ID Q01UP7_SOLUE Unreviewed; 947 AA.
AC Q01UP7;
DT 14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 14-NOV-2006, sequence version 1.
DT 27-MAR-2024, entry version 100.
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=Acid_5676 {ECO:0000313|EMBL:ABJ86623.1};
OS Solibacter usitatus (strain Ellin6076).
OC Bacteria; Acidobacteriota; Terriglobia; Bryobacterales; Solibacteraceae;
OC Solibacter.
OX NCBI_TaxID=234267 {ECO:0000313|EMBL:ABJ86623.1};
RN [1] {ECO:0000313|EMBL:ABJ86623.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Ellin6076 {ECO:0000313|EMBL:ABJ86623.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Janssen P.H., Kuske C.R., Richardson P.;
RT "Complete sequence of Solibacter usitatus Ellin6076.";
RL Submitted (OCT-2006) 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; CP000473; ABJ86623.1; -; Genomic_DNA.
DR AlphaFoldDB; Q01UP7; -.
DR STRING; 234267.Acid_5676; -.
DR KEGG; sus:Acid_5676; -.
DR eggNOG; COG0515; Bacteria.
DR eggNOG; COG1262; Bacteria.
DR eggNOG; COG1506; Bacteria.
DR HOGENOM; CLU_302644_0_0_0; -.
DR InParanoid; Q01UP7; -.
DR OrthoDB; 127412at2; -.
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; cd14014; STKc_PknB_like; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 3.90.1580.10; paralog of FGE (formylglycine-generating enzyme); 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR005532; SUMF_dom.
DR InterPro; IPR042095; SUMF_sf.
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; PF03781; FGE-sulfatase; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:ABJ86623.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:ABJ86623.1};
KW Transferase {ECO:0000313|EMBL:ABJ86623.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 289..307
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 9..273
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 947 AA; 104715 MW; B4694C13C2D8CDA2 CRC64;
MIGTRIGNYR ILEKLGQGGM GEVYRAEDER LKRSVAIKVL RHHENRDAAL RFLQEARAAS
ALNHPNIVQI YDLESHDGRD FIVMELASGR TLAALVRDHP LRVEEALDYA SQLASALAAA
HAGGIVHRDI KPANIVVSES GTIKVLDFGI AKLEPHGPSG DSTETAAPET AAGSFLGTVA
YASPEQAQGR PVDARSDIFS AGAVMYEMLT GTRAFDGDST PGILSKVLRD QPRAICELRA
EVPPAVARIV NRCLEKDIAL RYPSGTELAA DLTGCRAAPA AGISNLSRVA IAAVLLAAIG
LAGWLYYRSS RARWARNEAL PKIRQLIGKD DFPAAFDLTR AALSYVPDDP QLKQQWSEVS
LPLTMTTTPP GVTVSYRPYG DAALPWQPVG RTPLENVRVP LAYMRVRLAK EGWEPMEFAT
HTGFLVNGNL PLLRFGQVAA GMVKVASQAS WAAPNNLMPL PDYFLDKFEV TNREYQQFVD
SGGYRDAKHW RHSFLKDHRE VPREQALLLF RDTTGRPGPA RWELGAFPKG QADFPVSGVS
WFEAAAYCES VGKTLPTVHH WRKAAAFDVF SEILLFSNFS GTGPARVGAN PGITTFGAYD
MAGNVKEWCW NQTGELRSIL GGGWNEPSYA YRDDDAQDPM KREVTYGVRC AMYPSAVPAE
ALAPIGPPVR DYSTEKPVSD ETFEIFRRMY AYDRTPLNGK TESVDDSNED WRKEKVSYSA
AYGGERITAY LYLPRNAKPP YQTVLWVPGG YAWMLRNSET GVGTEFFNFL LRTGRAVLYP
VYQGTFERHV DNGGGPNARR DWTIQFAKDV SRSVDYLETR TDTQKDRLAY YGLSVGGTFG
ALFLALEPRL KTGILAAGGL FGERPPPEAD VLNFAPRVHV PVLMLNGRYD FVAPPATLQR
PMFRWLGTAE PDKRLIQFES GHMPPVEDLM REVLDWLDRY LGPVAPM
//
