ID A0A1Q9LU31_9PSEU Unreviewed; 665 AA.
AC A0A1Q9LU31;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, 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=BJP25_00105 {ECO:0000313|EMBL:OLR95538.1};
OS Actinokineospora bangkokensis.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Actinokineospora.
OX NCBI_TaxID=1193682 {ECO:0000313|EMBL:OLR95538.1, ECO:0000313|Proteomes:UP000186040};
RN [1] {ECO:0000313|EMBL:OLR95538.1, ECO:0000313|Proteomes:UP000186040}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=44EHW {ECO:0000313|EMBL:OLR95538.1,
RC ECO:0000313|Proteomes:UP000186040};
RA Greule A., Intra B., Flemming S., Rommel M.G., Panbangred W., Bechthold A.;
RT "The Draft Genome Sequence of Actinokineospora bangkokensis 44EHWT reveals
RT the biosynthetic pathway of antifungal compounds Thailandins with unusual
RT extender unit butylmalonyl-CoA.";
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};
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:OLR95538.1}.
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DR EMBL; MKQR01000001; OLR95538.1; -; Genomic_DNA.
DR RefSeq; WP_075972668.1; NZ_MKQR01000001.1.
DR AlphaFoldDB; A0A1Q9LU31; -.
DR STRING; 1193682.BJP25_00105; -.
DR OrthoDB; 9762169at2; -.
DR Proteomes; UP000186040; 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-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:OLR95538.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000186040};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:OLR95538.1};
KW Transferase {ECO:0000313|EMBL:OLR95538.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 339..359
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 11..274
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 369..444
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 445..514
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 515..579
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 582..650
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 542..574
FT /note="Disordered"
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 665 AA; 71086 MW; 88A5F3305556D742 CRC64;
MTTPRLLSNR YEIGDAIGYG GMSEVHLGRD VRLGREVAVK VLRADLARDP QFQERFRREA
QNAAALNHPA IVAVYDTGET RIDSGPLPYI VMEYVDGRTL RDIVKTEGPL PGQRAMEIMA
DVCAALDFSH RHGIVHRDVK PANVMITKTG AVKVMDFGIA RAVADGQVAV TQTAAVIGTA
QYLSPEQARG ESVDARSDVY ATGCVLFELL TGEPPFTGDS PVAVAYQHVR EDPRPPSQLN
PRVSPQLDAI VLKAMSKGAA NRYQSAAEMR TDIVRVLSGQ RPAAPMVMTD DDRTAVLGAG
RPQPEMRGRH RPESLDTEYD YDDYADEEEE RRRRQRKTWL IVLCSLIVVG LIGIVWYLLS
DSSADQADGS FTVPEVVGKS QAEAQSQLSN LGLQPVVENV PCQQTETGAP GPCGPDSIGK
VIGTDPSTGA AVRKGDRITL RVGVSPEKVA VPDVSGKTLQ EATDLLKQAK LSVAAQTEEE
VTTDDDLVGK VTSSNPAVGT SVSAGTEVKL VIGKAQEQVD VPNLVGQDYD TAAANLQRAG
LTAKRQDVSS NQPAGTVTDQ APKSGKLKPG STVTLSVSKG DQVEISMPNL EGKSRAEAEA
ALRQLGWTGS LNAVDYPTTD RDEVGKVLEQ DQQPGEKIAK DDTVNVTIGK SLIGGGGPDP
TTTNR
//
