ID   PTMA_STAAR              Reviewed;         144 AA.
AC   Q6GER9;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 88.
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; Synonyms=mtlA; OrderedLocusNames=SAR2246;
OS   Staphylococcus aureus (strain MRSA252).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282458;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MRSA252;
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
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   -!- SUBUNIT: Homodimer or homotrimer. Seems to be a monomer when not
CC       phosphorylated. {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}.
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DR   EMBL; BX571856; CAG41227.1; -; Genomic_DNA.
DR   RefSeq; WP_001292150.1; NC_002952.2.
DR   AlphaFoldDB; Q6GER9; -.
DR   SMR; Q6GER9; -.
DR   KEGG; sar:SAR2246; -.
DR   HOGENOM; CLU_072531_3_0_9; -.
DR   OMA; EDYIQAM; -.
DR   OrthoDB; 1810962at2; -.
DR   Proteomes; UP000000596; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00211; PTS_IIA_fru; 1.
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   3: Inferred from homology;
KW   Cytoplasm; Kinase; Phosphoprotein; Phosphotransferase system;
KW   Sugar transport; Transferase; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..144
FT                   /note="Mannitol-specific phosphotransferase enzyme IIA
FT                   component"
FT                   /id="PRO_0000186639"
FT   DOMAIN          3..142
FT                   /note="PTS EIIA type-2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00417"
FT   ACT_SITE        63
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P0A0E0,
FT                   ECO:0000255|PROSITE-ProRule:PRU00417"
FT   MOD_RES         63
FT                   /note="Phosphohistidine; by HPr"
FT                   /evidence="ECO:0000250|UniProtKB:P00550,
FT                   ECO:0000250|UniProtKB:P0A0E0"
SQ   SEQUENCE   144 AA;  15470 MW;  4144851EEBC3A5A9 CRC64;
     MSELFSNDNI FLNVNVNSQN EAIEKAGKAL VDSGAVTDAY IQAMKDREQV VSTFMGNGLA
     IPHGTDEAKT NVIHSGLTLL QIPEGVDWDG EVVKVVVGIA GKDGEHLDLL SKIAITFSEE
     GNVDRIVQAK SAEEIKQVFE EADA