PTMA_ECOLI
ID PTMA_ECOLI Reviewed; 147 AA.
AC P69824; P32058; Q2M9Q9;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Mannitol-specific cryptic phosphotransferase enzyme IIA component {ECO:0000303|PubMed:8353127};
DE AltName: Full=EIIA-Mtl {ECO:0000250|UniProtKB:P0A0E0};
DE AltName: Full=EIII-Mtl {ECO:0000250|UniProtKB:P0A0E0};
DE AltName: Full=PTS system mannitol-specific EIIA component {ECO:0000250|UniProtKB:P0A0E0};
GN Name=cmtB; OrderedLocusNames=b2934, JW2901;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=8353127; DOI=10.1016/0304-4165(93)90103-f;
RA Sprenger G.A.;
RT "Two open reading frames adjacent to the Escherichia coli K-12
RT transketolase (tkt) gene show high similarity to the mannitol
RT phosphotransferase system enzymes from Escherichia coli and various Gram-
RT positive bacteria.";
RL Biochim. Biophys. Acta 1158:103-106(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP STRUCTURE BY NMR, ACTIVE SITE, AND PHOSPHORYLATION AT HIS-67.
RX PubMed=17803963; DOI=10.1016/j.bbrc.2007.08.102;
RA Yu C., Li Y., Xia B., Jin C.;
RT "Solution structure of the cryptic mannitol-specific phosphotransferase
RT enzyme IIA CmtB from Escherichia coli.";
RL Biochem. Biophys. Res. Commun. 362:1001-1006(2007).
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; X72677; CAA51228.1; -; Genomic_DNA.
DR EMBL; U28377; AAA69101.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75971.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76997.1; -; Genomic_DNA.
DR PIR; S36122; S36122.
DR RefSeq; NP_417409.1; NC_000913.3.
DR RefSeq; WP_001239650.1; NZ_SSUV01000019.1.
DR PDB; 2OQ3; NMR; -; A=1-147.
DR PDBsum; 2OQ3; -.
DR AlphaFoldDB; P69824; -.
DR BMRB; P69824; -.
DR SMR; P69824; -.
DR BioGRID; 4261871; 15.
DR IntAct; P69824; 2.
DR STRING; 511145.b2934; -.
DR TCDB; 4.A.2.1.24; the pts fructose-mannitol (fru) family.
DR iPTMnet; P69824; -.
DR PaxDb; P69824; -.
DR PRIDE; P69824; -.
DR EnsemblBacteria; AAC75971; AAC75971; b2934.
DR EnsemblBacteria; BAE76997; BAE76997; BAE76997.
DR GeneID; 66673185; -.
DR GeneID; 945125; -.
DR KEGG; ecj:JW2901; -.
DR KEGG; eco:b2934; -.
DR PATRIC; fig|1411691.4.peg.3799; -.
DR EchoBASE; EB1739; -.
DR eggNOG; COG1762; Bacteria.
DR HOGENOM; CLU_072531_2_0_6; -.
DR OMA; VINDRAY; -.
DR PhylomeDB; P69824; -.
DR BioCyc; EcoCyc:CMTB-MON; -.
DR BioCyc; MetaCyc:CMTB-MON; -.
DR EvolutionaryTrace; P69824; -.
DR PRO; PR:P69824; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; 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 1: Evidence at protein level;
KW 3D-structure; 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_0000186681"
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:0000255|PROSITE-ProRule:PRU00417,
FT ECO:0000305|PubMed:17803963"
FT MOD_RES 67
FT /note="Phosphohistidine; by HPr"
FT /evidence="ECO:0000305|PubMed:17803963"
FT HELIX 4..6
FT /evidence="ECO:0007829|PDB:2OQ3"
FT STRAND 12..16
FT /evidence="ECO:0007829|PDB:2OQ3"
FT HELIX 21..27
FT /evidence="ECO:0007829|PDB:2OQ3"
FT HELIX 30..33
FT /evidence="ECO:0007829|PDB:2OQ3"
FT TURN 34..36
FT /evidence="ECO:0007829|PDB:2OQ3"
FT HELIX 40..52
FT /evidence="ECO:0007829|PDB:2OQ3"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:2OQ3"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:2OQ3"
FT STRAND 78..88
FT /evidence="ECO:0007829|PDB:2OQ3"
FT STRAND 97..104
FT /evidence="ECO:0007829|PDB:2OQ3"
FT HELIX 108..122
FT /evidence="ECO:0007829|PDB:2OQ3"
FT HELIX 125..132
FT /evidence="ECO:0007829|PDB:2OQ3"
FT HELIX 137..145
FT /evidence="ECO:0007829|PDB:2OQ3"
SQ SEQUENCE 147 AA; 16046 MW; 4E09A4E6D88D9190 CRC64;
MRLSDYFPES SISVIHSAKD WQEAIDFSMV SLLDKNYISE NYIQAIKDST INNGPYYILA
PGVAMPHARP ECGALKTGMS LTLLEQGVYF PGNDEPIKLL IGLSAADADS HIGAIQALSE
LLCEEEILEQ LLTASSEKQL ADIISRG
