PTMA_ECO57
ID PTMA_ECO57 Reviewed; 147 AA.
AC P69825; P32058;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Mannitol-specific cryptic phosphotransferase enzyme IIA component {ECO:0000250|UniProtKB:P69824};
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=cmtB; OrderedLocusNames=Z4278, ECs3809;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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; AE005174; AAG58064.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB37232.1; -; Genomic_DNA.
DR PIR; A98105; A98105.
DR PIR; D85950; D85950.
DR RefSeq; NP_311836.1; NC_002695.1.
DR RefSeq; WP_001239650.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P69825; -.
DR BMRB; P69825; -.
DR SMR; P69825; -.
DR STRING; 155864.EDL933_4142; -.
DR EnsemblBacteria; AAG58064; AAG58064; Z4278.
DR EnsemblBacteria; BAB37232; BAB37232; ECs_3809.
DR GeneID; 66673185; -.
DR GeneID; 916372; -.
DR KEGG; ece:Z4278; -.
DR KEGG; ecs:ECs_3809; -.
DR PATRIC; fig|386585.9.peg.3976; -.
DR eggNOG; COG1762; Bacteria.
DR HOGENOM; CLU_072531_2_0_6; -.
DR OMA; VINDRAY; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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..147
FT /note="Mannitol-specific cryptic phosphotransferase enzyme
FT IIA component"
FT /id="PRO_0000186682"
FT DOMAIN 5..147
FT /note="PTS EIIA type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00417"
FT ACT_SITE 67
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P0A0E0,
FT ECO:0000250|UniProtKB:P69824, ECO:0000255|PROSITE-
FT ProRule:PRU00417"
FT MOD_RES 67
FT /note="Phosphohistidine; by HPr"
FT /evidence="ECO:0000250|UniProtKB:P0A0E0,
FT ECO:0000250|UniProtKB:P69824"
SQ SEQUENCE 147 AA; 16046 MW; 4E09A4E6D88D9190 CRC64;
MRLSDYFPES SISVIHSAKD WQEAIDFSMV SLLDKNYISE NYIQAIKDST INNGPYYILA
PGVAMPHARP ECGALKTGMS LTLLEQGVYF PGNDEPIKLL IGLSAADADS HIGAIQALSE
LLCEEEILEQ LLTASSEKQL ADIISRG