ID A2SC27_METPP Unreviewed; 447 AA.
AC A2SC27;
DT 06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 99.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN OrderedLocusNames=Mpe_A0154 {ECO:0000313|EMBL:ABM93116.1};
OS Methylibium petroleiphilum (strain ATCC BAA-1232 / LMG 22953 / PM1).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Methylibium.
OX NCBI_TaxID=420662 {ECO:0000313|EMBL:ABM93116.1, ECO:0000313|Proteomes:UP000000366};
RN [1] {ECO:0000313|EMBL:ABM93116.1, ECO:0000313|Proteomes:UP000000366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1232 / LMG 22953 / PM1
RC {ECO:0000313|Proteomes:UP000000366};
RX PubMed=17158667; DOI=10.1128/JB.01259-06;
RA Kane S.R., Chakicherla A.Y., Chain P.S.G., Schmidt R., Shin M.W.,
RA Legler T.C., Scow K.M., Larimer F.W., Lucas S.M., Richardson P.M.,
RA Hristova K.R.;
RT "Whole-genome analysis of the methyl tert-butyl ether-degrading beta-
RT proteobacterium Methylibium petroleiphilum PM1.";
RL J. Bacteriol. 189:1931-1945(2007).
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DR EMBL; CP000555; ABM93116.1; -; Genomic_DNA.
DR RefSeq; WP_011827755.1; NC_008825.1.
DR AlphaFoldDB; A2SC27; -.
DR STRING; 420662.Mpe_A0154; -.
DR KEGG; mpt:Mpe_A0154; -.
DR eggNOG; COG0515; Bacteria.
DR HOGENOM; CLU_042510_0_0_4; -.
DR Proteomes; UP000000366; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00038; CAP_ED; 1.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR018490; cNMP-bd_dom_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR014710; RmlC-like_jellyroll.
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; PF00027; cNMP_binding; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00100; cNMP; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF51206; cAMP-binding domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Kinase {ECO:0000313|EMBL:ABM93116.1};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Reference proteome {ECO:0000313|Proteomes:UP000000366};
KW Transferase {ECO:0000313|EMBL:ABM93116.1}.
FT DOMAIN 18..285
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 312..413
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT BINDING 47
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 447 AA; 48992 MW; 41D149F26824A783 CRC64;
MSPSPASSDV LPERIGKYRV LRKLGEGATS EVFLCRDDFN ERDVAVKRVR ASALADVSDG
ALHARFFAAE AALVGRLQHP NVVQIFDAVP DPTEPYVVME HVAGTTLRPF CRADQLLPLD
QVVEIGFKCA MALGYVSRQG LIHRDVKPAN LLASTNANGD IVDVKVSDFG SVLNLQADTT
QVFRVGSLAY MSPEQLDGGT LDARADVYSL GAVLYHLIAG RPPFDASAQS VLMAQIYSAQ
PASLCGLRGG VEPALDAVIQ RALAKRADDR YADWDEFAQA LSALVANRQV PRGQVQGVLD
SERFTLLRAL EFFSQFGDVE LWEVVHRCAW QRYPLGHLIY RRGEEGNTFH IIAEGAVDVY
RDSQRVAHLG AGTSVGEMAY LAPNPELRRH STDVTVVAPA TMISFTPDSM ARLSPGCRHL
FDEAFIRVLV RRLHVAHEAL AHPRRIA
//
