ID S1N2Z9_9ENTE Unreviewed; 737 AA.
AC S1N2Z9;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
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=I568_02344 {ECO:0000313|EMBL:EOW79993.1};
OS Enterococcus columbae DSM 7374 = ATCC 51263.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=1121865 {ECO:0000313|EMBL:EOW79993.1, ECO:0000313|Proteomes:UP000014113};
RN [1] {ECO:0000313|EMBL:EOW79993.1, ECO:0000313|Proteomes:UP000014113}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51263 {ECO:0000313|EMBL:EOW79993.1,
RC ECO:0000313|Proteomes:UP000014113};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A., Russ C., Gilmore M., Surin D., Walker B., Young S., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Enterococcus columbae ATCC_51263 (PacBio/Illumina
RT hybrid assembly).";
RL Submitted (MAR-2013) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EOW79993.1}.
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DR EMBL; ASWJ01000011; EOW79993.1; -; Genomic_DNA.
DR RefSeq; WP_016184057.1; NZ_KE136498.1.
DR AlphaFoldDB; S1N2Z9; -.
DR STRING; 1121865.OMW_01951; -.
DR PATRIC; fig|1121865.3.peg.1896; -.
DR eggNOG; COG0515; Bacteria.
DR OrthoDB; 9788659at2; -.
DR Proteomes; UP000014113; 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 CDD; cd06577; PASTA_pknB; 4.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 3.30.10.20; -; 4.
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; 4.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00740; PASTA; 4.
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; 4.
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}; Reference proteome {ECO:0000313|Proteomes:UP000014113};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 343..364
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 12..272
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 367..435
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 436..506
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 507..576
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 577..643
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 310..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 541..560
FT /note="Disordered"
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 737 AA; 80427 MW; B2EEA2F0F177C0C6 CRC64;
MTEIGKKFNG RYLILGNIGS GGMANVFLAR DLILDREVAI KVLRYDFLND QSAIRRFQRE
MLAATELVHP NIVTVYDAGQ EEQTQFLVME YVKGMDLKRY IQTQYPIAYD RIVDIMQQIL
SAVSLAHQHR IIHRDLKPQN ILIDEQGTVK ITDFGIAVAL SETSITQTNS MLGSVHYLSP
EQARGSMATN QSDIYAIGII LYEMLTGKVP FDGESAVTIA LKHFQSEIPS IRIYNKDVPQ
SLENIVLKAT AKDPLDRYQS AEEMSADLAT ALEPQRLAEP VWHPNHVMEE TKVIPTATLS
QIEPVQAEEV KPEVEQLTHS KNEDSLAAQG KPAKKKKPSK KKLAIIGSAL LVLLAALLTL
FFVYGGGQNE VSVPSVAGLS ESAARSKLTN AGFKVADQTE SITSDKIAEG KVVKTDPEAK
AVVQKGRTIV LYLSSGSQKI KIKDYTGTDY KETLTALLKL GFKHAQIKKT EKYDDTVEKG
KIISQTPTAG SEVAPTKDKL SFVVSKGPKP VKMGNYMGMQ VNDAIADLNA RGITSSQIKQ
TYQTSEQPEG TVLSQNPSSD AQIIPGKTTI TLVVSSGSDQ VELPNLVGLT RDQVQSQADE
KGFKVNFEEE YSDQTPAGQV ISMDPQAGQK VKKNSSVTVT LSKGSNTSTF TVDVLATYKG
NAQDSASQTV TIWVKDATTG DSKKQVQSFI LDASNNNKRV SVDVSVQQGG TATIYAQRDN
EKEVSTVVSK ATTIQVP
//
