YWQD_BACSU
ID YWQD_BACSU Reviewed; 237 AA.
AC P96716;
DT 01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Tyrosine-protein kinase YwqD;
DE EC=2.7.10.2;
GN Name=ywqD; OrderedLocusNames=BSU36250;
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;
RX PubMed=9353933; DOI=10.1099/00221287-143-10-3313;
RA Presecan E., Moszer I., Boursier L., Cruz Ramos H., De La Fuente V.,
RA Hullo M.-F., Lelong C., Schleich S., Sekowska A., Song B.H., Villani G.,
RA Kunst F., Danchin A., Glaser P.;
RT "The Bacillus subtilis genome from gerBC (311 degrees) to licR (334
RT degrees).";
RL Microbiology 143:3313-3328(1997).
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 FUNCTION, MUTAGENESIS OF ASP-81; ASP-83; TYR-225; TYR-227 AND TYR-228, AND
RP PHOSPHORYLATION AT TYR-228.
RX PubMed=12970183; DOI=10.1093/emboj/cdg458;
RA Mijakovic I., Poncet S., Boel G., Maze A., Gillet S., Jamet E.,
RA Decottignies P., Grangeasse C., Doublet P., Le Marechal P., Deutscher J.;
RT "Transmembrane modulator-dependent bacterial tyrosine kinase activates UDP-
RT glucose dehydrogenases.";
RL EMBO J. 22:4709-4718(2003).
RN [4]
RP FUNCTION.
RC STRAIN=168;
RX PubMed=16549871; DOI=10.1093/nar/gkj514;
RA Mijakovic I., Petranovic D., Macek B., Cepo T., Mann M., Davies J.,
RA Jensen P.R., Vujaklija D.;
RT "Bacterial single-stranded DNA-binding proteins are phosphorylated on
RT tyrosine.";
RL Nucleic Acids Res. 34:1588-1596(2006).
CC -!- FUNCTION: May be involved in the regulation of capsular polysaccharide
CC biosynthesis. Autophosphorylates in vitro. Phosphorylates and activates
CC in vitro two UDP-glucose dehydrogenases, YwqF and TuaD, as well as the
CC DNA-binding proteins Ssb and SsbB. {ECO:0000269|PubMed:12970183,
CC ECO:0000269|PubMed:16549871}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2;
CC -!- INTERACTION:
CC P96716; O34483: hprK; NbExp=2; IntAct=EBI-9302929, EBI-5242785;
CC P96716; Q01464: minD; NbExp=4; IntAct=EBI-9302929, EBI-6502875;
CC P96716; O34507: prkC; NbExp=2; IntAct=EBI-9302929, EBI-6667154;
CC P96716; P37562: yabT; NbExp=3; IntAct=EBI-9302929, EBI-9303331;
CC P96716; P96715: ywqC; NbExp=6; IntAct=EBI-9302929, EBI-9302918;
CC -!- PTM: Autophosphorylated in vitro, which inhibits ATPase activity.
CC Dephosphorylated by YwqE in vitro. {ECO:0000269|PubMed:12970183}.
CC -!- SIMILARITY: Belongs to the CpsD/CapB family. {ECO:0000305}.
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DR EMBL; Z92952; CAB07457.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15642.1; -; Genomic_DNA.
DR PIR; G70066; G70066.
DR RefSeq; NP_391506.1; NC_000964.3.
DR RefSeq; WP_003244182.1; NZ_JNCM01000034.1.
DR AlphaFoldDB; P96716; -.
DR SMR; P96716; -.
DR IntAct; P96716; 14.
DR STRING; 224308.BSU36250; -.
DR iPTMnet; P96716; -.
DR PaxDb; P96716; -.
DR PRIDE; P96716; -.
DR EnsemblBacteria; CAB15642; CAB15642; BSU_36250.
DR GeneID; 936896; -.
DR KEGG; bsu:BSU36250; -.
DR PATRIC; fig|224308.179.peg.3923; -.
DR eggNOG; COG0489; Bacteria.
DR InParanoid; P96716; -.
DR OMA; NPVSEQF; -.
DR PhylomeDB; P96716; -.
DR BioCyc; BSUB:BSU36250-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0045226; P:extracellular polysaccharide biosynthetic process; IEA:InterPro.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR025669; AAA_dom.
DR InterPro; IPR005702; EPS_synthesis.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF13614; AAA_31; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01007; eps_fam; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Capsule biogenesis/degradation; Exopolysaccharide synthesis;
KW Kinase; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Transferase; Tyrosine-protein kinase.
FT CHAIN 1..237
FT /note="Tyrosine-protein kinase YwqD"
FT /id="PRO_0000217242"
FT SITE 81
FT /note="Required for activity"
FT SITE 83
FT /note="Required for activity"
FT MOD_RES 228
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:12970183"
FT MUTAGEN 81
FT /note="D->A: Abolishes ATPase activity."
FT /evidence="ECO:0000269|PubMed:12970183"
FT MUTAGEN 83
FT /note="D->A: Abolishes ATPase activity."
FT /evidence="ECO:0000269|PubMed:12970183"
FT MUTAGEN 225
FT /note="Y->F: Prevents phosphorylation and increases ATPase
FT activity; when associated with F-227 and F-228."
FT /evidence="ECO:0000269|PubMed:12970183"
FT MUTAGEN 227
FT /note="Y->F: Prevents phosphorylation and increases ATPase
FT activity; when associated with F-225 and F-228."
FT /evidence="ECO:0000269|PubMed:12970183"
FT MUTAGEN 228
FT /note="Y->F: Prevents phosphorylation and increases ATPase
FT activity; when associated with F-225 and F-227."
FT /evidence="ECO:0000269|PubMed:12970183"
SQ SEQUENCE 237 AA; 25790 MW; 40BE35B5E3FF97D7 CRC64;
MALRKNRGSR MQRNVIAMTE PKSLNSEQYR TIRTNIEFAS VDRQMKSVMI TSACPGEGKS
TTAANLAVVF AQQGKKVLLI DADLRKPTVH TAFFLENTVG LTSVLLKKSS MEQAVQASNE
KHLDVLTSGP IPPNPAELLS SKWMKELAYE ACAAYDMVIF DTPPILAVAD AQILGNVADG
SVLVISSGKT EKEQAAKAKE ALATCKSKLL GAIMNGKKLS KHSEYGYYGT KDNFMQK
