(data stored in ACNUC7421 zone)

SWISSPROT: YBDM_BACSU

ID   YBDM_BACSU              Reviewed;         256 AA.
AC   O31435; Q7DL55;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   11-DEC-2019, entry version 124.
DE   RecName: Full=Probable serine/threonine-protein kinase YbdM;
DE            EC=2.7.11.1;
GN   Name=ybdM; OrderedLocusNames=BSU02030;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RA   Haga K., Liu H., Yasumoto K., Takahashi H., Yoshikawa H.;
RT   "Sequence analysis of the 70kb region between 17 and 23 degree of the
RT   Bacillus subtilis chromosome.";
RL   Submitted (JUL-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).
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   -!- INTERACTION:
CC       P37469:dnaC; NbExp=3; IntAct=EBI-5255200, EBI-2122822;
CC       O34483:hprK; NbExp=5; IntAct=EBI-5255200, EBI-5242785;
CC       O34507:prkC; NbExp=3; IntAct=EBI-5255200, EBI-6667154;
CC       P42411:rsbT; NbExp=3; IntAct=EBI-5255200, EBI-5247957;
CC       P10728:spoIIAB; NbExp=2; IntAct=EBI-5255200, EBI-9344705;
CC       P37562:yabT; NbExp=2; IntAct=EBI-5255200, EBI-9303331;
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
DR   EMBL; AB006424; BAA33101.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB11997.1; -; Genomic_DNA.
DR   PIR; H69747; H69747.
DR   RefSeq; NP_388085.1; NC_000964.3.
DR   RefSeq; WP_003234892.1; NZ_JNCM01000030.1.
DR   SMR; O31435; -.
DR   IntAct; O31435; 14.
DR   STRING; 224308.BSU02030; -.
DR   PaxDb; O31435; -.
DR   PRIDE; O31435; -.
DR   EnsemblBacteria; CAB11997; CAB11997; BSU02030.
DR   GeneID; 938464; -.
DR   KEGG; bsu:BSU02030; -.
DR   PATRIC; fig|224308.179.peg.209; -.
DR   eggNOG; ENOG4105G0J; Bacteria.
DR   eggNOG; COG0515; LUCA.
DR   HOGENOM; HOG000089759; -.
DR   InParanoid; O31435; -.
DR   KO; K08884; -.
DR   OMA; GSYGIAY; -.
DR   PhylomeDB; O31435; -.
DR   BioCyc; BSUB:BSU02030-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   Pfam; PF00069; Pkinase; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   1: Evidence at protein level;
DR   PRODOM; O31435.
DR   SWISS-2DPAGE; O31435.
KW   ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..256
FT                   /note="Probable serine/threonine-protein kinase YbdM"
FT                   /id="PRO_0000360793"
FT   DOMAIN          25..256
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   NP_BIND         31..39
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        149
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         54
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   256 AA;  30059 MW;  2F9750DB23295343 CRC64;
     MALKLLKKLL FDRPLKNGVI LNHQYKIEEC LGMGGYGLVY LCTDILAQTP YVLKQLRPTK
     AKKEKEKVRF QQEIKLLKNI HHPQIPGFID EFIIDGQAYY VMQFIEGENI EELLFFRKQP
     FTELMALQLI SQLLEIIEYL HDRLIFHSDI RTPNIIINDG RLCLIDFGLA KQLTPEEMEE
     IKVRKQDDFF DLGETLLFLL YSQYKGKKKK NGTWLEELTL TKEVTLLLKR LLGIEEEYQH
     TASIREDLNR AIQSVT
//

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