ID A0A1H2CSX6_9ACTN Unreviewed; 595 AA.
AC A0A1H2CSX6;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=SAMN04489716_6677 {ECO:0000313|EMBL:SDT73464.1};
OS Actinoplanes derwentensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Actinoplanes.
OX NCBI_TaxID=113562 {ECO:0000313|EMBL:SDT73464.1, ECO:0000313|Proteomes:UP000198688};
RN [1] {ECO:0000313|EMBL:SDT73464.1, ECO:0000313|Proteomes:UP000198688}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43941 {ECO:0000313|EMBL:SDT73464.1,
RC ECO:0000313|Proteomes:UP000198688};
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; LT629758; SDT73464.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H2CSX6; -.
DR STRING; 113562.SAMN04489716_6677; -.
DR OrthoDB; 308915at2; -.
DR Proteomes; UP000198688; Chromosome i.
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; SSF54184; Penicillin-binding protein 2x (pbp-2x), c-terminal domain; 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:SDT73464.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000198688};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:SDT73464.1};
KW Transferase {ECO:0000313|EMBL:SDT73464.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 335..357
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 12..285
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 370..437
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 503..568
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 565..595
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..585
FT /note="Polar residues"
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 595 AA; 63609 MW; 51AB548765BB1917 CRC64;
MTAQARLLGG RYQVGELLGY GGMAEVHKGR DLRLGRDVAI KMLRTDLARD ATFQERFRRE
AQNSAALNHP AIVAVYDTGE EISAAGEKHP FIVMEFVNGQ TLKELLAQEQ RLQPRRALEI
IADICAALEF SHRHGIIHRD IKPGNVMITQ SGQVKVMDFG IARALASGAT TMTQTSAVIG
TAQYLSPEQA RGESVDARSD VYAAGCVLFE LVVGHPPFVG DSPVSVAYQH VREEPKPPSS
IVRDLPPEID AMALKALSKN PLNRYQSAQE MRADALRAVS GRPVMATPVM SQAETMALNG
GPQQWQPQGA TTMQRPVQGG YPGGVQQKPE SRSSWVMAVV AGLAVLVVVV LGVALAMNRK
ADSGTNTANE PVPVAMPKLE GLSNKDAVAE LTRLKFTNFN ATDPETGEDC NNTVSKQNPD
QGATVQLTDP VTYTICTKPE EVPVPSDLRG GSFNAVKATL EGLGLKVDPR EVDSIQPKNQ
VIEVESAGEK VPPGTTITVR YSNNNLVEVP DLKGRSQSAA EAVLNERGLI ANVVLVQADG
EPGTVLDQSP VKDKKVKKGS TVTIQVIEEQ QPNPDPSTSE STGTGDGEGG GEENP
//
