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Database: UniProt
Entry: A0A099JXG3_9MICO
LinkDB: A0A099JXG3_9MICO
Original site: A0A099JXG3_9MICO 
ID   A0A099JXG3_9MICO        Unreviewed;       650 AA.
AC   A0A099JXG3;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   27-MAR-2024, entry version 34.
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=BJ997_001415 {ECO:0000313|EMBL:MBB5640867.1}, GY21_00485
GN   {ECO:0000313|EMBL:KGJ82856.1};
OS   Cryobacterium roopkundense.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Cryobacterium.
OX   NCBI_TaxID=1001240 {ECO:0000313|EMBL:KGJ82856.1, ECO:0000313|Proteomes:UP000029864};
RN   [1] {ECO:0000313|EMBL:KGJ82856.1, ECO:0000313|Proteomes:UP000029864}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RuG17 {ECO:0000313|EMBL:KGJ82856.1,
RC   ECO:0000313|Proteomes:UP000029864};
RA   Sisinthy S.;
RL   Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:MBB5640867.1, ECO:0000313|Proteomes:UP000561726}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21065 {ECO:0000313|EMBL:MBB5640867.1,
RC   ECO:0000313|Proteomes:UP000561726};
RA   Klenk H.-P.;
RT   "Sequencing the genomes of 1000 actinobacteria strains.";
RL   Submitted (AUG-2020) 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:KGJ82856.1}.
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DR   EMBL; JPXF01000001; KGJ82856.1; -; Genomic_DNA.
DR   EMBL; JACHBQ010000001; MBB5640867.1; -; Genomic_DNA.
DR   RefSeq; WP_035834453.1; NZ_JPXF01000001.1.
DR   AlphaFoldDB; A0A099JXG3; -.
DR   STRING; 1001240.GY21_00485; -.
DR   eggNOG; COG0515; Bacteria.
DR   eggNOG; COG2815; Bacteria.
DR   OrthoDB; 9762169at2; -.
DR   Proteomes; UP000029864; Unassembled WGS sequence.
DR   Proteomes; UP000561726; 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; 4.
DR   CDD; cd14014; STKc_PknB_like; 1.
DR   Gene3D; 3.30.10.20; -; 4.
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; PTHR45832:SF24; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR45832; SERINE/THREONINE-PROTEIN KINASE SAMKA-RELATED-RELATED; 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:KGJ82856.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029864};
KW   Serine/threonine-protein kinase {ECO:0000313|EMBL:KGJ82856.1};
KW   Transferase {ECO:0000313|EMBL:MBB5640867.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        355..376
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          18..274
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          380..445
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   DOMAIN          521..583
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   DOMAIN          584..650
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   REGION          314..344
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   650 AA;  68111 MW;  F0508E75B953C650 CRC64;
     MSETPTDQMI GRLIDGRYQV RSRIARGGMA TVYLATDLRL ERRVAIKIMH GHLADDNAFK
     SRFIQEARSA ARLAHPNVVN VFDQGQDADA AYLVMEYLPG ITLRDLLKDY GKLTPEQTVD
     ILEAVLSGLA AAHKAGIVHR DVKPENVLLA DDGRIKISDF GLARAVNNNT ATGQALLGTI
     AYLSPELVTR GIADARSDIY ALGIMTFEML TGEQPYVGEA PMQIAYQHAN DTVPRPSSKV
     PSTPQDLDEL VQWATARDPE QRPRDARVML DQLLAGRGHS DPSAQPTALQ PTALQPTMML
     PNLSAATANA ETQILGGTPP TNVLGPLTAT GVGPRQPDNS ARLTTKARRR KGRGFWLFAL
     VILIASALGG TGWYFGSGPG SDIAIPAVAT LSPGDAVAQL TAVGLASDQT TAYSADVPEG
     VVVSTDPGAG KRVAKDSVVT IIVSLGLQPI TLPPLTGLSQ EAATAEITEL QAEVGGVDPV
     FDDSVASGTV ISATRASDDG DVSQGGDYFQ GLPVDLVVSL GPIPSVSGET VADATQTLEA
     AGLIAAPGEQ TYSDTVPEGR VVSSTAPDGP VRSGATITLT ISRGPEPVQI PDVVGKPWSE
     AKQILEDASL RLDYNIFADA APGLFTVTKV TPGAGESVPR GSSVKINFSA
//
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