ID A0A0A2WLJ4_9GAMM Unreviewed; 941 AA.
AC A0A0A2WLJ4;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=LF41_3162 {ECO:0000313|EMBL:KGQ19130.1};
OS Lysobacter dokdonensis DS-58.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Lysobacter.
OX NCBI_TaxID=1300345 {ECO:0000313|EMBL:KGQ19130.1, ECO:0000313|Proteomes:UP000030518};
RN [1] {ECO:0000313|EMBL:KGQ19130.1, ECO:0000313|Proteomes:UP000030518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS-58 {ECO:0000313|EMBL:KGQ19130.1,
RC ECO:0000313|Proteomes:UP000030518};
RA Kim J.F., Kwak M.-J.;
RT "Genome sequences of Lysobacter dokdonensis DS-58.";
RL Submitted (SEP-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:KGQ19130.1}.
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DR EMBL; JRKJ01000009; KGQ19130.1; -; Genomic_DNA.
DR RefSeq; WP_052116274.1; NZ_JRKJ01000009.1.
DR AlphaFoldDB; A0A0A2WLJ4; -.
DR STRING; 1300345.LF41_3162; -.
DR PATRIC; fig|1300345.3.peg.1699; -.
DR eggNOG; COG0457; Bacteria.
DR eggNOG; COG0515; Bacteria.
DR eggNOG; COG3063; Bacteria.
DR OrthoDB; 9801841at2; -.
DR Proteomes; UP000030518; Unassembled WGS sequence.
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; cd14014; STKc_PknB_like; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
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; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
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; PF13374; TPR_10; 1.
DR Pfam; PF13424; TPR_12; 1.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00028; TPR; 4.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF48452; TPR-like; 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}; Kinase {ECO:0000313|EMBL:KGQ19130.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000030518};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:KGQ19130.1};
KW Transferase {ECO:0000313|EMBL:KGQ19130.1}.
FT DOMAIN 76..361
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 107
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 941 AA; 104106 MW; CBDEA6F731235E42 CRC64;
MDPERWQRLS PLLDALFELD QDERERSLRL MREEDPQTAE DLEALLKLET DREDFLSEPL
VAPLPGPRPG VEVGPYRLER LLGEGGMGQV WLAARADGLY QRRVALKLLR PGLVDPNLRV
RFTRERQILA RLAHPHIARL LDAGVSHDHQ PYLALEYIEG EPITDYCRVH RLSLESRLDL
FHQVCDAVSH AHANLIVHRD LKPSNILVTP AGDVRLLDFG IAKLIDADVA APEQTRTGVR
AFTLHYAAPE QVRGEPVSTM TDVYSLGVVL YELLADAKPY RLKRQTDAEW EEAILQGDPT
KPSSALQRQA DAGEGDTAML RRRARNVTGD LDNIVLKALA KKPEQRYPSV EAMSLDLERY
LAGKPVLARP QSVGYRLRKY VVRHRWALAT GIVVTGVLGA ALTIVSWQGQ QAVQETARAQ
ALQDFVIGLF EGAGAAPRDD AIDMRSLLDN GIVRANRELA RQPLARAEVF GIIARLRIGL
GDYPEAMSLL QRQAEILKAV GDDAPASLQL EAATQQGLAH RQLDDPRTCV DAMQPWMERA
RREQSQLPAQ VAEFYSQLAR CRSAVGEFNS ARQLLEYSMT IRRETLDDEA GVAENLYDLA
NVDADDGKPD IALASLRNAL AFLHQRVGER HPLAIQIHRR IAILLREKGR PAEAAKSVDA
ALALSAELLG ERHPTTLALH RQRASVYMEQ GWLDVAERDL RDTTPLLIER VGERHVDVGA
SFYTLGMLAW EQGRLEEAER DLAQAVAIWR TSSARTRMVR AMAEHAQVLQ ALGRVDQARG
EVAQAKQLAV AQLGLKHPFV ADVEYAHGLI LANEGDHAGA KARLASAVKL SRNAEGQPAI
DTQAMELSLA RELARDGDKN ALATLARMAG AASTNASEPR NLRWRARAYL GEANCRGADA
SKANADLDAL AAEMRTGLPQ GGRLPREVET IRRACVPLPM Q
//