ID   Q1IIB0_KORVE            Unreviewed;       938 AA.
AC   Q1IIB0;
DT   13-JUN-2006, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2006, sequence version 1.
DT   27-MAR-2024, entry version 103.
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_4390 {ECO:0000313|EMBL:ABF43390.1};
OS   Koribacter versatilis (strain Ellin345).
OC   Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC   Koribacter.
OX   NCBI_TaxID=204669 {ECO:0000313|EMBL:ABF43390.1, ECO:0000313|Proteomes:UP000002432};
RN   [1] {ECO:0000313|EMBL:ABF43390.1, ECO:0000313|Proteomes:UP000002432}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ellin345 {ECO:0000313|EMBL:ABF43390.1,
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; ABF43390.1; -; Genomic_DNA.
DR   RefSeq; WP_011525187.1; NC_008009.1.
DR   AlphaFoldDB; Q1IIB0; -.
DR   STRING; 204669.Acid345_4390; -.
DR   EnsemblBacteria; ABF43390; ABF43390; Acid345_4390.
DR   KEGG; aba:Acid345_4390; -.
DR   eggNOG; COG0515; Bacteria.
DR   eggNOG; COG0823; Bacteria.
DR   HOGENOM; CLU_012906_0_0_0; -.
DR   OrthoDB; 101360at2; -.
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: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; 3.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 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:ABF43390.1};
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:ABF43390.1};
KW   Transferase {ECO:0000313|EMBL:ABF43390.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        350..371
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          9..287
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          280..311
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        291..311
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         38
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   938 AA;  100539 MW;  C7ADFC3A5EF017E1 CRC64;
     MIGQTFSHYR ILEKLGGGGM GVVYKAEDTR LHRFVALKFL PPELARDPQA LARFQREAQA
     ASALNHPNIC TIYDIGDDNG QGFIAMEFLE GMTLKHRINS QPVDLETVLT LAIDIADALD
     AAHSKGIVHR DIKPANIFVI ERGHAKVLDF GLAKVTPRSA SSVPSANTMT ATELAVEDEH
     LTSPGSTLGT IAYMSPEQAK GKELDARSDL FSFGSVLYEM VTGALPFQGE TSALMFDAIL
     NRDPLPPLRF NPKVPAKLEE IIQKALEKDR DLRYQHASEM RSDLKRLQRD SSSAPRQASA
     PTTEASSARV SAAYVPPSSS ASAAPVAQAS APSHSTGSSS VIAVAREHKF GLVGIAVVAL
     GLLGAGGFGI YEFLSRSAQA PFQNFTVAQL TNTGKARQSA ISPDGKYVVS VQDDNGVRSL
     WLRNVPTGSD TQVLPPSPVI YATLTFSPDG NYIYYRKASS AAQSEWDIFR IPVLGGSPQV
     LAKDVDSNVT FSPDGTKMAY FRGNDPEVGK LYFLIANLDG SNEETVYIGS AVDLPRSIAW
     SADGKRLFYN IFTLKTALSE IRQIEIASKK ASLLSAQTST LVQELERLPG SSSLLIRGLD
     KSNYTKSQIG VLSDSGQVVP ITRDTNSYEG MSLSGDGKTI AAVQQRVTRT FWTAAMSNDA
     LAAPPQSVAG VENAHTFAFN PDGSLLVSDD QTLRRTDLAG AATTTVLGDG NAYIVELAPC
     GDRYFVLQWA FHGGGYSYPV WRVNLDGSNP LRLTDGSYDG RPNCSPDGKT VYFEPTTSKA
     TVARVPIDGG KQETVPGSEV ERGFGIGVGH AVSPDGKLLA FNAEISTDAQ GHVGEKIVFV
     TLDGSGAAQR IINADPRISS GRLANTLTFT PDGKSVAYVV REHGVENVFI QPIDGTPGHQ
     LTNFTSQLIS NFHWSPDGKT LAIARADASS DVVLLKEK
//