ID A0A1G8MHZ0_9BACI Unreviewed; 650 AA.
AC A0A1G8MHZ0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=SAMN04488123_104173 {ECO:0000313|EMBL:SDI67524.1};
OS Natribacillus halophilus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Natribacillus.
OX NCBI_TaxID=549003 {ECO:0000313|EMBL:SDI67524.1, ECO:0000313|Proteomes:UP000198853};
RN [1] {ECO:0000313|EMBL:SDI67524.1, ECO:0000313|Proteomes:UP000198853}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21771 {ECO:0000313|EMBL:SDI67524.1,
RC ECO:0000313|Proteomes:UP000198853};
RA de Groot N.N.;
RL Submitted (OCT-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};
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DR EMBL; FNEN01000004; SDI67524.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G8MHZ0; -.
DR OrthoDB; 9788659at2; -.
DR Proteomes; UP000198853; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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; 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 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; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:SDI67524.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000198853};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:SDI67524.1};
KW Transferase {ECO:0000313|EMBL:SDI67524.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 335..357
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 9..269
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 358..424
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 425..491
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 492..557
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 266..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..289
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 650 AA; 71492 MW; 267AEC73F6D5A0EB CRC64;
MIGERIDGRY EVKAYIGGGM AHVYRARDII LERDVAVKVL QPQHAEDDEF VRRFQREARA
ATSLVHANVV DIYDLGEKDG LFYIVMEYVG GNTLKEKIVN EGALSFPETM RIFSELAVAI
AYAHDQGIIH RDLKPQNILL DEDGSVKVTD FGIARASSAA TITHTNSVLG SVHYLSPEQA
RAGTLTAKTD IYALGVILFE MVTGLLPFNA DSAVSIALKH LQEPFPNPGD LRADLPGSIN
NMIRKATAKD PLRRYENVEE MRQDAETALL PERFHEPPIT VDDSDEESTR PIPAVGPHQD
VEDTKVANGE GDEGASEEEP GDDGKEKKKR RFWKIAGLAL LLLLAIIAAF TVVPALLSPD
EADVPELVGS QEEEATTQLE SLGLEADTEY EFHDVAEEGV VFNQDPDAGR TVLEGQAVTL
FVSEGQETVE MPDVEGLQIE QAVEELEDFE DVDVTSEPAE NVAADLVMEQ NPSADQEVVP
NETTVQLVYS ETPEITLEDL TGTTQEGVDN YLESNNLNGS FQTNHSDSVP EGSVISHDPG
PYDTVEEGDE INFIVSDGPP PEEEEEEPVQ TVEAVIPVEV SEMNDDQDVF EIEIEYEDST
TDGTEVYEEE EITSSTTYRV PLEVTPDTDG SYTLYVNGDE VQSNSFSYED
//
