ID   Q1IV32_KORVE            Unreviewed;       894 AA.
AC   Q1IV32;
DT   13-JUN-2006, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2006, sequence version 1.
DT   27-MAR-2024, entry version 98.
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_0263 {ECO:0000313|EMBL:ABF39268.1};
OS   Koribacter versatilis (strain Ellin345).
OC   Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC   Koribacter.
OX   NCBI_TaxID=204669 {ECO:0000313|EMBL:ABF39268.1, ECO:0000313|Proteomes:UP000002432};
RN   [1] {ECO:0000313|EMBL:ABF39268.1, ECO:0000313|Proteomes:UP000002432}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ellin345 {ECO:0000313|EMBL:ABF39268.1,
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; ABF39268.1; -; Genomic_DNA.
DR   RefSeq; WP_011521070.1; NC_008009.1.
DR   AlphaFoldDB; Q1IV32; -.
DR   STRING; 204669.Acid345_0263; -.
DR   EnsemblBacteria; ABF39268; ABF39268; Acid345_0263.
DR   KEGG; aba:Acid345_0263; -.
DR   eggNOG; COG0515; Bacteria.
DR   eggNOG; COG0823; Bacteria.
DR   HOGENOM; CLU_012906_0_0_0; -.
DR   Proteomes; UP000002432; Chromosome.
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; 2.120.10.30; TolB, C-terminal domain; 2.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   Gene3D; 2.120.10.60; Tricorn protease N-terminal domain; 1.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR011659; PD40.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR43289; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED; 1.
DR   PANTHER; PTHR43289:SF32; SERINE_THREONINE-PROTEIN KINASE PKAB; 1.
DR   Pfam; PF07676; PD40; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF82171; DPP6 N-terminal domain-like; 2.
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:ABF39268.1};
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:ABF39268.1};
KW   Transferase {ECO:0000313|EMBL:ABF39268.1}.
FT   DOMAIN          16..297
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         45
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   894 AA;  96431 MW;  3E2462C300501C42 CRC64;
     MAHHMAVAPG TKLGPYEIQS QLGAGGMGEV YRAKDLRLDR SVAIKVLPGH LSSNPELKER
     FVREARAISS LNHPRICTLH DVGQQEGVDF LVMEFLEGES LAQRLQKGAL PIKEVLKIGV
     EVSEALEVAH RAGIVHRDLK PGNIMLTKTG AKLMDFGLAK AVESTMAAGT SSAPLLSGAP
     TMSGLSPLSP LTMAGAVVGT VQYMAPEQVE GKLADARSDI FALGATLYEA ATGKRAFDGK
     SQIAVANSIL EKDPEPASTL NPQVPRGVDH VIARCLAKDP EQRWQTARDL GLELGWSAQA
     SPSSTQITPV KRRSQSLPWI VSGALALLLL VALFSWLNRS SPATQAQYFA APFTFTARDL
     TIAPNGHTVA VVGYRSEAHK NGIFLYELGS QNVRLVPDTD GASFPFWSAD GLSLGFFADG
     KLRRVDIAGG PAQTLCDAPG GRGGTWNKDG VIVFTPSGAL RTGLWRISAA GGKPEQLTTP
     DASKGEDGHR WPVFLPDGQH YIYTIFNNTV HTEFAGLAVG ALGSKEQHFL LHAISNGSYA
     APGYLLYYRD NTLFAQRFNA TKLQLEGEPA ALLSDLQYMP RIQRATFSST GTGAVLAQLR
     TGNAVSQLTW FDRSGKSLGD VADPDYFGAL SLSPNGQSLA VDKVDSGSQN TDVWLLDLHG
     GAPRRITFDP SIDALPVWSP AASEIAFVTN RELHFSVYRK SVDGHATESV LINDLPDNYP
     NDWSRDGKYF LYVHGTGLWY LTFSDMTKKE FLNAGTSALK TGHFSPDGKW IAYASNESGK
     WEIYVTSFPD AKGKWEISSG GGEQPHWRGD GKELYYLSSS AKMMAVPVTT GANFSAGTPA
     ALFQADPREL VATTEQVGYD VSSDGQKFLI NSAIRNGESQ QVTVILNWNE KLNK
//