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
//