ID A0A0M1P3A9_9BACL Unreviewed; 715 AA.
AC A0A0M1P3A9;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:KOR88544.1};
GN ORFNames=AM231_04850 {ECO:0000313|EMBL:KOR88544.1};
OS Paenibacillus solani.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1705565 {ECO:0000313|EMBL:KOR88544.1, ECO:0000313|Proteomes:UP000036932};
RN [1] {ECO:0000313|Proteomes:UP000036932}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FJAT-22460 {ECO:0000313|Proteomes:UP000036932};
RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA Shi H., Pan Z., Liu X.;
RT "Genome sequencing project for genomic taxonomy and phylogenomics of
RT Bacillus-like bacteria.";
RL Submitted (AUG-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 -!- SIMILARITY: Belongs to the protein kinase superfamily. NEK Ser/Thr
CC protein kinase family. NIMA subfamily. {ECO:0000256|ARBA:ARBA00010886}.
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:KOR88544.1}.
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DR EMBL; LIUT01000001; KOR88544.1; -; Genomic_DNA.
DR RefSeq; WP_054401528.1; NZ_LIUT01000001.1.
DR AlphaFoldDB; A0A0M1P3A9; -.
DR PATRIC; fig|1705565.3.peg.2857; -.
DR OrthoDB; 9788659at2; -.
DR Proteomes; UP000036932; 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; PTHR43671:SF13; LD04361P; 1.
DR PANTHER; PTHR43671; SERINE/THREONINE-PROTEIN KINASE NEK; 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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:KOR88544.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000036932};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:KOR88544.1};
KW Transferase {ECO:0000313|EMBL:KOR88544.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 334..353
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 358..426
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 427..497
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 498..566
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 408..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 652..715
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 715 AA; 79546 MW; 343E5660CDFA4886 CRC64;
MIGHELAGRY KIIERIGGGG MALVYKAQDI LLNRNVAIKV LRQQFVHDEE FIRRFRREAQ
SAASLSHSNV VSIYDVGQEE DVHYIVMEYI EGQNLNEIIK ERAPLQVEEA VRIAIQICDA
LGHAHHNQII HRDIKPHNIL IGRNGRVKVT DFGIARAVTS TTITQTGSVV GSVHYFSPEH
AKGVVTGEKS DLYSLGIVLY QMLTARLPFL GESPISVALK HLQEEFDEPR EVNPLIPQSV
ENIILKSMRK NPEERYQSAE EMMDDLETCL LPMRLNEPKM EFEDDADSTL VMPALKTMQR
SSQHHIDQED DSEEEELVEK HTGKPKKKWV KPTIIIVSVL LFLGIMVGVV MYVNKMLEVP
EVKVPQVVGM TEEQAIRELE DSGLTVDEEV IRKYKPEVEP GIVYAQSKDP DSMLKKGSPV
QLSVGDEKPL EKMPDLNGKT FKEAVAILTD LGVNEKAIKQ STVNNDDVPV GQIFDQSPSA
ESPIDPNQVE VRVTISKGKE TINMPSLIGM DKDKAVALIE SVGLKVGPIK EKSSFEVKKG
EVMEQWPHDP NQAVEPNAVI TLFVSSGYPA DALEYNYSVP VSPSVEGQES KIRVVFSDAL
GDNQEAVNKT ITNSEMVPVK LTLAPEKHAT VMIFRDGRQV DTYSVSYTDV KNGTVPQPTF
EQPPVEPDVP VDINPDEGNG EEDFNEEDDA AYNWNHGNNG NNGNGKGHGK DKDND
//
