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 28-JUN-2023, entry version 108.
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; Pseudomonadota; 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 PATRIC; fig|1411691.4.peg.3597; -.
DR EchoBASE; EB2618; -.
DR InParanoid; P42905; -.
DR PhylomeDB; P42905; -.
DR Proteomes; UP000000625; Chromosome.
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 PANTHER; PTHR32502; N-ACETYLGALACTOSAMINE PERMEASE II COMPONENT-RELATED; 1.
DR PANTHER; PTHR32502:SF8; N-ACETYLGALACTOSAMINE PERMEASE IIC COMPONENT 1; 1.
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
//
