ID A0A1H3M5Z5_9MICO Unreviewed; 566 AA.
AC A0A1H3M5Z5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=SAMN05216554_1271 {ECO:0000313|EMBL:SDY71639.1};
OS Herbiconiux ginsengi.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Herbiconiux.
OX NCBI_TaxID=381665 {ECO:0000313|EMBL:SDY71639.1, ECO:0000313|Proteomes:UP000198891};
RN [1] {ECO:0000313|EMBL:SDY71639.1, ECO:0000313|Proteomes:UP000198891}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.3491 {ECO:0000313|EMBL:SDY71639.1,
RC ECO:0000313|Proteomes:UP000198891};
RA de Groot N.N.;
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; FNPZ01000001; SDY71639.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H3M5Z5; -.
DR STRING; 381665.SAMN05216554_1271; -.
DR Proteomes; UP000198891; 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:SF32; SERINE_THREONINE-PROTEIN KINASE PKAB; 1.
DR Pfam; PF03793; PASTA; 3.
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; 2.
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:SDY71639.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000198891};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:SDY71639.1};
KW Transferase {ECO:0000313|EMBL:SDY71639.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 335..356
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 12..280
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 365..431
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 432..499
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT BINDING 41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 566 AA; 59939 MW; 37816BAE910B9954 CRC64;
MTDDNRLLAG RYRLGELIGR GGMSNVYSGR DERLGRQVAI KLLKSSLAGD PVFRTRFRQE
AQAASRMAHP TIVRVFDAGE ERVAEPGGFE GVVPFIVMEF VEGKLLKDVI REGPVDSAEA
IRITEGILTA LEYSHRAGVV HRDIKPGNVM ITHGGQVKVM DFGIARAISD SSATVAQTTA
ILGTAQYFSP EQARGESVDA RTDLYSTGVV LFEMLTGEPP FKGETPVAVA YQHVSEMPVA
PSSINPMVSP AIDQVVLHAL AKDRFARFQS AVEFRTDLEI AGAGRIPSKR LPADDFQSSL
FGAPPSLAQG TEAALTQLAG DDEYAVRTQS RPPVVWIWAG IASVAVILVA IVFWVLTLQP
TDELPSASRE IPTVTGQTYE AADATLQQLD LVTARFDVYS DTIPAGQVVD TDPGTGTIVS
PGTVVSVNVS QGKEAIAVPN LQNMSATDAA NAITAAKFVV GQTNKENSAD VPADVVIRSD
PASGTQAHAG DTINIFVSTG MVTVPDVAGQ PIDVASSSLT QLLLDVKVEQ DPGCKSAPSN
PVSTQSIAPG DALQKSEITI RYCTGA
//
