ID A0A0N6ZVB5_9MICO Unreviewed; 607 AA.
AC A0A0N6ZVB5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=NI26_00080 {ECO:0000313|EMBL:AIV39076.1};
OS Curtobacterium sp. MR_MD2014.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Curtobacterium.
OX NCBI_TaxID=1561023 {ECO:0000313|EMBL:AIV39076.1, ECO:0000313|Proteomes:UP000069933};
RN [1] {ECO:0000313|Proteomes:UP000069933}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR_MD2014 {ECO:0000313|Proteomes:UP000069933};
RA Mariita R.M., Bhatgnagar S., Hanselmann K., Hossain M.J., Dawson S.C.,
RA Korlach J., Boitano M., Liles M.R., Moss A.G., Leadbetter J.R.,
RA Newman D.K.;
RT "Isolation and characterization of species affiliated with family
RT Actinomycetaceae.";
RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AIV39076.1, ECO:0000313|Proteomes:UP000069933}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR_MD2014 {ECO:0000313|EMBL:AIV39076.1,
RC ECO:0000313|Proteomes:UP000069933};
RX PubMed=26722011;
RA Mariita R.M., Bhatnagar S., Hanselmann K., Hossain M.J., Korlach J.,
RA Boitano M., Roberts R.J., Liles M.R., Moss A.G., Leadbetter J.R.,
RA Newman D.K., Dawson S.C.;
RT "Complete Genome Sequence of Curtobacterium sp. Strain MR_MD2014, Isolated
RT from Topsoil in Woods Hole, Massachusetts.";
RL Genome Announc. 3:0-0(2015).
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; CP009755; AIV39076.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N6ZVB5; -.
DR STRING; 1561023.NI26_00080; -.
DR KEGG; cum:NI26_00080; -.
DR PATRIC; fig|1561023.3.peg.15; -.
DR OrthoDB; 9762169at2; -.
DR Proteomes; UP000069933; Chromosome.
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; 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:AIV39076.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000069933};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:AIV39076.1};
KW Transferase {ECO:0000313|EMBL:AIV39076.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 342..363
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 12..282
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 372..438
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 439..506
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 507..568
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 569..607
FT /note="Disordered"
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 607 AA; 63457 MW; 64EB0527BA27CDA3 CRC64;
MTAGITLLAD RYEIGDVIGR GGMATVHVGT DTRLGRKVAV KLLKPSLATD PTFRIRFRQE
AQAAARMAHP TIVRVYDAGE ETVTEPSGAQ VQVPYIVMEH VDGRALSDVL DDGPLDPAEA
VRITEGILTA LEYSHRAGVV HRDIKPANVM VTHSGQVKVM DFGIARAITD TSATVAQTTS
ILGTASYFSP EQARGETVDA RTDLYSTGVL LFELLTGRPP FVGDSPVAVA YQHVSEQPVA
PSTLVPEVSP ALDAVTLHAL VKDRTRRFQT AADFRTDLQQ AAAGKVPVST RTLQQNAAHD
ASTMLFGVNP RTTSNPAVAF RELDDDAADH RPQRTQNRPP VAWIWLGIIL TAAVIAGVVF
FVANLQPGKA PVSSSVSVPN VVGATWDSAR TELEKRDLSA VEVGENSDDV AKDTVIRTEP
GEGTNVARKQ SIRVVVSLGP EQVAVPDVAN QTQDAAEQAL KDAGFAVGAI NSDYSSDVPE
GTVMSSDPGS STQLTKGSVV NLTVSNGKVQ MPDVTQQPIS AANEALANLG LKVVASPTYT
CTGSTVVQQS VPQGDVAQGS TITLTYCAAS AQRPSQAPSV PDRGGDDSSG SDGGGGSGTV
QGGGAGQ
//
