ID A0A2Y9ASR8_9MICO Unreviewed; 635 AA.
AC A0A2Y9ASR8;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=SAMN05216184_11431 {ECO:0000313|EMBL:SSA45507.1};
OS Georgenia satyanarayanai.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Bogoriellaceae;
OC Georgenia.
OX NCBI_TaxID=860221 {ECO:0000313|EMBL:SSA45507.1, ECO:0000313|Proteomes:UP000250222};
RN [1] {ECO:0000313|EMBL:SSA45507.1, ECO:0000313|Proteomes:UP000250222}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10826 {ECO:0000313|EMBL:SSA45507.1,
RC ECO:0000313|Proteomes:UP000250222};
RA Cai Z.;
RL Submitted (OCT-2016) 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};
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DR EMBL; UETB01000014; SSA45507.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2Y9ASR8; -.
DR OrthoDB; 9762169at2; -.
DR Proteomes; UP000250222; 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; 3.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 3.30.10.20; -; 3.
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; 2.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00740; PASTA; 3.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51178; PASTA; 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:SSA45507.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000250222};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:SSA45507.1};
KW Transferase {ECO:0000313|EMBL:SSA45507.1};
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..283
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 374..441
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 442..512
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 513..581
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 548..635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..614
FT /note="Acidic residues"
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 635 AA; 67630 MW; B12A9BEB785B9FDF CRC64;
MDEVPKVLAG RYEVRELIGR GGMAEVYIGY DNRLSRTVAI KVLRSDLARD PTFQARFRRE
AQSAASLNHP AIVSVYDTGE DDVVTSAGER AHVPYIVMEY VEGHTVRSLL TDGSAVPIDE
ASEIVIGVLS ALAYSHREGI VHRDIKPGNV MLTPTGQVKV MDFGIARAMA DSAATMTQTH
AVVGTAQYLS PEQARGEVVD ARSDIYSTGC LLYELLTGQP PFSGDSAVAV AYQHVREIPK
PPSEVASDIP EALDRIVLKS LAKDREDRYP DATAMRSDLE AALRGGAVSA PATSTWAAAA
AAASQPTTVM GASPAATQAM PAARTRTAVA AEEDAEEDRR SPWWVWLLVL VGLLAAAGVA
YLLLTRDDAD EPVAPATVTV PELEGMDQTE AREAVEEEGL TFAIGDPEFS AEIEPGLFVS
SDPEVGATVE EGETVTVSFS SGPEAVEMPD VIGLSQRQAQ DQLSEQELGI PVRITYRPIN
DPDYEQDRVA QTEPEAGVAI EPDSEVVLHI ATGNVEVPDF ASDPSGDPTT FEEARDALAE
LGISVTRTAR ETGDFEPGTV LEQSRSGTVP RLTSIELVVA EPAPEPPPEP TTPSDDEPPS
DEEPPPEDEP TDEETSAVGP GNSDFGRDQG RGNGP
//
