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Database: UniProt
Entry: H8MFL4_CORCM
LinkDB: H8MFL4_CORCM
Original site: H8MFL4_CORCM 
ID   H8MFL4_CORCM            Unreviewed;       672 AA.
AC   H8MFL4;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2012, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   Name=pknB10 {ECO:0000313|EMBL:AFE09898.1};
GN   OrderedLocusNames=COCOR_05744 {ECO:0000313|EMBL:AFE09898.1};
OS   Corallococcus coralloides (strain ATCC 25202 / DSM 2259 / NBRC 100086 / M2)
OS   (Myxococcus coralloides).
OC   Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC   Myxococcaceae; Corallococcus.
OX   NCBI_TaxID=1144275 {ECO:0000313|EMBL:AFE09898.1, ECO:0000313|Proteomes:UP000007587};
RN   [1] {ECO:0000313|EMBL:AFE09898.1, ECO:0000313|Proteomes:UP000007587}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25202 / DSM 2259 / NBRC 100086 / M2
RC   {ECO:0000313|Proteomes:UP000007587};
RX   PubMed=22582372; DOI=10.1128/JB.00397-12;
RA   Huntley S., Zhang Y., Treuner-Lange A., Kneip S., Sensen C.W.,
RA   Sogaard-Andersen L.;
RT   "Complete Genome Sequence of the Fruiting Myxobacterium Corallococcus
RT   coralloides DSM 2259.";
RL   J. Bacteriol. 194:3012-3013(2012).
RN   [2] {ECO:0000313|Proteomes:UP000007587}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25202 / DSM 2259 / NBRC 100086 / M2
RC   {ECO:0000313|Proteomes:UP000007587};
RA   Huntley S., Zhang Y., Treuner-Lange A., Sensen C.W., Sogaard-Andersen L.;
RT   "Genome sequence of the fruiting myxobacterium Corallococcus coralloides
RT   DSM 2259.";
RL   Submitted (MAR-2012) 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; CP003389; AFE09898.1; -; Genomic_DNA.
DR   RefSeq; WP_014398532.1; NC_017030.1.
DR   AlphaFoldDB; H8MFL4; -.
DR   STRING; 1144275.COCOR_05744; -.
DR   KEGG; ccx:COCOR_05744; -.
DR   eggNOG; COG0515; Bacteria.
DR   eggNOG; COG2114; Bacteria.
DR   eggNOG; COG4753; Bacteria.
DR   HOGENOM; CLU_433379_0_0_7; -.
DR   InParanoid; H8MFL4; -.
DR   OrthoDB; 9801841at2; -.
DR   Proteomes; UP000007587; Chromosome.
DR   GO; GO:0004016; F:adenylate cyclase activity; IEA:UniProt.
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:0009190; P:cyclic nucleotide biosynthetic process; IEA:InterPro.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd07302; CHD; 1.
DR   CDD; cd17536; REC_YesN-like; 1.
DR   CDD; cd14014; STKc_PknB_like; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 3.30.70.1230; Nucleotide cyclase; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR001054; A/G_cyclase.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR029787; Nucleotide_cyclase.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   PANTHER; PTHR43289; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED; 1.
DR   PANTHER; PTHR43289:SF6; SERINE_THREONINE-PROTEIN KINASE NEKL-3; 1.
DR   Pfam; PF00211; Guanylate_cyc; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   SMART; SM00044; CYCc; 1.
DR   SMART; SM00448; REC; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000313|EMBL:AFE09898.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007587};
KW   Serine/threonine-protein kinase {ECO:0000313|EMBL:AFE09898.1};
KW   Transferase {ECO:0000313|EMBL:AFE09898.1}.
FT   DOMAIN          11..274
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          287..406
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          455..585
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
FT   REGION          635..672
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          395..422
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         40
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT   MOD_RES         341
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   672 AA;  71673 MW;  51D5A4B036CCCB19 CRC64;
     MDTGRPLGGR YALERRIGGG GMGAIWRAVD LQLQRHVALK LIASDVVART PEAHRHFEQE
     AQAVARLRHP HVVQVHDSGV DGGVPYIVME LLEGEDLETR LTQQGRLSPA RVAALVTPVA
     RALAAAHAAG LVHRDLKPAN LFLAHVDGEE VVKVLDFGLA RSLLPNGAPA QAEGLTGTLR
     YMSPEQLRAD PDLDARADLW SLAVVLYRAL TGQFPYGAES VGALLRGAFH PPAVPVSQLV
     PELGASGDAF FQRALSPTLA QRFTSARELA AAFVALVEAG RAGQAATVLV VDDEPDVELL
     MRQRFRRHVR DGVYRFVFAR DGEEALEALR QHPDTHAVLC DLNMPRMDGL TFLSRVGEVD
     PLVKVVMVSA YGDLPNLRTA MNRGAFDFLV KPVDLDDLES TLAKTVRHVA ELRRAVRSTE
     ENALLRMFVH GGIVDRVLPL VRGPGGLAGE QVDATVAFLD VADFTAVTRQ HPPESALRRL
     NANFEVILPE LESRGGVVDK FLGDAVMAVF QGEGHVARAL DACLAVRQRL QGLAWSGGDA
     SPYAHGVCMG VDTGPVLSGN VGAAGRGRLD HTVLGDVVNT AARLATVAAR DQVLVSEALA
     ARLQDAFDCR LAGDRHLPGA GGQALAVREV VARHGSQSAS SADRTSEQVA PAVMEAPASP
     PRPGAFTAKG PT
//
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