ID E9DKA6_9STRE Unreviewed; 621 AA.
AC E9DKA6;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 51.
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=HMPREF0848_01062 {ECO:0000313|EMBL:EFX55465.1};
OS Streptococcus sp. C150.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=435842 {ECO:0000313|EMBL:EFX55465.1, ECO:0000313|Proteomes:UP000005993};
RN [1] {ECO:0000313|EMBL:EFX55465.1, ECO:0000313|Proteomes:UP000005993}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C150 {ECO:0000313|EMBL:EFX55465.1,
RC ECO:0000313|Proteomes:UP000005993};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Earl A., Feldgarden M., Gevers D., Young S., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A.M., Borenstein D., Chapman S.B., Chen Z., Engels R.,
RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E.R.,
RA Heiman D.I., Hepburn T.A., Howarth C., Jen D., Larson L., Mehta T.,
RA Park D., Pearson M., Richards J., Roberts A., Saif S., Shea T.D.,
RA Shenoy N., Sisk P., Stolte C., Sykes S.N., Walk T., White J., Yandava C.,
RA Sibley C.D., Field T.R., Grinwis M., Eshaghurshan C.S., Surette M.G.,
RA Haas B., Nusbaum C., Birren B.;
RT "The Genome Sequence of Streptococcus sp. C150.";
RL Submitted (MAR-2010) 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};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004162};
CC Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004162}. Membrane
CC {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004167}.
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DR EMBL; GL698449; EFX55465.1; -; Genomic_DNA.
DR RefSeq; WP_008535145.1; NZ_GL698449.1.
DR AlphaFoldDB; E9DKA6; -.
DR eggNOG; COG0515; Bacteria.
DR eggNOG; COG2815; Bacteria.
DR HOGENOM; CLU_000288_135_2_9; -.
DR Proteomes; UP000005993; Unassembled WGS sequence.
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 GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR CDD; cd06577; PASTA_pknB; 2.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 3.30.10.20; -; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR022686; G2P_N.
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; 3.
DR Pfam; PF05144; Phage_CRI; 1.
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}; Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW Cell division {ECO:0000256|ARBA:ARBA00022618};
KW Kinase {ECO:0000313|EMBL:EFX55465.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Transferase {ECO:0000313|EMBL:EFX55465.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 341..361
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 12..277
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 363..430
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 431..502
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 504..578
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 294..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 470..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 582..621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 42
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 621 AA; 67687 MW; 0CFDA87FB32E3130 CRC64;
MIQVGKLFAG RYRILKAIGR GGMADVYLAN DLILDNEEVA IKVLRTNYQT DQVAVARFQR
EARAMAELSH PNIVAIRDIG EEDGQQFLAM EYVDGSDLKK YIQDHAPLSN QDVVRIMGEV
LSAMTLAHQK GIIHRDLKPQ NVLLTKDGTA KVTDFGIAVA FAETSLTQTN SMLGSVHYLS
PEQARGSKAT IQSDIYAMGI MLFEMLTGHI PYDGDSAVTI ALQHFQKPLP SILAENHNVP
QALENVVIRA TAKKLENRYH STLEMSRDLV TSLHPSHSRD AKVVFDDMTD TKTLPKVDPV
PSATLEKKTA AQPSEPTPTQ SKHPRKKPSP AKKKKNLFST LLKVFLGLVF IGIIIFAYLV
FTNPDNAQVP NVVGQELSTA QTKLESAGFK VGDVKEVEDD SVDKGKVIKT DPTAGTTRKE
GTSIDVYVSS GDKGFTLKDY KGKNYKDAVK DLTSNYGVSE DQIDIQNVED DSADEGEILS
QSPGKNKTFN PKDSKAKIKF RVATPKTITM PDVTGLTVST AVQTLNRKDI SSSNIEYHDY
NTGAKLDKDK VPSSTEVLYQ DPQVGTAVDG TVILYVSITT ASSSLQSSST STTHSSSTSS
STESTSSSTE TSTEATHTEQ Q
//
