ID   Q8FNS3_COREF            Unreviewed;       741 AA.
AC   Q8FNS3; C8NQ30;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   27-MAR-2024, entry version 120.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
OS   Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189
OS   / NBRC 100395).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=196164 {ECO:0000313|EMBL:BAC18880.1, ECO:0000313|Proteomes:UP000001409};
RN   [1] {ECO:0000313|EMBL:BAC18880.1, ECO:0000313|Proteomes:UP000001409}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395
RC   {ECO:0000313|Proteomes:UP000001409};
RX   PubMed=12840036; DOI=10.1101/gr.1285603;
RA   Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S.,
RA   Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.;
RT   "Comparative complete genome sequence analysis of the amino acid
RT   replacements responsible for the thermostability of Corynebacterium
RT   efficiens.";
RL   Genome Res. 13:1572-1579(2003).
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; BA000035; BAC18880.1; -; Genomic_DNA.
DR   RefSeq; WP_006768071.1; NZ_GG700683.1.
DR   AlphaFoldDB; Q8FNS3; -.
DR   STRING; 196164.gene:10742498; -.
DR   KEGG; cef:CE2070; -.
DR   eggNOG; COG0515; Bacteria.
DR   eggNOG; COG2815; Bacteria.
DR   HOGENOM; CLU_000288_135_2_11; -.
DR   OrthoDB; 9762169at2; -.
DR   Proteomes; UP000001409; Chromosome.
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; 5.
DR   CDD; cd14014; STKc_PknB_like; 1.
DR   Gene3D; 3.30.10.20; -; 5.
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; 5.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00740; PASTA; 5.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF54184; Penicillin-binding protein 2x (pbp-2x), c-terminal domain; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51178; PASTA; 4.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:BAC18880.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001409};
KW   Serine/threonine-protein kinase {ECO:0000313|EMBL:BAC18880.1};
KW   Transferase {ECO:0000313|EMBL:BAC18880.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        391..412
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          14..272
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          414..480
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   DOMAIN          481..547
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   DOMAIN          548..615
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   DOMAIN          682..741
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   REGION          323..381
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          722..741
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        341..363
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   741 AA;  78804 MW;  655FB3058197C2B9 CRC64;
     MVNLRVGDVL EDRYRIETPI ARGGMSTVYR CIDLRLGRSV AVKVMDAAYV NDPVFRQRFR
     REARSMAQLS HPNLVNVFDF SSSGDHAFIV MELITGGTLR ELLAERGPMP PHAAIGVMRG
     VLTGLTAAHR AGMVHRDIKP DNVLITRDHR VKLSDFGLVR AASAGQSRDD KIVGTVAYLS
     PEQVEGTEIG PASDVYSAGI VLFELLTGTT PFDGADDMDH AYARLTEVVP APSSLIDGIP
     SLVDALVATA TALNPEDRFS DASEFLTAME DVARELNLPG FKVPAPVSSA ANRADAAVPE
     AQPTDMFTTH LPQVHHADDT SVIPLQADPN SNETSILPAH PEPPGGIPVP VPEPPPPAPR
     PETALQPEGG SAPASEQLDI QPVTNRSKAK LAVWIALITL LIAGVAIGGW WFGSGRYGDI
     PQVLGLEEYQ AVAVVEEAGF IPVTDTRYHN EVPAGSIIGT DPSFGERLPR GEDVTILVSQ
     GRPVVPDLGE DRSVETVRSA LEDRTFVWVD APGEYSDDIP EGQVASTTPP PGTDLDIGSH
     VQVHLSRGPA PVVIPDVSGM GVDQATRVLE NAGINVERVE EAFDPETPRG RVFATSPDIA
     SEVSRGDEIV LRVSNAIEVP DVLGLREDEA LEALAEAGVT VASTSSVPDE AARTADTVVA
     ISPEAGELIN PADPQVRLGL AGQVEVPSLL GRRVDDARDY LEDIGLTLVA DGNDDDDRIL
     TQSPRARSAV PAGSEVEVRA L
//