ID   PTPC2_ECOLI             Reviewed;         133 AA.
AC   P42905;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-MAY-2022, entry version 103.
DE   RecName: Full=Putative N-acetylgalactosamine permease IIC component 2;
DE   AltName: Full=EIIC-Aga';
DE   AltName: Full=PTS system N-acetylgalactosamine-specific EIIC component 2;
GN   Name=agaW; OrderedLocusNames=b3134;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
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   [2]
RP   DISCUSSION OF SEQUENCE.
RX   PubMed=8932697; DOI=10.1099/13500872-142-2-231;
RA   Reizer J., Ramseier T.M., Reizer A., Charbit A., Saier M.H. Jr.;
RT   "Novel phosphotransferase genes revealed by bacterial genome sequencing: a
RT   gene cluster encoding a putative N-acetylgalactosamine metabolic pathway in
RT   Escherichia coli.";
RL   Microbiology 142:231-250(1996).
RN   [3]
RP   SUBCELLULAR LOCATION, AND TOPOLOGY [LARGE SCALE ANALYSIS].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=15919996; DOI=10.1126/science.1109730;
RA   Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT   "Global topology analysis of the Escherichia coli inner membrane
RT   proteome.";
RL   Science 308:1321-1323(2005).
CC   -!- FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase
CC       system (PTS), a major carbohydrate active -transport system, catalyzes
CC       the phosphorylation of incoming sugar substrates concomitant with their
CC       translocation across the cell membrane. This system is involved in N-
CC       acetylgalactosamine transport.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein. Note=When
CC       overexpressed using vectors that provide a promoter and ribosome
CC       binding site (PubMed:15919996). {ECO:0000269|PubMed:15919996}.
CC   -!- DOMAIN: The EIIC domain forms the PTS system translocation channel and
CC       contains the specific substrate-binding site.
CC   -!- CAUTION: Could be the product of a pseudogene. {ECO:0000305}.
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DR   EMBL; U18997; AAA57937.1; -; Genomic_DNA.
DR   EMBL; U00096; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; B65103; B65103.
DR   AlphaFoldDB; P42905; -.
DR   SMR; P42905; -.
DR   PRIDE; P42905; -.
DR   PATRIC; fig|1411691.4.peg.3597; -.
DR   EchoBASE; EB2618; -.
DR   PhylomeDB; P42905; -.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IBA:GO_Central.
DR   InterPro; IPR004700; PTS_IIC_man.
DR   Pfam; PF03609; EII-Sor; 1.
DR   PROSITE; PS51106; PTS_EIIC_TYPE_4; 1.
PE   5: Uncertain;
KW   Cell inner membrane; Cell membrane; Membrane; Phosphotransferase system;
KW   Reference proteome; Sugar transport; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..133
FT                   /note="Putative N-acetylgalactosamine permease IIC
FT                   component 2"
FT                   /id="PRO_0000186661"
FT   TOPO_DOM        1..2
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00429"
FT   TOPO_DOM        24..32
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        33..53
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00429"
FT   TOPO_DOM        54..65
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        66..86
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00429"
FT   TOPO_DOM        87..93
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        94..114
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00429"
FT   TOPO_DOM        115..133
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255, ECO:0000269|PubMed:15919996"
FT   DOMAIN          1..133
FT                   /note="PTS EIIC type-4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00429"
SQ   SEQUENCE   133 AA;  13721 MW;  6F45186ABE8D7C38 CRC64;
     MEISLLQAFA LGIIAFIAGL DMFNGLTHMH RPVVLGPLVG LVLGDLHTGI LTGGTLELVW
     MGLAPLAGAQ PPNVIIGTIV GTAFAITTGV KPDVAVGVAV PFAVAVQMGI TFLFSVMSGV
     MSRCDLATNP RRI