ID B4D509_9BACT Unreviewed; 756 AA.
AC B4D509;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, 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 ORFNames=CfE428DRAFT_3997 {ECO:0000313|EMBL:EDY18612.1};
OS Chthoniobacter flavus Ellin428.
OC Bacteria; Verrucomicrobiota; Spartobacteria; Chthoniobacterales;
OC Chthoniobacteraceae; Chthoniobacter.
OX NCBI_TaxID=497964 {ECO:0000313|EMBL:EDY18612.1, ECO:0000313|Proteomes:UP000005824};
RN [1] {ECO:0000313|EMBL:EDY18612.1, ECO:0000313|Proteomes:UP000005824}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ellin428 {ECO:0000313|EMBL:EDY18612.1,
RC ECO:0000313|Proteomes:UP000005824};
RX PubMed=21460085; DOI=10.1128/JB.00295-11;
RA Kant R., van Passel M.W., Palva A., Lucas S., Lapidus A.,
RA Glavina Del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S.,
RA Larimer F.W., Land M.L., Hauser L., Sangwan P., de Vos W.M., Janssen P.H.,
RA Smidt H.;
RT "Genome sequence of Chthoniobacter flavus Ellin428, an aerobic
RT heterotrophic soil bacterium.";
RL J. Bacteriol. 193:2902-2903(2011).
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:EDY18612.1}.
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DR EMBL; ABVL01000012; EDY18612.1; -; Genomic_DNA.
DR AlphaFoldDB; B4D509; -.
DR STRING; 497964.CfE428DRAFT_3997; -.
DR eggNOG; COG0515; Bacteria.
DR InParanoid; B4D509; -.
DR Proteomes; UP000005824; Unassembled WGS sequence.
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; cd00161; RICIN; 1.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 2.80.10.50; -; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
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; PF00069; Pkinase; 1.
DR Pfam; PF14200; RicinB_lectin_2; 2.
DR SMART; SM00458; RICIN; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF50370; Ricin B-like lectins; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:EDY18612.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000005824};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:EDY18612.1};
KW Transferase {ECO:0000313|EMBL:EDY18612.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 313..335
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 30..286
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 639..701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 639..657
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..683
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 684..701
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 59
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 756 AA; 82453 MW; 8E681DC3C3DD9617 CRC64;
MDVTDVEPLS AVVCPTCGAP STVSTMIDHF ELVDMLGHGG MGAVYKAHDT SLDRMVALKL
LKKSSGTPEQ IKQLETEAAI TASINHPHVV RVFSTGMDHG RFYIAMELVE KGTLDKLIEL
QGRVAEAQVL EVGIQIASGL RAAHEAGLIH RDVKPGNILF TDAHTSKIVD FGLAIFAEDE
VKVRGEIWGT PYYVAPEKLD QKPEDFRSDI YSLGGTLFHA LAGRPPFEAE NASLVALKHL
KSQAVSLQAF APQVSSNTNY VINRTLNKDP EKRYQSYDEL IEHLEYALNE LQAGRGKAEG
KRVVLETEQE KKAMGVLTFA MIGVLVVLLG VGVLFRNQIF SGSPEEQAKK GSALMAEGVS
GLAKSEPASA VTSLAAVAAQ KPKQPWLNWA DMLMGLAQIA SGHRQEGMSS FQRVEARGPY
SKSDADKATA DFFMETTRQM TSEHVIDPKA VQAPAGGAGP AAFLFYGMKD WEAGAVDEAA
DFFRRFRQAE FTGTDAWLEG LKPMATDYVE EYTAYQMAAD AWKGAKTIDQ KRTAVKQLRA
VQGKLAPKAQ ELAVTAAAEL SKVEKERSAM LAQGKIPDGR YRLTNRKTGK ALEVEGHSHD
DGHKVQTYSY NNGGNQQWRI IPQDNGTYML VNAEGGKALS LPTNPTTLDH HNPPSNGKPT
ATPTPTPKPD PKAPKPTPTP TPKPVTDDNT QAQQSNVNKA IPWQRWRIEK IENNYFKITS
QLDGKALTAK GQDNGAAVIQ APYDNAQEQQ WKIEGL
//
