1; NZ_KE136524.1.
DR   AlphaFoldDB; Q820A8; -.
DR   SMR; Q820A8; -.
DR   STRING; 226185.EF_3120; -.
DR   EnsemblBacteria; AAO82800; AAO82800; EF_3120.
DR   KEGG; efa:EF3120; -.
DR   PATRIC; fig|226185.45.peg.453; -.
DR   eggNOG; COG0515; Bacteria.
DR   eggNOG; COG2815; Bacteria.
DR   HOGENOM; CLU_000288_135_2_9; -.
DR   Proteomes; UP000001415; 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-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd06577; PASTA_pknB; 5.
DR   CDD; cd14014; STKc_PknB_like; 1.
DR   Gene3D; 3.30.10.20; -; 5.
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:SF37; SERINE_THREONINE-PROTEIN KINASE A; 1.
DR   Pfam; PF03793; PASTA; 5.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00740; PASTA; 5.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF54184; Penicillin-binding protein 2x (pbp-2x), c-terminal domain; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51178; PASTA; 5.
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}; Kinase {ECO:0000313|EMBL:AAO82800.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000001415};
KW   Serine/threonine-protein kinase {ECO:0000313|EMBL:AAO82800.1};
KW   Transferase {ECO:0000313|EMBL:AAO82800.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        333..354
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          12..269
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          357..424
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   DOMAIN          425..495
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   DOMAIN          496..566
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   DOMAIN          567..637
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   DOMAIN          638..703
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   REGION          609..629
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          661..695
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        615..629
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        662..691
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         41
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   718 AA;  77420 MW;  B841DEF71C00CEA5 CRC64;
     MIEIGKKLNG RYHIIGSIGS GGMANVYLAH DLILDRDVAV KVLRFDFQND QAAIRRFQRE
     ALAATELVHP NIVSVYDVGE EDGLQYLVME YVKGMDLKRY IQTHFPIPYS TVVDITQQIL
     SAVAMAHEHR IIHRDLKPQN ILIDEHGTVK ITDFGIAIAL SETSITQTNT MLGSVHYLSP
     EQARGSMATN QSDIYAVGII LYEMLTGNVP FDGESAVTIA LKHFQEEIPS VKMFDPGIPQ
     SLENVVRHAT AKDPSDRYKT ANEMAEDLYT SLSASRLNEP AWEPTALLGE TKVLTPIPED
     IAEPEETTPV EVPEDIADDI LAEQPPKKNR KKLWIGLAIA ALISLAIGGL AFAMSGGKDV
     EVPDVTNETK ADASQALKSA GLKVDSETKK IPDDKIEEGK VVKTDPEAKS SVKKGRSVTL
     YISSGTEKIE MADYTKESYE SAVEALKKLG FSEDQITTKK EYSDSVSTDS IIKQKPAAGK
     KVDPKKDNVT LTVSQGPETV TLPSYAGYSY ENAVNALAQL GISDSQITRV DQASDTVEPG
     LVITQDPAPG GTVTPKNGQV TLYVSKGSDK VTLSDYSGIS YDNAVSRLIA LGIPESQIKR
     VDEESDKVEK DTVISQEPAS GTAVDPKNDT ITLHVSKGSD SVTVPDISGY SPKAAEDSIN
     NAGLKINEQG LSGSGDGQVV ERTSPSAGSK VKKGDSVTVY YSKANDSKST TSESSTSN
//