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Database: UniProt
Entry: A0A1U7PHG6_9BACI
LinkDB: A0A1U7PHG6_9BACI
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ID   A0A1U7PHG6_9BACI        Unreviewed;       653 AA.
AC   A0A1U7PHG6;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-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=SAMN05428946_0242 {ECO:0000313|EMBL:SIT67595.1};
OS   Edaphobacillus lindanitolerans.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Edaphobacillus.
OX   NCBI_TaxID=550447 {ECO:0000313|EMBL:SIT67595.1, ECO:0000313|Proteomes:UP000187550};
RN   [1] {ECO:0000313|EMBL:SIT67595.1, ECO:0000313|Proteomes:UP000187550}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MNA4 {ECO:0000313|EMBL:SIT67595.1,
RC   ECO:0000313|Proteomes:UP000187550};
RA   Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL   Submitted (JAN-2017) 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; FTPL01000001; SIT67595.1; -; Genomic_DNA.
DR   RefSeq; WP_076756550.1; NZ_FTPL01000001.1.
DR   AlphaFoldDB; A0A1U7PHG6; -.
DR   STRING; 550447.SAMN05428946_0242; -.
DR   OrthoDB; 9788659at2; -.
DR   Proteomes; UP000187550; 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; 2.60.40.2560; -; 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:SF37; SERINE_THREONINE-PROTEIN KINASE A; 1.
DR   Pfam; PF03793; PASTA; 3.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF21160; PrkC-like_PASTA-like; 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:SIT67595.1};
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:SIT67595.1};
KW   Transferase {ECO:0000313|EMBL:SIT67595.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        341..363
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          10..270
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          364..431
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   DOMAIN          432..499
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   DOMAIN          500..567
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   REGION          271..336
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          395..421
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          463..484
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         39
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   653 AA;  71792 MW;  2B9A3E67733A65A1 CRC64;
     MIGKRISGRY EVLGLLGGGG MSTVYLARDM ILDRPVAIKI LRYDLADEEE LRKRFHREAL
     SATSLIHPHI VNIYDVGEDG ELHYLVMEYV EGQTLKEYIQ EKAPLPAARA VDIMMQLCDG
     ISAAHLHGII HRDIKPQNIL MDGDGRVKLT DFGIAMALSA TALTRTNSVM GTVHYLSPEQ
     ARGGIATKRS DLYSLGIVLY EMLTGKLPFS GESPVSIALK HLHEETPPVR DERPDIPQSL
     ENVILKATAK NPAYRYPSAE VMLKDLSTVL SPERRDEPKF MPPPPDDEAT KAMPAIKDMP
     GRPAGDTRVP EPAPMTETPP EPVTAKEQEQ KQKRKRKKWP WLLAGTVILA ALVGVLLYLL
     GVFGPKQAEV PDVTGKPAEE AMSLIRDAGL EIGGQTEEHS PDVEKGSVIR TSPGAGSLND
     EGTEVDLVIS AGEEPVELTD FTGRDYDSIS EIVDEFGFKN VRKEEEYSDE PEGTVIRQEP
     EGGEKIVPSE TELVLTVSKG IEKISTKDLS GFDEDELNEY ARTSGFNIRI TAEKPSDSVE
     AGRVLSQEPE AGTELERGAT IKVVLSKGAE ADPVKTFIQG VTIPYEPSEE GAAQKVTIYI
     GDLSHKIEEP AEEFEITEDT TKRIRMEIKE GGSATYRIER DGKTVAEETI PYE
//
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