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Database: UniProt
Entry: A0A3M8T2P8_9GAMM
LinkDB: A0A3M8T2P8_9GAMM
Original site: A0A3M8T2P8_9GAMM 
ID   A0A3M8T2P8_9GAMM        Unreviewed;       938 AA.
AC   A0A3M8T2P8;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 20.
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=EER27_04380 {ECO:0000313|EMBL:RNF85032.1};
OS   Lysobacter psychrotolerans.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Lysobacter.
OX   NCBI_TaxID=1327343 {ECO:0000313|EMBL:RNF85032.1, ECO:0000313|Proteomes:UP000267049};
RN   [1] {ECO:0000313|EMBL:RNF85032.1, ECO:0000313|Proteomes:UP000267049}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZS60 {ECO:0000313|EMBL:RNF85032.1,
RC   ECO:0000313|Proteomes:UP000267049};
RA   Luo Y., Sheng H.;
RT   "Lysobacter cryohumiis sp. nov., isolated from soil in the Tianshan
RT   Mountains, Xinjiang, China.";
RL   Submitted (NOV-2018) 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:RNF85032.1}.
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DR   EMBL; RIBS01000002; RNF85032.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3M8T2P8; -.
DR   OrthoDB; 9801841at2; -.
DR   Proteomes; UP000267049; 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; 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; PF13424; TPR_12; 2.
DR   SMART; SM00220; S_TKc; 1.
DR   SMART; SM00028; TPR; 5.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF48452; TPR-like; 2.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS50005; TPR; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:RNF85032.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000267049};
KW   Serine/threonine-protein kinase {ECO:0000313|EMBL:RNF85032.1};
KW   TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW   Transferase {ECO:0000313|EMBL:RNF85032.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        378..398
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          75..358
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REPEAT          586..619
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   BINDING         106
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   938 AA;  102710 MW;  7F8C98B8B2333D98 CRC64;
     MANTQLDRDA LQLLREVLEH APEARAGAIA ARCEGRPELR ERVEALLARV DEDETHGPLP
     PPMQPAVDGE RLGPWRLRRR IGHGGMGEVL LAERADGAFE REVAIKRIRA GYAPLAERFL
     RERAILARLQ HPQIAQLLDG GIDDHGNPWF ALEYVRGETI TRWCDQHKVG VDTRVGLLAR
     LCEAVQFAHA NLVVHRDIKP ANVLVGADGE PKLLDFGIAR LLDDGDATQT QLLAMTPSYA
     APEQRRGETP TIATDIYQLG LLLREMLGGP LPARTGEAGP PPWPRLAADY AARMRDDAAG
     ALAIASARGL APSRLQAVLR GDLERIVAVA TADEPGDRYP TAQALADDLR RWQQHLPVRV
     HRDGWAYRGR KFVRRHRVAS SLVAVLAMVA VGAGGFGWRK LQAEREQFQR AEATIAFLRD
     VFVESKPEQT EGEALTAAQL LERAAAGLPE RFGDDPRTRG QLESEVGTVF MSMGYMAKAR
     PHLRYAMEQL APERDARPDE YLQLVEYLSY ASAEDHDHQA AFDVIDANMA FARSLPQVNE
     PPAARLLLER GNALAGLGQE ERALVDYREA LALLMADGGG ATKYKARAHT NVAIALVRSG
     QVREAIPVYE QALRLHQQTP DALEADQLVA RYNLARAQSR LGETDIAIAG YEAVLPRMTK
     LLSVHHPRVA TLRLQLALSY GVRGDYRRGA DLMMAQLPHL RGKDIDPEVL AQSEGFAAKL
     LNAALRPDLA APLARQADQR LNPAGFAAAA DRPDDVHANV RHILGEVSLQ QGDLAGAERA
     FQAALQESLL LAEGKPDAGA SGAMDALGRC RLLAGDSAGA IDWFERALAM MRQRKSQATR
     VDPRLVRSEI HLQWARAVQS RDASAVLVLA AMRPRYAAAL NAAEHPLLWQ FDLLHARLAH
     DLGGAGPAPQ RLHQSRTKLQ ALAGDAPLSE PFGLVFDF
//
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