ID A0A2R4T4W3_9ACTN Unreviewed; 658 AA.
AC A0A2R4T4W3;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=SLUN_20140 {ECO:0000313|EMBL:AVZ74131.1};
OS Streptomyces lunaelactis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1535768 {ECO:0000313|EMBL:AVZ74131.1, ECO:0000313|Proteomes:UP000244201};
RN [1] {ECO:0000313|EMBL:AVZ74131.1, ECO:0000313|Proteomes:UP000244201}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MM109 {ECO:0000313|EMBL:AVZ74131.1,
RC ECO:0000313|Proteomes:UP000244201};
RA Naome A., Martinet L., Maciejewska M., Anderssen S., Adam D., Tenconi E.,
RA Deflandre B., Arguelles-Arias A., Calusinska M., Copieters W., Karim L.,
RA Hanikenne M., Baurain D., van Wezel G., Smargiasso N., de Pauw E.,
RA Delfosse P., Rigali S.;
RT "Complete genome sequence of Streptomyces lunaelactis MM109T, a Ferroverdin
RT A producer isolated from cave moonmilk deposits.";
RL Submitted (JAN-2018) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP026304; AVZ74131.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2R4T4W3; -.
DR KEGG; slk:SLUN_20140; -.
DR OrthoDB; 9762169at2; -.
DR Proteomes; UP000244201; 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; 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; 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; 4.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00740; PASTA; 4.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51178; PASTA; 4.
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:AVZ74131.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000244201};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:AVZ74131.1};
KW Transferase {ECO:0000313|EMBL:AVZ74131.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 347..365
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 11..277
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 374..439
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 440..505
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 507..570
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 573..640
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 298..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 406..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 606..658
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..642
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 658 AA; 68943 MW; 18ABBFCCFF2C7574 CRC64;
MEEPRRLGGR YELGSVLGRG GMAEVYLAHD TRLGRTVAVK TLRADLARDP SFQARFRREA
QSAASLNHPA IVAVYDTGED YVDGVSIPYI VMEYVDGSTL RELLHSGRRL LPERTLEMTI
GILQALEYSH RAGIVHRDIK PANVMLTRTG QVKVMDFGIA RAMGDSGMTM TQTAAVIGTA
QYLSPEQAKG EQVDARSDLY STGCLLYELL TVRPPFVGDS PVAVAYQHVR EEPQPPSNFD
PEITPEMDAI VLKALVKDPD YRYQSADEMR ADIEACLDGQ PVAATAAMGS VGYGGYGSDD
QPTTALRQAD PAGQTSMLPP VNPDGGGYGG YDDRPDRRRQ KKSNTSTILL VLAGILVLVG
AVLIGKSVFG GGGGNGDVPV PLLVGKTFDE AKVLATNAGV EVAQSGTDRC DQPKGSICTQ
TPDGGKMKEG DTVQVVVSEG APKIEVPDVT DKPVDKATQI LEGKVFKVKT KEIESDEDPG
TVLTQSPVGG AQAEKNSTVT LTVAKQTKVP VPPVVGAQFD AAKAQLEGLE FTVARVDVDS
TEPAGQVIKQ DPAGNSKAAK GATITLTVSK GPQTPQVPVP QIRGMTVAQA KQQLAQSGFT
TVGFAPGSSQ DDNALVTNTD PQPGTQVDPA TTTVTLTTVG GGGNGGGNGG GFIGGGDG
//
