ID YRZF_BACSU Reviewed; 215 AA. AC O32057; C0SPA9; Q799D9; DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot. DT 05-MAY-2009, sequence version 2. DT 27-MAR-2024, entry version 133. DE RecName: Full=Putative serine/threonine-protein kinase YrzF; DE EC=2.7.11.1; GN Name=yrzF; OrderedLocusNames=BSU27785; ORFNames=BSU27780; OS Bacillus subtilis (strain 168). OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=224308; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=168; RA Tosato V., Bolotin A., Bertani I., Valentino I., Bruschi C.V.; RT "A 17.8 kb segment in the spoVB-nadC region of the Bacillus subtilis 168 RT chromosome: sequencing and ruv operon identification."; RL Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=168; RX PubMed=9384377; DOI=10.1038/36786; RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K., RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., RA Yoshikawa H., Danchin A.; RT "The complete genome sequence of the Gram-positive bacterium Bacillus RT subtilis."; RL Nature 390:249-256(1997). RN [3] RP SEQUENCE REVISION TO C-TERMINUS. RX PubMed=19383706; DOI=10.1099/mic.0.027839-0; RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.; RT "From a consortium sequence to a unified sequence: the Bacillus subtilis RT 168 reference genome a decade later."; RL Microbiology 155:1758-1775(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 -!- 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; CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein CC kinase family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=CAB75326.1; Type=Frameshift; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Y15896; CAB75326.1; ALT_FRAME; Genomic_DNA. DR EMBL; AL009126; CAB14738.2; -; Genomic_DNA. DR PIR; E69982; E69982. DR RefSeq; NP_390656.2; NC_000964.3. DR RefSeq; WP_003246159.1; NZ_JNCM01000036.1. DR AlphaFoldDB; O32057; -. DR SMR; O32057; -. DR STRING; 224308.BSU27785; -. DR PaxDb; 224308-BSU27785; -. DR EnsemblBacteria; CAB14738; CAB14738; BSU_27785. DR GeneID; 936570; -. DR KEGG; bsu:BSU27785; -. DR PATRIC; fig|224308.179.peg.3018; -. DR eggNOG; COG2112; Bacteria. DR InParanoid; O32057; -. DR OrthoDB; 529320at2; -. DR BioCyc; BSUB:BSU27785-MONOMER; -. DR Proteomes; UP000001570; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR002575; Aminoglycoside_PTrfase. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR PANTHER; PTHR37171; SERINE/THREONINE-PROTEIN KINASE YRZF-RELATED; 1. DR PANTHER; PTHR37171:SF1; SERINE_THREONINE-PROTEIN KINASE YRZF-RELATED; 1. DR Pfam; PF01636; APH; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. PE 3: Inferred from homology; KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome; KW Serine/threonine-protein kinase; Transferase. FT CHAIN 1..215 FT /note="Putative serine/threonine-protein kinase YrzF" FT /id="PRO_0000387941" FT DOMAIN 27..215 FT /note="Protein kinase" FT ACT_SITE 135 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT BINDING 33..41 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 54 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" SQ SEQUENCE 215 AA; 24720 MW; 9C019DDEFE44490F CRC64; MLTKAEALAH TVIYRKNSRF DKVKEKSEEL TLIGKGRSAY VFALTEGGRK MALKVFFPEY QATAVKEAAI YEKLAGSAFY PDIYETGDSF ILMEYIKGET FYNCLKKGIA ISDDMIQQVE EALSDARAAG LNPSDIHLRN LILTETGAVR VIDVARFEQT KTCTQWDDLK SAYHALYKKP IFPKKIPGFW LEIIAFLYKK DWFQKHFAQR KRKYS //