ID A0A150FBG4_9BACI Unreviewed; 646 AA.
AC A0A150FBG4;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=AXI58_09010 {ECO:0000313|EMBL:KXZ22123.1};
OS Bacillus nakamurai.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1793963 {ECO:0000313|EMBL:KXZ22123.1, ECO:0000313|Proteomes:UP000075430};
RN [1] {ECO:0000313|EMBL:KXZ22123.1, ECO:0000313|Proteomes:UP000075430}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL B-41092 {ECO:0000313|EMBL:KXZ22123.1,
RC ECO:0000313|Proteomes:UP000075430};
RA Wen L., He K., Yang H.;
RL Submitted (FEB-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:KXZ22123.1}.
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DR EMBL; LSBA01000005; KXZ22123.1; -; Genomic_DNA.
DR RefSeq; WP_061520477.1; NZ_LSBA01000005.1.
DR AlphaFoldDB; A0A150FBG4; -.
DR STRING; 1793963.AXI58_09010; -.
DR OrthoDB; 9788659at2; -.
DR Proteomes; UP000075430; 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:KXZ22123.1};
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:KXZ22123.1};
KW Transferase {ECO:0000313|EMBL:KXZ22123.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 328..352
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 11..271
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 353..421
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 422..489
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 490..556
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 294..318
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 646 AA; 71554 MW; 8D6A53FFBBB3C306 CRC64;
MLTGKRISGR YHILRPIGGG GMANVYLAED IILEREVAIK VLRFDFVNDN DFIRRFRREA
QSASSLDHPN IVSIYDIGEE GDIYYIVMEY VEGMTLKEYI TTHGPLHPKE ALSIMEQIVS
AIAHAHHNHI VHRDIKPHNI LIDHMGHIKV TDFGIATALS STTITHTNSV LGSVHYLSPE
QARGGLATKK SDIYALGIVL FELLTGKIPF DGESAVSIAL KHLQTETPSA KKWNPSIPQS
VENIILKATA KDPFHRYESA EDMEEDIRTA FDADRLNEER FSVQDDEEMT KAIPIITDGS
EVTPPEPQKQ AEDDDEKSVK KKKRKWPWVL LAVCFVLITA SVLAVTVFPS LFMPKDVSVP
DVKGLEYEKA EALLEKNGLQ ADPDVTDIED EKVQEGLMVK TDPKAGSTVK EGSAVKMYKS
IGKAKTQLID VKGRSIDKAK EALKEKGFKH VNVKEVNDAS DAGTVIDQDP SAGTEMVAGD
DEVNLTVSIG PADITLRDLK TYSKEAASGY LEDNGLNLVE KEAHSDDVPK GQVIKQEPSA
GTAVKPGSDV EVTFSLGPEE KPAKTVKENI SIPYEPDHEG DELEVQIAID DKDHSISDTY
ETFKIKEPTE KTIELKIEQG QKGYYQVMVN HKVVSYKTIE YPKDKG
//
