PTXC_ECOLI
ID PTXC_ECOLI Reviewed; 368 AA.
AC P31452; A0A385XJP0; P76731; Q2M7Z5;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Phosphotransferase IIC component GlvC;
DE AltName: Full=PTS system EIIC component;
GN Name=glvC {ECO:0000303|PubMed:8019415}; Synonyms=ptiC;
GN OrderedLocusNames=b3683, JW3660;
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=7686882; DOI=10.1006/geno.1993.1230;
RA Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.;
RT "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome:
RT organizational symmetry around the origin of replication.";
RL Genomics 16:551-561(1993).
RN [2]
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 [3]
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 [4]
RP DISCUSSION OF SEQUENCE.
RX PubMed=8019415; DOI=10.1002/pro.5560030309;
RA Reizer J., Michotey V., Reizer A., Saier M.H. Jr.;
RT "Novel phosphotransferase system genes revealed by bacterial genome
RT analysis: unique, putative fructose- and glucoside-specific systems.";
RL Protein Sci. 3:440-450(1994).
RN [5]
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 operon may be cryptic in
CC wild-type K12 strains (Probable). {ECO:0000250,
CC ECO:0000305|PubMed:8019415}.
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 -!- MISCELLANEOUS: Is shorter than orthologs at the C-terminus by about 170
CC amino acids. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA62035.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305|PubMed:8019415};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L10328; AAA62035.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AYC08253.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77611.1; -; Genomic_DNA.
DR PIR; D65170; D65170.
DR RefSeq; WP_000952140.1; NZ_CP047127.1.
DR AlphaFoldDB; P31452; -.
DR SMR; P31452; -.
DR BioGRID; 4260807; 9.
DR STRING; 316407.85676361; -.
DR PRIDE; P31452; -.
DR EnsemblBacteria; AYC08253; AYC08253; b3683.
DR EnsemblBacteria; BAE77611; BAE77611; BAE77611.
DR KEGG; ecj:JW3660; -.
DR PATRIC; fig|83333.103.peg.4618; -.
DR EchoBASE; EB1661; -.
DR eggNOG; COG1263; Bacteria.
DR HOGENOM; CLU_012312_1_0_6; -.
DR InParanoid; P31452; -.
DR PhylomeDB; P31452; -.
DR BioCyc; EcoCyc:GLVC-MON; -.
DR PRO; PR:P31452; -.
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:0008982; F:protein-N(PI)-phosphohistidine-sugar phosphotransferase activity; IEA:InterPro.
DR GO; GO:0090563; F:protein-phosphocysteine-sugar phosphotransferase activity; IBA:GO_Central.
DR GO; GO:0008643; P:carbohydrate transport; TAS:EcoliWiki.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IBA:GO_Central.
DR InterPro; IPR003352; PTS_EIIC.
DR InterPro; IPR013013; PTS_EIIC_1.
DR InterPro; IPR010975; PTS_IIBC_a_glc.
DR InterPro; IPR004719; PTS_maltose/Glc_sub_IIC.
DR Pfam; PF02378; PTS_EIIC; 1.
DR TIGRFAMs; TIGR00852; pts-Glc; 1.
DR TIGRFAMs; TIGR02005; PTS-IIBC-alpha; 1.
DR PROSITE; PS51103; PTS_EIIC_TYPE_1; 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..368
FT /note="Phosphotransferase IIC component GlvC"
FT /id="PRO_0000186579"
FT TOPO_DOM 1..11
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TOPO_DOM 33..59
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TOPO_DOM 81..86
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TOPO_DOM 108..129
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 130..150
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TOPO_DOM 151..173
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TOPO_DOM 195..198
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 199..221
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TOPO_DOM 222..224
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 225..245
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TOPO_DOM 246..276
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 277..297
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TOPO_DOM 298..306
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 307..327
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TOPO_DOM 328
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 329..349
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TOPO_DOM 350..368
FT /note="Periplasmic"
FT /evidence="ECO:0000255, ECO:0000269|PubMed:15919996"
FT DOMAIN 1..368
FT /note="PTS EIIC type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
SQ SEQUENCE 368 AA; 39692 MW; D6E858D618D3EB90 CRC64;
MLSQIQRFGG AMFTPVLLFP FAGIVVGLAI LLQNPMFVGE SLTDPNSLFA QIVHIIEEGG
WTVFRNMPLI FAVGLPIGLA KQAQGRACLA VMVSFLTWNY FINAMGMTWG SYFGVDFTQD
AVAGSGLTMM AGIKTLDTSI IGAIIISGIV TALHNRLFDK KLPVFLGIFQ GTSYVVIIAF
LVMIPCAWLT LLGWPKVQMG IESLQAFLRS AGALGVWVYT FLERILIPTG LHHFIYGQFI
FGPAAVEGGI QMYWAQHLQE FSLSAEPLKS LFPEGGFALH GNSKIFGAVG ISLAMYFTAA
PENRVKVAGL LIPATLTAML VGITEPLEFT FLFISPLLFA VHAVLAASMS TVMYLFGVVG
NMGGGLID
