ID   PTMA_STRMU              Reviewed;         145 AA.
AC   Q02420;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-AUG-2022, entry version 122.
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:0000303|PubMed:1322373};
DE   AltName: Full=PTS system mannitol-specific EIIA component {ECO:0000250|UniProtKB:P0A0E0};
GN   Name=mtlF {ECO:0000303|PubMed:1322373}; Synonyms=mtlA2;
GN   OrderedLocusNames=SMU_1183;
OS   Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=210007;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 700611 / UA130 / Serotype c;
RX   PubMed=1322373; DOI=10.1128/iai.60.8.3369-3375.1992;
RA   Honeyman A.L., Curtiss R. III;
RT   "Isolation, characterization, and nucleotide sequence of the Streptococcus
RT   mutans mannitol-phosphate dehydrogenase gene and the mannitol-specific
RT   factor III gene of the phosphoenolpyruvate phosphotransferase system.";
RL   Infect. Immun. 60:3369-3375(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700610 / UA159;
RX   PubMed=12397186; DOI=10.1073/pnas.172501299;
RA   Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA   Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA   Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT   "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT   pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
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}.
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DR   EMBL; AF210133; AAA26941.1; -; Genomic_DNA.
DR   EMBL; AE014133; AAN58873.1; -; Genomic_DNA.
DR   PIR; B44798; B44798.
DR   RefSeq; NP_721567.1; NC_004350.2.
DR   RefSeq; WP_002262167.1; NC_004350.2.
DR   AlphaFoldDB; Q02420; -.
DR   SMR; Q02420; -.
DR   STRING; 210007.SMU_1183; -.
DR   PRIDE; Q02420; -.
DR   EnsemblBacteria; AAN58873; AAN58873; SMU_1183.
DR   KEGG; smu:SMU_1183; -.
DR   PATRIC; fig|210007.7.peg.1061; -.
DR   eggNOG; COG4668; Bacteria.
DR   HOGENOM; CLU_072531_3_0_9; -.
DR   OMA; EDYIQAM; -.
DR   PhylomeDB; Q02420; -.
DR   Proteomes; UP000002512; 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   Reference proteome; Sugar transport; Transferase; Transport.
FT   CHAIN           1..145
FT                   /note="Mannitol-specific phosphotransferase enzyme IIA
FT                   component"
FT                   /id="PRO_0000186644"
FT   DOMAIN          1..144
FT                   /note="PTS EIIA type-2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00417"
FT   ACT_SITE        61
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P0A0E0,
FT                   ECO:0000255|PROSITE-ProRule:PRU00417"
FT   MOD_RES         61
FT                   /note="Phosphohistidine; by HPr"
FT                   /evidence="ECO:0000250|UniProtKB:P00550,
FT                   ECO:0000250|UniProtKB:P0A0E0"
SQ   SEQUENCE   145 AA;  15878 MW;  684973EEE46409C3 CRC64;
     MEFQKDLIKL NQHFPDKEAA IRFCGQLLAD GGYVEPAYID AMIQRDKELS VYMGNFIAIP
     HGTDDAKKDV LKSGITVVQV PDGVNFGTED DPQVATVLFG IAGIGDEHLQ IIQNISIFCA
     DVDNVVKLAD AQTEDEVVKL LSQVN