ID A0A1L8WRW8_9ENTE Unreviewed; 671 AA.
AC A0A1L8WRW8;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=RV14_GL000999 {ECO:0000313|EMBL:OJG83765.1};
OS Enterococcus ratti.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=150033 {ECO:0000313|EMBL:OJG83765.1, ECO:0000313|Proteomes:UP000182152};
RN [1] {ECO:0000313|EMBL:OJG83765.1, ECO:0000313|Proteomes:UP000182152}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15687 {ECO:0000313|EMBL:OJG83765.1,
RC ECO:0000313|Proteomes:UP000182152};
RA Zhong Z., Sun Z., Liu W., Zhang W., Zhang H.;
RT "Draft genome sequences of 29 type strains of Enterococci.";
RL Submitted (DEC-2014) 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:OJG83765.1}.
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DR EMBL; JXLB01000002; OJG83765.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1L8WRW8; -.
DR STRING; 150033.RV14_GL000999; -.
DR Proteomes; UP000182152; 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-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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}; Kinase {ECO:0000313|EMBL:OJG83765.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000182152};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:OJG83765.1};
KW Transferase {ECO:0000313|EMBL:OJG83765.1};
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 5..262
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 356..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..562
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 563..631
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 628..671
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 646..664
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 34
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 671 AA; 73550 MW; C8091B38E317FACA CRC64;
MNGRYQITGN IGSGGMANVF LAHDLILDRD VAIKVLRFDF QNDQTAIRRF QREALAATEL
VHPNIVSVYD VGEEDNMQYL VMEYVKGMDL KRYIQTHYPV PYETAVNIMQ QILSAISLAH
SHQIIHRDLK PQNVLIDNEG VVKITDFGIA IALSETSITQ TNTMLGSVHY LSPEQARGSM
ATKQSDIYAL GIILYEILTG SVPFDGESAV TIALKHFQDE LPSIKDLDPA TPQALENIVL
KATAKEPSDR YKSAEEMSED LATALSPVRV NEAKWQPQAM NNETKVLSPI EEDTPMPESF
KTMPLPQEKS EEELVPAEEE KLPDPKIQKH KKWWLILLVS LALLGIGAVA FFVFGGRDEV
VVPNVSGLSE SSAIETLTNA DLEVAAKTEK IADDKIEEGS VVKTDPAAGT TVKQKRKVIL
YVSSGKKKIK LEDYIGRSYD EVSNQLKKMG FSSDRIKREE AFSNDVEKGM IISQSEGEGT
RVDPTTDTIS FVVSQGAQPT MSDYTGQNYE TVRGMLNSNG YKNVSATYDY SDRVPAGAII
SQLPNSGEPL TESSYISFVV SQGPNVKTLN DISGYTKSDA QSYLSDIGAE YIGHESYEYS
ETVDKDKVIR TIPGVGASIS PGTIVNVIYS KGPEPEKESS SSEKETSSSS KDSTGSSSSS
KEESSTSSTE K
//
