ID   PTNC_ECOL6              Reviewed;         266 AA.
AC   P69802; P08187; Q47351;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1988, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=PTS system mannose-specific EIIC component {ECO:0000250|UniProtKB:P69801};
DE   AltName: Full=EII-P-Man {ECO:0000250|UniProtKB:P69801};
DE   AltName: Full=EIIC-Man {ECO:0000250|UniProtKB:P69801};
DE   AltName: Full=Mannose permease IIC component {ECO:0000250|UniProtKB:P69801};
GN   Name=manY; OrderedLocusNames=c2224;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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:P69801}.
CC   -!- SUBUNIT: Homotrimer of protomers that are composed of two subunits, IIC
CC       and IID. {ECO:0000250|UniProtKB:P69801}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|PROSITE-
CC       ProRule:PRU00429}; Multi-pass membrane protein {ECO:0000255|PROSITE-
CC       ProRule:PRU00429}.
CC   -!- DOMAIN: The PTS EIIC type-4 domain forms the PTS system translocation
CC       channel and contains the specific substrate-binding site.
CC       {ECO:0000255|PROSITE-ProRule:PRU00429}.
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DR   EMBL; AE014075; AAN80683.1; -; Genomic_DNA.
DR   RefSeq; WP_000406926.1; NC_004431.1.
DR   AlphaFoldDB; P69802; -.
DR   SMR; P69802; -.
DR   STRING; 199310.c2224; -.
DR   PRIDE; P69802; -.
DR   EnsemblBacteria; AAN80683; AAN80683; c2224.
DR   GeneID; 66674293; -.
DR   KEGG; ecc:c2224; -.
DR   eggNOG; COG3715; Bacteria.
DR   HOGENOM; CLU_069101_0_0_6; -.
DR   OMA; LSWIHVS; -.
DR   BioCyc; ECOL199310:C2224-MON; -.
DR   Proteomes; UP000001410; 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; IPR004700; PTS_IIC_man.
DR   Pfam; PF03609; EII-Sor; 1.
DR   TIGRFAMs; TIGR00822; EII-Sor; 1.
DR   PROSITE; PS51106; PTS_EIIC_TYPE_4; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Formylation; Membrane;
KW   Phosphotransferase system; Sugar transport; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..266
FT                   /note="PTS system mannose-specific EIIC component"
FT                   /id="PRO_0000186647"
FT   TOPO_DOM        1..4
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P69801"
FT   INTRAMEM        5..43
FT                   /evidence="ECO:0000250|UniProtKB:P69801"
FT   TOPO_DOM        44..46
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P69801"
FT   INTRAMEM        47..86
FT                   /evidence="ECO:0000250|UniProtKB:P69801"
FT   TOPO_DOM        87..90
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P69801"
FT   TRANSMEM        91..124
FT                   /evidence="ECO:0000250|UniProtKB:P69801"
FT   TOPO_DOM        125..132
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P69801"
FT   TRANSMEM        133..160
FT                   /evidence="ECO:0000250|UniProtKB:P69801"
FT   TOPO_DOM        161..176
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P69801"
FT   TRANSMEM        177..200
FT                   /evidence="ECO:0000250|UniProtKB:P69801"
FT   TOPO_DOM        201..207
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P69801"
FT   TRANSMEM        208..218
FT                   /evidence="ECO:0000250|UniProtKB:P69801"
FT   TOPO_DOM        219..224
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P69801"
FT   TRANSMEM        225..242
FT                   /evidence="ECO:0000250|UniProtKB:P69801"
FT   TOPO_DOM        243..266
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P69801"
FT   DOMAIN          1..237
FT                   /note="PTS EIIC type-4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00429"
FT   MOD_RES         1
FT                   /note="N-formylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:P69801"
SQ   SEQUENCE   266 AA;  27636 MW;  EAFDD9E4B809AF23 CRC64;
     MEITTLQIVL VFIVACIAGM GSILDEFQFH RPLIACTLVG IVLGDMKTGI IIGGTLEMIA
     LGWMNIGAAV APDAALASII STILVIAGHQ SIGAGIALAI PLAAAGQVLT IIVRTITVAF
     QHAADKAADN GNLTAISWIH VSSLFLQAMR VAIPAVIVAL SVGTSEVQNM LNAIPEVVTN
     GLNIAGGMIV VVGYAMVINM MRAGYLMPFF YLGFVTAAFT NFNLVALGVI GTVMAVLYIQ
     LSPKYNRVAG APAQAAGNND LDNELD