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Database: UniProt
Entry: A0A370MX93_9BURK
LinkDB: A0A370MX93_9BURK
Original site: A0A370MX93_9BURK 
ID   A0A370MX93_9BURK        Unreviewed;       605 AA.
AC   A0A370MX93;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
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=DLM46_35210 {ECO:0000313|EMBL:RDJ97998.1};
OS   Paraburkholderia lacunae.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=2211104 {ECO:0000313|EMBL:RDJ97998.1, ECO:0000313|Proteomes:UP000254875};
RN   [1] {ECO:0000313|Proteomes:UP000254875}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S27 {ECO:0000313|Proteomes:UP000254875};
RA   Feng T.;
RL   Submitted (MAY-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:RDJ97998.1}.
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DR   EMBL; QHKS01000041; RDJ97998.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A370MX93; -.
DR   OrthoDB; 9801841at2; -.
DR   Proteomes; UP000254875; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR   CDD; cd14014; STKc_PknB_like; 1.
DR   Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR036457; PPM-type-like_dom_sf.
DR   InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR43289; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED; 1.
DR   PANTHER; PTHR43289:SF32; SERINE_THREONINE-PROTEIN KINASE PKAB; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF13672; PP2C_2; 1.
DR   SMART; SM00331; PP2C_SIG; 1.
DR   SMART; SM00332; PP2Cc; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF81606; PP2C-like; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51746; PPM_2; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000254875};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        584..603
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          56..281
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51746"
FT   DOMAIN          314..579
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   605 AA;  65806 MW;  3DCE01F80091781D CRC64;
     MSGPFSPDSL PAPNTGRMPD DPERRPASRR GMGGQEIDLQ LRPERGECAA LEIGCLSCPA
     RARGQDHINE DYVGVMLGDL AARAASGSVI ALADGVSGSK GGRVAAELSV RTFIDAYYGL
     PDTLQPGVAA ARALEAIHGW LHQIGRVDPA LKQMAASFAA LIVRRATAYL VAAGDVRLYL
     LRDGQLTQLG DDDVMPVAFG SYVAHAVGMH PTLVTRIETL ELREGDRLLM CSDGLYRRVP
     MRELQTVLAA RSSALDTARR LDALAVARGS QDDVTSVVVD VGSLPLLDVG YLERVVGALP
     IPAVPDAGHV VDGYLLKSVL SDGFYSRIFA GYDLADPNTP LALKFPKPRV EQDENVRQSI
     VRERWLAGKI GDDGVLAPLP VDADRQTRLY VVMPLGAGVT LEKLLAAPQP IALPRALKIA
     RQLGRSIDAL NRRNIFHRDI KPENVLVMRG DDTRLLDLGF GYMPGMQVPG PDVAPGSPAY
     MAPELMKGAL GDARSEVFAY GVTLYRLFSG GRLPYGFNGR VPLYHYRPDA PQWLDLVLEK
     ALQPDPARRY QDVLEVCADL ERFSSDRDAL APARRKPLLE SDPVLFWQSV VVLLLALLLW
     SLMRH
//
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