ID A0A2P4UGB7_9ACTN Unreviewed; 637 AA.
AC A0A2P4UGB7;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-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 Name=spk1 {ECO:0000313|EMBL:POM24114.1};
GN ORFNames=BTM25_27410 {ECO:0000313|EMBL:POM24114.1};
OS Actinomadura rubteroloni.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Thermomonosporaceae; Actinomadura.
OX NCBI_TaxID=1926885 {ECO:0000313|EMBL:POM24114.1, ECO:0000313|Proteomes:UP000242367};
RN [1] {ECO:0000313|EMBL:POM24114.1, ECO:0000313|Proteomes:UP000242367}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5-2 {ECO:0000313|EMBL:POM24114.1,
RC ECO:0000313|Proteomes:UP000242367};
RX PubMed=28463423; DOI=10.1002/chem.201701005;
RA Guo H., Benndorf R., Leichnitz D., Klassen J.L., Vollmers J., Gorls H.,
RA Steinacker M., Weigel C., Dahse H.M., Kaster A.K., de Beer Z.W.,
RA Poulsen M., Beemelmanns C.;
RT "Isolation, Biosynthesis and Chemical Modifications of Rubterolones A-F:
RT Rare Tropolone Alkaloids from Actinomadura sp. 5-2.";
RL Chemistry 23:9338-9345(2017).
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:POM24114.1}.
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DR EMBL; MTBP01000002; POM24114.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P4UGB7; -.
DR Proteomes; UP000242367; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd06577; PASTA_pknB; 4.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 3.30.10.20; -; 4.
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; 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; 4.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00740; PASTA; 4.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF54184; Penicillin-binding protein 2x (pbp-2x), c-terminal domain; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51178; PASTA; 4.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:POM24114.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000242367};
KW Transferase {ECO:0000313|EMBL:POM24114.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 339..360
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 18..281
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 367..429
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 430..494
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 495..561
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 578..637
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 298..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 519..553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 637 AA; 66808 MW; 8ABAF633E186F5CC CRC64;
MDTSTADPLV GTVLDGRYRI ESRIARGGMA TVYVARDLRL DRTVAIKVMH AHLAADEEFV
RRFIGEAKAA AALSHPNVVA VYDQRTDGEH VFLVMELVHG RTLRDLLTER TRLGPRAALE
IMQPVLAALG AAHRAGLVHR DVKPENVLIA ADGQVKVADF GLARAETAGR MTRTGLIIGT
VGYLAPEQVL TGHADVRSDV YAAGVLLFEL LTGRLPYEGD TPLAVAYQHA NGTVPAPSEL
VPGLPAPVDA LVARATARDA ADRPQDANAF LATVAEVHGG LAPDFDARLA ASEPGATAVL
QTPAPPPGDG RTAVLDPADG APAGPPPRGG AFGGSGRRWA IVAVAAVAAI VLGWAVWYQF
SGQYDHVPEE IIGMKPAAAT KELRGHGLAV RQGDTVYSDR VDRGEVAATD PAPGARVSQG
MTITLHVSKG HVPREVPDVK GRTESDARDL LESKGFRVGG VSSLPSETIA KGRAIRTRPT
AGTKVSTDQP VALVMSSGMT VPDLTGWSTG DAKNALTAMG LDVKTQDRKQ DGKPGGTVVG
QDPAPGSGVS RGDRVTLYVT PRDCLIGNWF CNDGKGDEGN KVPVPSVIGK SFDDARRAIE
SSGFRMRIGT RVGDRVIGQT PIPDSRAARG GVITVYG
//
