ID S2X118_9ACTN Unreviewed; 608 AA.
AC S2X118;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
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=HMPREF9306_00452 {ECO:0000313|EMBL:EPD33694.1};
OS Propionimicrobium lymphophilum ACS-093-V-SCH5.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Propionimicrobium.
OX NCBI_TaxID=883161 {ECO:0000313|EMBL:EPD33694.1, ECO:0000313|Proteomes:UP000014417};
RN [1] {ECO:0000313|EMBL:EPD33694.1, ECO:0000313|Proteomes:UP000014417}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACS-093-V-SCH5 {ECO:0000313|EMBL:EPD33694.1,
RC ECO:0000313|Proteomes:UP000014417};
RG The Broad Institute Genomics Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Saerens B., Vaneechoutte M.,
RA Walker B., Young S., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M., Berlin A.M.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Propionimicrobium lymphophilum ACS-093-V-SCH5.";
RL Submitted (APR-2013) 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:EPD33694.1}.
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DR EMBL; AGZR01000004; EPD33694.1; -; Genomic_DNA.
DR RefSeq; WP_016455302.1; NZ_KE150269.1.
DR AlphaFoldDB; S2X118; -.
DR STRING; 883161.HMPREF9306_00452; -.
DR PATRIC; fig|883161.3.peg.456; -.
DR HOGENOM; CLU_000288_135_2_11; -.
DR OrthoDB; 9769043at2; -.
DR Proteomes; UP000014417; 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-EC.
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}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000014417};
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 10..277
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 371..437
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 438..508
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 509..577
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 580..608
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 608 AA; 65019 MW; F02E06CD9585C65F CRC64;
MTGRTLSGRY KLVEIIGRGG MAEVWRARDE RLNRDVAIKQ LRVNLATDSN FQARFNREAQ
SAAGLNHPNI VGVYDTGTER DEHGIMVPYI VMELVQGRTL REILRSGQRI PDATAFQYTT
GVLDALAYSH KAGIVHRDIK PANVMLTTAG QIKVMDFGIA RAVSDTSATM TQTAAIIGTA
QYLSPEQARG ETVDARSDLY STGCLLYELL TGKPPFQGDS PVSVAYQHVR EAVTPPSQLN
PNVTPQMDAV VLKALAKDPE QRYQSAEEMR ADCARLLSGE QVTAVIPPAV VTPAGDDMAT
QVFTPNDTVS ETAIQTGPAR ALDPTTQDAI EEYEEPKKKR SWLTFVLVGL LLVLLGIVGF
FFLQMNGSDD KKDVVSVPSV LTSMEEAAKN TLTEANLVPK VKYSDGDAET KGQVIAQDPV
GGTEVRIGST VTITVNSGPK TLAVPDGLIG MSETEARAAL AEAGFTNVIK QDAPANKEGP
DTAEDTVVDV QPASGKKIQS DTQITIYVAT GKSTLPRVIG MTADEAKAEL AKSGFTNVEV
WETETSVEAD NGKVTLQNPT GNTTQLRSTS ITLTVARYKA PAPAATTTAP GGERTNAADP
GRNPEGEN
//
