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Database: UniProt
Entry: A0A0M3D726_9MICO
LinkDB: A0A0M3D726_9MICO
Original site: A0A0M3D726_9MICO 
ID   A0A0M3D726_9MICO        Unreviewed;       562 AA.
AC   A0A0M3D726;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 25.
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=AAY78_09075 {ECO:0000313|EMBL:KKX97900.1};
OS   Microbacterium sp. Ag1.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=1643443 {ECO:0000313|EMBL:KKX97900.1, ECO:0000313|Proteomes:UP000034223};
RN   [1] {ECO:0000313|EMBL:KKX97900.1, ECO:0000313|Proteomes:UP000034223}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ag1 {ECO:0000313|EMBL:KKX97900.1,
RC   ECO:0000313|Proteomes:UP000034223};
RA   Syromyatnikov M.Y., Popov V.N.;
RL   Submitted (APR-2015) 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:KKX97900.1}.
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DR   EMBL; LBCR01000029; KKX97900.1; -; Genomic_DNA.
DR   RefSeq; WP_046747988.1; NZ_LBCR01000029.1.
DR   AlphaFoldDB; A0A0M3D726; -.
DR   OrthoDB; 9762169at2; -.
DR   Proteomes; UP000034223; 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; 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}; Kinase {ECO:0000313|EMBL:KKX97900.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141};
KW   Serine/threonine-protein kinase {ECO:0000313|EMBL:KKX97900.1};
KW   Transferase {ECO:0000313|EMBL:KKX97900.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        331..352
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          12..280
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          362..428
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   DOMAIN          429..496
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   DOMAIN          497..561
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   BINDING         41
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   562 AA;  59586 MW;  84B6058073E9AF89 CRC64;
     MSTEPRIVAG RYRVDELIGH GGMAKVYRGY DLTLGRDVAI KILDADLARD TTFRNRFRLE
     AQAASRMSHP SIVRVFDAGD PSTSDIGSDE PPYIVMELVK GTLLKDIIAA GPVPAADAVR
     YVDGILEALD YSHRAGVVHR DIKPGNVMVT DKGQVKVMDF GIARAVSDSS STVAETTQII
     GTAAYFSPEQ AKGEPVDARA DLYSTGVVLY ELLTGRQPFR GESPVAVAYQ HVSETPVPPT
     EVNEDAPRTL DPIVLRALAK DPYQRYPDAA HFRAALDSAM TGNAPTRKEL GALTSELYGA
     SPRQAQETAR SLRQLSADTT MTRTQSGPPV AWIWAGVALL AVLLASVLFW VVTISMRPPE
     VSSTSRTIPN LVNVSSERAQ DDLANLDLSS KIVIETSSEV SEGNVIRTDP EAGVSVEEGS
     TVTLYVSKGE ETVVMPKIEG MALDDATNAL KAAGLELGTV IQRNDKALAA NTVISASEKA
     DAELDPGTVV NLVVASGTVT LTDLAGWTVD AATANLTDLG LVAVPTETAE CPATEPPTVH
     SMSVAPGDVP VGSSVQIFFC TG
//
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