ID B2GHD8_KOCRD Unreviewed; 646 AA.
AC B2GHD8;
DT 10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT 10-JUN-2008, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN OrderedLocusNames=KRH_20670 {ECO:0000313|EMBL:BAG30414.1};
OS Kocuria rhizophila (strain ATCC 9341 / DSM 348 / NBRC 103217 / DC2201).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Kocuria.
OX NCBI_TaxID=378753 {ECO:0000313|EMBL:BAG30414.1, ECO:0000313|Proteomes:UP000008838};
RN [1] {ECO:0000313|EMBL:BAG30414.1, ECO:0000313|Proteomes:UP000008838}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9341 / DSM 348 / NBRC 103217 / DC2201
RC {ECO:0000313|Proteomes:UP000008838};
RX PubMed=18408034; DOI=10.1128/JB.01853-07;
RA Takarada H., Sekine M., Kosugi H., Matsuo Y., Fujisawa T., Omata S.,
RA Kishi E., Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT "Complete genome sequence of the soil actinomycete Kocuria rhizophila.";
RL J. Bacteriol. 190:4139-4146(2008).
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DR EMBL; AP009152; BAG30414.1; -; Genomic_DNA.
DR RefSeq; WP_012399135.1; NC_010617.1.
DR AlphaFoldDB; B2GHD8; -.
DR STRING; 378753.KRH_20670; -.
DR KEGG; krh:KRH_20670; -.
DR eggNOG; COG0515; Bacteria.
DR eggNOG; COG2815; Bacteria.
DR HOGENOM; CLU_000288_135_2_11; -.
DR OrthoDB; 9762169at2; -.
DR Proteomes; UP000008838; Chromosome.
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; 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 NCBIfam; NF033483; PknB_PASTA_kin; 1.
DR PANTHER; PTHR43289; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED; 1.
DR PANTHER; PTHR43289:SF32; SERINE_THREONINE-PROTEIN KINASE PKAB; 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.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Kinase {ECO:0000313|EMBL:BAG30414.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Reference proteome {ECO:0000313|Proteomes:UP000008838};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:BAG30414.1};
KW Transferase {ECO:0000313|EMBL:BAG30414.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 366..390
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 14..279
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 397..463
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 464..530
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 531..599
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 307..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 569..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..605
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 43
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 646 AA; 67619 MW; C1767944D1206553 CRC64;
MGSPQLPELV NERYEVGEVI GRGGMATVHV GQDVRLGRRV AIKILRPELA ADESFHERFQ
REAHAVASLN HHSIVAIYDT GEIRPQGPDG VLRPYIVMEY VPGQTLRELI HGPGVTPHEA
VEYMLGILDA LSFSHRAGIV HRDIKPANVK VTPDGGVKVM DFGIARAVED TQAALTQSQA
VLGTAQYLSP EQARGAAVDP RSDLYSAACV LFEMLTGRAP FVGESSVAIA AQHVRDAPPA
PSALNPQLPP AVDRFMERAL AKNPQDRFAD AGQMRRALRE LEAQLSSDLG ATQPIGTATA
VDSHTKTLPA VGTGAPAAAV TAAGRSEDTE TTETSPVQPG PFEPDDDDAA APEPATAAPS
RGRRGWVIAL ALVLLLSLLG VGTVLGVQWW QGSQVEQVAR VSIPQVVGMD STTAENTLRD
AGLNPTFTKE HSDSVPDKHV IRMDPAAGTE VDRNATVSVV VSEGPATVTV PEDIVGQSLE
YARESIQHAG LTVGPVSTVN SATVPANAVI SADPAPGSSV ARASAVKLQV STGKVTVPDV
VGRSRADAER ALRADDVRLN AAVEIRETED AETGTVLEQS APAGSSVSQG STITITVARK
TAPSPTPTPS RTPEETTEPS APAETATATP EPRPTAGASK TRGDHG
//
