(data stored in ACNUC7421 zone)

SWISSPROT: PTMA_BACSU

ID   PTMA_BACSU              Reviewed;         143 AA.
AC   C0H3V2;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   11-DEC-2019, entry version 59.
DE   RecName: Full=Mannitol-specific phosphotransferase enzyme IIA component {ECO:0000250|UniProtKB:P0A0E0};
DE   AltName: Full=EIIA {ECO:0000250|UniProtKB:P0A0E0};
DE   AltName: Full=EIII {ECO:0000250|UniProtKB:P0A0E0};
DE   AltName: Full=PTS system mannitol-specific EIIA component {ECO:0000250|UniProtKB:P0A0E0};
GN   Name=mtlF; OrderedLocusNames=BSU03982; ORFNames=BSU03980;
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).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RC   STRAIN=168;
RX   PubMed=17218307; DOI=10.1074/mcp.m600464-mcp200;
RA   Macek B., Mijakovic I., Olsen J.V., Gnad F., Kumar C., Jensen P.R.,
RA   Mann M.;
RT   "The serine/threonine/tyrosine phosphoproteome of the model bacterium
RT   Bacillus subtilis.";
RL   Mol. Cell. Proteomics 6:697-707(2007).
CC   -!- FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase
CC       system (sugar PTS), a major carbohydrate active transport system,
CC       catalyzes the phosphorylation of incoming sugar substrates
CC       concomitantly with their translocation across the cell membrane. The
CC       enzyme II CmtAB PTS system is involved in D-mannitol transport.
CC       {ECO:0000250|UniProtKB:P0A0E0}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- DOMAIN: The PTS EIIA type-2 domain is phosphorylated by phospho-HPr on
CC       a histidyl residue. Then, it transfers the phosphoryl group to the PTS
CC       EIIB type-2 domain. {ECO:0000255|PROSITE-ProRule:PRU00417}.
DR   EMBL; AL009126; CAX52549.1; -; Genomic_DNA.
DR   RefSeq; WP_003246714.1; NZ_JNCM01000031.1.
DR   RefSeq; YP_003097678.1; NC_000964.3.
DR   SMR; C0H3V2; -.
DR   STRING; 224308.BSU03982; -.
DR   TCDB; 4.A.2.1.5; the pts fructose-mannitol (fru) family.
DR   iPTMnet; C0H3V2; -.
DR   jPOST; C0H3V2; -.
DR   PaxDb; C0H3V2; -.
DR   PRIDE; C0H3V2; -.
DR   EnsemblBacteria; CAX52549; CAX52549; BSU03982.
DR   GeneID; 8303136; -.
DR   KEGG; bsu:BSU03982; -.
DR   PATRIC; fig|224308.179.peg.422; -.
DR   eggNOG; COG2213; LUCA.
DR   eggNOG; COG4668; LUCA.
DR   HOGENOM; HOG000227563; -.
DR   KO; K02798; -.
DR   OMA; HGVSEYV; -.
DR   PhylomeDB; C0H3V2; -.
DR   BioCyc; BSUB:BSU03982-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IBA:GO_Central.
DR   Gene3D; 3.40.930.10; -; 1.
DR   InterPro; IPR016152; PTrfase/Anion_transptr.
DR   InterPro; IPR002178; PTS_EIIA_type-2_dom.
DR   Pfam; PF00359; PTS_EIIA_2; 1.
DR   SUPFAM; SSF55804; SSF55804; 1.
DR   PROSITE; PS51094; PTS_EIIA_TYPE_2; 1.
DR   PROSITE; PS00372; PTS_EIIA_TYPE_2_HIS; 1.
PE   1: Evidence at protein level;
DR   PRODOM; C0H3V2.
DR   SWISS-2DPAGE; C0H3V2.
KW   Cytoplasm; Kinase; Phosphoprotein; Phosphotransferase system;
KW   Reference proteome; Sugar transport; Transferase; Transport.
FT   CHAIN           1..143
FT                   /note="Mannitol-specific phosphotransferase enzyme IIA
FT                   component"
FT                   /id="PRO_0000376996"
FT   DOMAIN          2..142
FT                   /note="PTS EIIA type-2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00417"
FT   ACT_SITE        62
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00417"
FT   MOD_RES         62
FT                   /note="Phosphohistidine; by HPr"
FT                   /evidence="ECO:0000250|UniProtKB:P00550,
FT                   ECO:0000250|UniProtKB:P0A0E0"
FT   MOD_RES         74
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:17218307"
SQ   SEQUENCE   143 AA;  15747 MW;  A107403396C2548C CRC64;
     MQVLAKENIK LNQTVSSKEE AIKLAGQTLI DNGYVTEDYI SKMFEREETS STFMGNFIAI
     PHGTEEAKSE VLHSGISIIQ IPEGVEYGEG NTAKVVFGIA GKNNEHLDIL SNIAIICSEE
     ENIERLISAK SEEDLIAIFN EVN
//

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