PTMA_ENTFA
ID PTMA_ENTFA Reviewed; 145 AA.
AC P27547;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-APR-2003, sequence version 2.
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:1904856};
DE AltName: Full=PTS system mannitol-specific EIIA component {ECO:0000250|UniProtKB:P0A0E0};
GN Name=mtlF {ECO:0000303|PubMed:1904856}; OrderedLocusNames=EF_0412;
OS Enterococcus faecalis (strain ATCC 700802 / V583).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=226185;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1904856; DOI=10.1128/jb.173.12.3709-3715.1991;
RA Fischer R., von Strandmann R.P., Hengstenberg W.;
RT "Mannitol-specific phosphoenolpyruvate-dependent phosphotransferase system
RT of Enterococcus faecalis: molecular cloning and nucleotide sequences of the
RT enzyme IIIMtl gene and the mannitol-1-phosphate dehydrogenase gene,
RT expression in Escherichia coli, and comparison of the gene products with
RT similar enzymes.";
RL J. Bacteriol. 173:3709-3715(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700802 / V583;
RX PubMed=12663927; DOI=10.1126/science.1080613;
RA Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
RA Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C.,
RA DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., Nelson W.C.,
RA Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M.,
RA Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT faecalis.";
RL Science 299:2071-2074(2003).
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; M38386; AAA24779.1; -; Genomic_DNA.
DR EMBL; AE016830; AAO80271.1; -; Genomic_DNA.
DR PIR; A39435; WQSO3M.
DR RefSeq; NP_814200.1; NC_004668.1.
DR RefSeq; WP_002355279.1; NZ_KE136524.1.
DR AlphaFoldDB; P27547; -.
DR SMR; P27547; -.
DR STRING; 226185.EF_0412; -.
DR EnsemblBacteria; AAO80271; AAO80271; EF_0412.
DR GeneID; 60892856; -.
DR KEGG; efa:EF0412; -.
DR PATRIC; fig|226185.45.peg.2920; -.
DR eggNOG; COG4668; Bacteria.
DR HOGENOM; CLU_072531_3_0_9; -.
DR OMA; EDYIQAM; -.
DR Proteomes; UP000001415; 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_0000186634"
FT DOMAIN 2..145
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:0000250|UniProtKB:P0A0E0,
FT 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 CONFLICT 25..27
FT /note="CGE -> SGQ (in Ref. 1; AAA24779)"
FT /evidence="ECO:0000305"
FT CONFLICT 52..53
FT /note="VY -> AH (in Ref. 1; AAA24779)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 145 AA; 15947 MW; AD7417F03A191C4C CRC64;
MENLTNISIE LNQQFNTKEE AIRFCGEKLV EAGCVEPAYI EAMIERDQLL SVYMGNFIAI
PHGTEEAKKL VKKSGICVVQ VPEGVNFGTE EDEKIATVLF GIAGVGEEHL QLVQQIALYC
SDMDNVVQLA DALSKEEITE NLAIA