PTND_ECO57
ID PTND_ECO57 Reviewed; 286 AA.
AC P69807; P08188;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=PTS system mannose-specific EIID component {ECO:0000250|UniProtKB:P69805};
DE AltName: Full=EII-M-Man {ECO:0000250|UniProtKB:P69805};
DE AltName: Full=EIID-Man {ECO:0000250|UniProtKB:P69805};
DE AltName: Full=Mannose permease IID component {ECO:0000250|UniProtKB:P69805};
GN Name=manZ; OrderedLocusNames=Z2862, ECs2529;
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 ManXYZ PTS system is involved in mannose transport.
CC {ECO:0000250|UniProtKB:P69805}.
CC -!- SUBUNIT: Homotrimer of protomers that are composed of two subunits, IIC
CC and IID. {ECO:0000250|UniProtKB:P69805}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:P69805}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P69805}.
CC -!- DOMAIN: The EIID domain, with its homologous EIIC domain, forms the PTS
CC system translocation channel and contains part of its specific
CC substrate-binding site. {ECO:0000255|PROSITE-ProRule:PRU00431}.
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DR EMBL; AE005174; AAG56808.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB35952.1; -; Genomic_DNA.
DR PIR; A98945; A98945.
DR PIR; D85793; D85793.
DR RefSeq; NP_310556.4; NC_002695.1.
DR AlphaFoldDB; P69807; -.
DR SMR; P69807; -.
DR STRING; 155864.EDL933_2789; -.
DR PRIDE; P69807; -.
DR EnsemblBacteria; AAG56808; AAG56808; Z2862.
DR EnsemblBacteria; BAB35952; BAB35952; ECs_2529.
DR GeneID; 914171; -.
DR KEGG; ece:Z2862; -.
DR KEGG; ecs:ECs_2529; -.
DR PATRIC; fig|386585.9.peg.2649; -.
DR eggNOG; COG3716; Bacteria.
DR HOGENOM; CLU_060742_2_0_6; -.
DR OMA; TLLCMWL; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR InterPro; IPR004704; PTS_IID_man.
DR Pfam; PF03613; EIID-AGA; 1.
DR TIGRFAMs; TIGR00828; EIID-AGA; 1.
DR PROSITE; PS51108; PTS_EIID; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Formylation; Membrane;
KW Phosphotransferase system; Reference proteome; Sugar transport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..286
FT /note="PTS system mannose-specific EIID component"
FT /id="PRO_0000186652"
FT TOPO_DOM 1..17
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P69805"
FT INTRAMEM 18..55
FT /evidence="ECO:0000250|UniProtKB:P69805"
FT TOPO_DOM 56..62
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P69805"
FT INTRAMEM 63..95
FT /evidence="ECO:0000250|UniProtKB:P69805"
FT TOPO_DOM 96..103
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P69805"
FT TRANSMEM 104..143
FT /evidence="ECO:0000250|UniProtKB:P69805"
FT TOPO_DOM 144..147
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:P69805"
FT TRANSMEM 148..176
FT /evidence="ECO:0000250|UniProtKB:P69805"
FT TOPO_DOM 177..186
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P69805"
FT TRANSMEM 187..212
FT /evidence="ECO:0000250|UniProtKB:P69805"
FT TOPO_DOM 213..244
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:P69805"
FT TRANSMEM 245..258
FT /evidence="ECO:0000250|UniProtKB:P69805"
FT TOPO_DOM 259..264
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P69805"
FT TRANSMEM 265..283
FT /evidence="ECO:0000250|UniProtKB:P69805"
FT TOPO_DOM 284..286
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:P69805"
FT DOMAIN 14..284
FT /note="PTS EIID"
FT /evidence="ECO:0000250|UniProtKB:P69805"
FT MOD_RES 1
FT /note="N-formylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P69805"
SQ SEQUENCE 286 AA; 31303 MW; F460050C589B44DF CRC64;
MSEMVDTTQT TTEKKLTQSD IRGVFLRSNL FQGSWNFERM QALGFCFSMV PAIRRLYPEN
NEARKQAIRR HLEFFNTQPF VAAPILGVTL ALEEQRANGA EIDDGAINGI KVGLMGPLAG
VGDPIFWGTV RPVFAALGAG IAMSGSLLGP LLFFILFNLV RLATRYYGVA YGYSKGIDIV
KDMGGGFLQK LTEGASILGL FVMGALVNKW THVNIPLVVS RITDQTGKEH VTTVQTILDQ
LMPGLVPLLL TFACMWLLRK KVNPLWIIVG FFVIGIAGYA CGLLGL
