PTPC1_ECOLI
ID PTPC1_ECOLI Reviewed; 267 AA.
AC P42910; Q2M971;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=N-acetylgalactosamine permease IIC component 1;
DE AltName: Full=EIIC-Aga;
DE AltName: Full=PTS system N-acetylgalactosamine-specific EIIC component 1;
GN Name=agaC; Synonyms=yraE; OrderedLocusNames=b3139, JW3108;
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 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 [3]
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 [4]
RP 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; Multi-pass membrane protein.
CC -!- DOMAIN: The EIIC domain forms the PTS system translocation channel and
CC contains the specific substrate-binding site.
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DR EMBL; U18997; AAA57942.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76173.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77185.1; -; Genomic_DNA.
DR PIR; G65103; G65103.
DR RefSeq; NP_417608.1; NC_000913.3.
DR RefSeq; WP_000544489.1; NZ_STEB01000001.1.
DR AlphaFoldDB; P42910; -.
DR SMR; P42910; -.
DR BioGRID; 4262422; 14.
DR STRING; 511145.b3139; -.
DR PaxDb; P42910; -.
DR PRIDE; P42910; -.
DR EnsemblBacteria; AAC76173; AAC76173; b3139.
DR EnsemblBacteria; BAE77185; BAE77185; BAE77185.
DR GeneID; 66672960; -.
DR GeneID; 947652; -.
DR KEGG; ecj:JW3108; -.
DR KEGG; eco:b3139; -.
DR PATRIC; fig|1411691.4.peg.3591; -.
DR EchoBASE; EB2623; -.
DR eggNOG; COG3715; Bacteria.
DR HOGENOM; CLU_069101_2_1_6; -.
DR OMA; HEITLIQ; -.
DR PhylomeDB; P42910; -.
DR BioCyc; EcoCyc:AGAC-MON; -.
DR PRO; PR:P42910; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
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 TIGRFAMs; TIGR00822; EII-Sor; 1.
DR PROSITE; PS51106; PTS_EIIC_TYPE_4; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Membrane; Phosphotransferase system;
KW Reference proteome; Sugar transport; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..267
FT /note="N-acetylgalactosamine permease IIC component 1"
FT /id="PRO_0000186660"
FT TOPO_DOM 1..10
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00429"
FT TOPO_DOM 32..33
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 34..54
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00429"
FT TOPO_DOM 55..66
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 67..87
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00429"
FT TOPO_DOM 88..94
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 95..115
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00429"
FT TOPO_DOM 116..141
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 142..162
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00429"
FT TOPO_DOM 163..177
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00429"
FT TOPO_DOM 199..209
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 210..230
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00429"
FT TOPO_DOM 231..267
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 1..237
FT /note="PTS EIIC type-4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00429"
SQ SEQUENCE 267 AA; 28645 MW; C44F4D0827FE56C6 CRC64;
MHEITLLQGL SLAALVFVLG IDFWLEALFL FRPIIVCTLT GAILGDIQTG LITGGLTELA
FAGLTPAGGV QPPNPIMAGL MTTVIAWSTG VDAKTAIGLG LPFSLLMQYV ILFFYSAFSL
FMTKADKCAK EADTAAFSRL NWTTMLIVAS AYAVIAFLCT YLAQGAMQAL VKAMPAWLTH
GFEVAGGILP AVGFGLLLRV MFKAQYIPYL IAGFLFVCYI QVSNLLPVAV LGAGFAVYEF
FNAKSRQQAQ PQPVASKNEE EDYSNGI
