ID Q1IJ33_KORVE Unreviewed; 769 AA.
AC Q1IJ33;
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_4117 {ECO:0000313|EMBL:ABF43117.1};
OS Koribacter versatilis (strain Ellin345).
OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC Koribacter.
OX NCBI_TaxID=204669 {ECO:0000313|EMBL:ABF43117.1, ECO:0000313|Proteomes:UP000002432};
RN [1] {ECO:0000313|EMBL:ABF43117.1, ECO:0000313|Proteomes:UP000002432}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ellin345 {ECO:0000313|EMBL:ABF43117.1,
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; ABF43117.1; -; Genomic_DNA.
DR RefSeq; WP_011524916.1; NC_008009.1.
DR AlphaFoldDB; Q1IJ33; -.
DR STRING; 204669.Acid345_4117; -.
DR EnsemblBacteria; ABF43117; ABF43117; Acid345_4117.
DR KEGG; aba:Acid345_4117; -.
DR eggNOG; COG0457; Bacteria.
DR eggNOG; COG0515; Bacteria.
DR eggNOG; COG5616; Bacteria.
DR HOGENOM; CLU_013589_0_0_0; -.
DR OrthoDB; 9797180at2; -.
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; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR Gene3D; 3.40.50.10070; TolB, N-terminal domain; 1.
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; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
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; PF14559; TPR_19; 1.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00028; TPR; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50005; TPR; 2.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:ABF43117.1};
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:ABF43117.1};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW Transferase {ECO:0000313|EMBL:ABF43117.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 311..332
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 9..286
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REPEAT 573..606
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 643..676
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT BINDING 38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 769 AA; 83583 MW; B4290BDB89FDE1FD CRC64;
MIGQTISHYQ IVEKIGGGGM GVVYKAEDTR LHRFVALKFL PANVAGDAQA LARFRREAQA
ASALNHPNIC TIYDIGEENG QAFIAMEFLD GMTLKHKASG LAMDMDTILP FAIEIADALD
AAHTAGIVHR DIKPANLFLT KRGHAKVLDF GLAKVGGAAA ASATSKPADN TISVVRDEDL
TSPGSTLGTV AYMSPEQVAA KDLDARTDLF SFGVVLYEIA TGRLPFPGES TGLIFKAILD
NAPEPMTKLN PAIPAEFERV VFKALEKDRD LRYQSAAELR ADLKRIQRGS ESLRSSVVQA
PAKRRLSNKQ IARIAITGAV ALLLIIFSSI AWQRSHDAAK QTAATSSSKP SVAVLPLKNL
SGDGDNNYFS EGMTEEITTK LSKIQAINVA SHSSVVAAKT ADKSATDIGK ALNVRYVLEG
SVRKAGNEVR INVQLIDAAN GFQVWADDFT GEMKDVFSLQ EQTAMKIAQS LNLKLSPQEE
QAIQHRATDN PQAYDAYLRG SALTNTFDSK DALEGARKNF EEALKYDANY PPAVAGLSWV
EAQLYRNVES DPKHLELAEK YGQKALQLAP DAADTHLAIG SIAAIKYDYN TAAREFRRAT
ELAPDSGYAS DLLSWALSYQ IPPDPIGAEA AARKALRLQA SIYPAYYHLG RALIAQGRYS
EALESFEQMR RLSPTSNTAG LGFGQVYIAQ GEYDKAIEVL LKYPQANTIN YYWLAAAYAA
KGDNAKALAT IQKAFDLGFR DFGAINASPY FEKLRSDPKF QAMVAKYRK
//
