ID   Q1INH1_KORVE            Unreviewed;       985 AA.
AC   Q1INH1;
DT   13-JUN-2006, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2006, sequence version 1.
DT   27-MAR-2024, entry version 102.
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=Acid345_2578 {ECO:0000313|EMBL:ABF41579.1};
OS   Koribacter versatilis (strain Ellin345).
OC   Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC   Koribacter.
OX   NCBI_TaxID=204669 {ECO:0000313|EMBL:ABF41579.1, ECO:0000313|Proteomes:UP000002432};
RN   [1] {ECO:0000313|EMBL:ABF41579.1, ECO:0000313|Proteomes:UP000002432}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ellin345 {ECO:0000313|EMBL:ABF41579.1,
RC   ECO:0000313|Proteomes:UP000002432};
RX   PubMed=19201974; DOI=10.1128/AEM.02294-08;
RA   Ward N.L., Challacombe J.F., Janssen P.H., Henrissat B., Coutinho P.M.,
RA   Wu M., Xie G., Haft D.H., Sait M., Badger J., Barabote R.D., Bradley B.,
RA   Brettin T.S., Brinkac L.M., Bruce D., Creasy T., Daugherty S.C.,
RA   Davidsen T.M., DeBoy R.T., Detter J.C., Dodson R.J., Durkin A.S.,
RA   Ganapathy A., Gwinn-Giglio M., Han C.S., Khouri H., Kiss H., Kothari S.P.,
RA   Madupu R., Nelson K.E., Nelson W.C., Paulsen I., Penn K., Ren Q.,
RA   Rosovitz M.J., Selengut J.D., Shrivastava S., Sullivan S.A., Tapia R.,
RA   Thompson L.S., Watkins K.L., Yang Q., Yu C., Zafar N., Zhou L., Kuske C.R.;
RT   "Three genomes from the phylum Acidobacteria provide insight into the
RT   lifestyles of these microorganisms in soils.";
RL   Appl. Environ. Microbiol. 75:2046-2056(2009).
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; CP000360; ABF41579.1; -; Genomic_DNA.
DR   RefSeq; WP_011523380.1; NC_008009.1.
DR   AlphaFoldDB; Q1INH1; -.
DR   STRING; 204669.Acid345_2578; -.
DR   EnsemblBacteria; ABF41579; ABF41579; Acid345_2578.
DR   KEGG; aba:Acid345_2578; -.
DR   eggNOG; COG0412; Bacteria.
DR   eggNOG; COG0515; Bacteria.
DR   eggNOG; COG1262; Bacteria.
DR   HOGENOM; CLU_302644_0_0_0; -.
DR   OrthoDB; 127412at2; -.
DR   Proteomes; UP000002432; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016787; F:hydrolase activity; 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; 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; IPR002925; Dienelactn_hydro.
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; PF01738; DLH; 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:ABF41579.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000002432};
KW   Serine/threonine-protein kinase {ECO:0000313|EMBL:ABF41579.1};
KW   Transferase {ECO:0000313|EMBL:ABF41579.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        306..325
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          12..285
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         41
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   985 AA;  109383 MW;  ED7E0D8F3D7DB177 CRC64;
     MALAPGTKIG PYQVDALLGK GGMGEVYTAR DTRLQRTVAI KILPSHLSYN PDLRARFEQE
     AKSISALQHP NICVIHDVGS QDDIEFMVME YVQGDTLDKL IPKGGLPAEI AIRYAIQIAD
     AIGCAHSAGI VHRDLKPSNV IVDKSGLVKV LDFGLAKTSA LAAQAGAMET ITVGTSPGTI
     VGTVAYMSPE QAEGKAVDTR SDVFSFGAVF YEMLSGHRAF EGESSAALLA SVLRDEPKPL
     TEVRRDLDPE IRRIVTRCLK KDPAARYADG NDLARDLKRC RETLFPESGT GMSAVRLAHE
     VKRPRVLIPA VLLLLLIAAG TMMLVKRSRD AHWARETALP QISQLVDEGK FETAFQLATK
     AESAIPGDPA LEKVWKQVTF ELTLETSAPD VSVYRREYDD HNGPWIFVGK APFKSIRQPR
     GTRLWKLEKP GYVTVIRTTN SLLDRYFVST DPMTAHVTMD AVADAPPGMV RVAPSKSLKE
     LLIPGFEGMP HLDLPDYWLD QYEVTNRAFE AFVDAGGYRN PSFWKHDFIR DGKKLTFDQA
     MALFQDATGR TGPKDWVGGQ YPKGQDDYPV AGISWYEAAA YAEYAGKSLP SIYHFNRAAG
     PQFSYLIEPA SNFGTGGPVP VGSRQGIGPF GTSDMAGNVK EWIFTEAENG KHYVLGGAWD
     EPTYMFVDPD AQAPFLRASN IGFRCVKYIN PDAIPKVAFD RILSARRDLT AVKPVSDQVF
     SAYRSLYSYD KAPLNAHVDK LEKTEDDWTV EKIAYDAPYG NERAFAYLFL PTKANPPFQT
     VLFFPGSNAL ELRKFNLYPT AAIDALVRSG RAVIYPVYKG TYERGDGMES DVPNMSTTWR
     DHVVMWAKDA SRAIDYVESR PDLDHAKVAY YGYSWGSEMG TIIPAIEPRI KVVTLALGGF
     DLHQSLPEVD TVNFAQRIKQ PTLMLNGRYD FFFPMDATQE PLYRMLGAPK DDKKHLIYDT
     SHTIPRNELI KENLNWLDKY LGPVK
//