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PTXA_BACSU
ID   PTXA_BACSU              Reviewed;          76 AA.
AC   O32292;
DT   26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Putative phosphotransferase enzyme IIA component YyzE;
DE   AltName: Full=PTS system EIIA component;
GN   Name=yyzE; OrderedLocusNames=BSU40120;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
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   -!- FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase
CC       system (PTS), a major carbohydrate active -transport system, catalyzes
CC       the phosphorylation of incoming sugar substrates concomitant with their
CC       translocation across the cell membrane. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- DOMAIN: The EIIA domain is phosphorylated by phospho-HPr on a histidyl
CC       residue. Then, it transfers the phosphoryl group to the EIIB domain.
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DR   EMBL; AL009126; CAB16049.1; -; Genomic_DNA.
DR   PIR; D70092; D70092.
DR   RefSeq; NP_391892.1; NC_000964.3.
DR   RefSeq; WP_003226990.1; NC_000964.3.
DR   AlphaFoldDB; O32292; -.
DR   SMR; O32292; -.
DR   STRING; 224308.BSU40120; -.
DR   PaxDb; O32292; -.
DR   EnsemblBacteria; CAB16049; CAB16049; BSU_40120.
DR   GeneID; 937724; -.
DR   KEGG; bsu:BSU40120; -.
DR   PATRIC; fig|224308.179.peg.4339; -.
DR   eggNOG; COG2190; Bacteria.
DR   PhylomeDB; O32292; -.
DR   BioCyc; BSUB:BSU40120-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:GO_Central.
DR   GO; GO:0016301; F:kinase activity; IBA:GO_Central.
DR   GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IBA:GO_Central.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 2.70.70.10; -; 1.
DR   InterPro; IPR011055; Dup_hybrid_motif.
DR   InterPro; IPR001127; PTS_EIIA_1_perm.
DR   Pfam; PF00358; PTS_EIIA_1; 1.
DR   SUPFAM; SSF51261; SSF51261; 1.
DR   PROSITE; PS51093; PTS_EIIA_TYPE_1; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Kinase; Phosphotransferase system; Reference proteome;
KW   Sugar transport; Transferase; Transport.
FT   CHAIN           1..76
FT                   /note="Putative phosphotransferase enzyme IIA component
FT                   YyzE"
FT                   /id="PRO_0000376798"
FT   DOMAIN          1..76
FT                   /note="PTS EIIA type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00416"
FT   ACT_SITE        22
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   76 AA;  8242 MW;  392CC402DFB44400 CRC64;
     MVTPTKHAIG LRSASGVELL AHIGLDTVTF DGTPFSLKVK EGDTVKKGEV LVEFDKAFIE
     DIEESALHQK IFTVVS
 
 
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