ID   PTMA_GEOSE              Reviewed;         145 AA.
AC   Q45420;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 79.
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:8824601};
DE   AltName: Full=PTS system mannitol-specific EIIA component {ECO:0000250|UniProtKB:P0A0E0};
GN   Name=mtlF {ECO:0000303|PubMed:8824601};
OS   Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=1422;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 29609 / DSM 2027 / NCA 1503 / NCIMB 8924;
RX   PubMed=8824601; DOI=10.1128/jb.178.19.5586-5591.1996;
RA   Henstra S.A., Tolner B., ten Hoeve Duurkens R.H., Konings W.N.,
RA   Robillard G.T.;
RT   "Cloning, expression, and isolation of the mannitol transport protein from
RT   the thermophilic bacterium Bacillus stearothermophilus.";
RL   J. Bacteriol. 178:5586-5591(1996).
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; U18943; AAC44465.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q45420; -.
DR   SMR; Q45420; -.
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   CHAIN           1..145
FT                   /note="Mannitol-specific phosphotransferase enzyme IIA
FT                   component"
FT                   /id="PRO_0000186633"
FT   DOMAIN          4..144
FT                   /note="PTS EIIA type-2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00417"
FT   ACT_SITE        64
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P0A0E0,
FT                   ECO:0000255|PROSITE-ProRule:PRU00417"
FT   MOD_RES         64
FT                   /note="Phosphohistidine; by HPr"
FT                   /evidence="ECO:0000250|UniProtKB:P00550,
FT                   ECO:0000250|UniProtKB:P0A0E0"
SQ   SEQUENCE   145 AA;  16024 MW;  E6488EFE4071FBC4 CRC64;
     MSMPILKKEN IVLHARVENK TEAIRLAGQI LVNNGYVEDS YIDKMFEREA LTSTYMGNFI
     AIPHGTEDAK QFVKHSGISI IQIPDGVDFG DGNIVKLLIG IAGKNNEHLE ILSKIAIVCS
     EVENVETMIK AATEEEILSI LNEVN