PTNC_ECOLI
ID PTNC_ECOLI Reviewed; 266 AA.
AC P69801; P08187; Q47351;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=PTS system mannose-specific EIIC component {ECO:0000303|PubMed:2999119};
DE AltName: Full=EII-P-Man {ECO:0000303|PubMed:2951378};
DE AltName: Full=EIIC-Man {ECO:0000303|PubMed:2999119};
DE AltName: Full=Mannose permease IIC component {ECO:0000303|PubMed:2999119};
GN Name=manY; Synonyms=pel, ptsP; OrderedLocusNames=b1818, JW1807;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND FORMYLATION AT MET-1.
RX PubMed=2951378; DOI=10.1016/s0021-9258(18)61180-9;
RA Erni B., Zanolari B., Kocher H.P.;
RT "The mannose permease of Escherichia coli consists of three different
RT proteins. Amino acid sequence and function in sugar transport, sugar
RT phosphorylation, and penetration of phage lambda DNA.";
RL J. Biol. Chem. 262:5238-5247(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-40.
RC STRAIN=K12;
RA Saris P.E.J., Liljestroem P., Palva E.T.;
RT "Nucleotide sequence of manX(ptsL) encoding the enzyme III(Man) (II-A(Man))
RT function in the phosphotransferase system of Escherichia coli K-12.";
RL FEMS Microbiol. Lett. 49:69-73(1988).
RN [6]
RP FUNCTION.
RX PubMed=4604906; DOI=10.1073/pnas.71.7.2895;
RA Adler J., Epstein W.;
RT "Phosphotransferase-system enzymes as chemoreceptors for certain sugars in
RT Escherichia coli chemotaxis.";
RL Proc. Natl. Acad. Sci. U.S.A. 71:2895-2899(1974).
RN [7]
RP FUNCTION.
RX PubMed=353494; DOI=10.1007/bf00266608;
RA Elliott J., Arber W.;
RT "E. coli K-12 pel mutants, which block phage lambda DNA injection, coincide
RT with ptsM, which determines a component of a sugar transport system.";
RL Mol. Gen. Genet. 161:1-8(1978).
RN [8]
RP FUNCTION.
RX PubMed=2999119; DOI=10.1016/s0021-9258(17)36282-8;
RA Erni B., Zanolari B.;
RT "The mannose-permease of the bacterial phosphotransferase system. Gene
RT cloning and purification of the enzyme IIMan/IIIMan complex of Escherichia
RT coli.";
RL J. Biol. Chem. 260:15495-15503(1985).
RN [9]
RP TOPOLOGY, AND SUBCELLULAR LOCATION.
RX PubMed=8774730; DOI=10.1111/j.1432-1033.1996.0810u.x;
RA Huber F., Erni B.;
RT "Membrane topology of the mannose transporter of Escherichia coli K12.";
RL Eur. J. Biochem. 239:810-817(1996).
RN [10]
RP TOPOLOGY.
RX PubMed=7811395; DOI=10.1515/bchm3.1994.375.8.551;
RA Rhiel E., Flukiger K., Wehrli C., Erni B.;
RT "The mannose transporter of Escherichia coli K12: oligomeric structure, and
RT function of two conserved cysteines.";
RL Biol. Chem. Hoppe-Seyler 375:551-559(1994).
RN [11]
RP INDUCTION.
RX PubMed=11361067;
RA Plumbridge J.;
RT "Regulation of PTS gene expression by the homologous transcriptional
RT regulators, Mlc and NagC, in Escherichia coli (or how two similar
RT repressors can behave differently).";
RL J. Mol. Microbiol. Biotechnol. 3:371-380(2001).
RN [12]
RP TOPOLOGY [LARGE SCALE ANALYSIS], AND SUBCELLULAR LOCATION.
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).
RN [13]
RP REVIEW, AND TOPOLOGY.
RX PubMed=32710850; DOI=10.1016/j.bbamem.2020.183412;
RA Jeckelmann J.M., Erni B.;
RT "The mannose phosphotransferase system (Man-PTS) - Mannose transporter and
RT receptor for bacteriocins and bacteriophages.";
RL Biochim. Biophys. Acta 1862:183412-183412(2020).
RN [14] {ECO:0007744|PDB:6K1H}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.52 ANGSTROMS), SUBUNIT, SUBCELLULAR
RP LOCATION, TOPOLOGY, AND MUTAGENESIS OF ASN-65.
RX PubMed=31209249; DOI=10.1038/s41422-019-0194-z;
RA Liu X., Zeng J., Huang K., Wang J.;
RT "Structure of the mannose transporter of the bacterial phosphotransferase
RT system.";
RL Cell Res. 29:680-682(2019).
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:0000269|PubMed:2951378, ECO:0000269|PubMed:2999119}.
CC -!- FUNCTION: Also functions as a receptor for bacterial chemotaxis and is
CC required for infection of the cell by bacteriophage lambda where it
CC most likely functions as a pore for penetration of lambda DNA.
CC {ECO:0000269|PubMed:353494, ECO:0000269|PubMed:4604906}.
CC -!- SUBUNIT: Homotrimer of protomers that are composed of two subunits, IIC
CC and IID. {ECO:0000269|PubMed:31209249}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00429, ECO:0000269|PubMed:15919996,
CC ECO:0000269|PubMed:31209249, ECO:0000269|PubMed:8774730}; Multi-pass
CC membrane protein {ECO:0000255|PROSITE-ProRule:PRU00429,
CC ECO:0000269|PubMed:31209249}.
CC -!- INDUCTION: Transcriptionally regulated by the Mlc transcriptional
CC repressor and by the cAMP-CRP complex. Also weakly repressed by NagC.
CC {ECO:0000269|PubMed:11361067}.
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; J02699; AAA24444.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74888.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15625.1; -; Genomic_DNA.
DR EMBL; M36404; AAA24111.1; ALT_TERM; Genomic_DNA.
DR PIR; A30285; WQECMP.
DR RefSeq; NP_416332.1; NC_000913.3.
DR RefSeq; WP_000406926.1; NZ_STEB01000009.1.
DR PDB; 6K1H; EM; 3.52 A; B/E/Y=1-266.
DR PDB; 7DYR; EM; 2.28 A; B/E/Y=1-266.
DR PDBsum; 6K1H; -.
DR PDBsum; 7DYR; -.
DR AlphaFoldDB; P69801; -.
DR SMR; P69801; -.
DR BioGRID; 4259145; 502.
DR ComplexPortal; CPX-5968; D-mannose-specific enzyme II complex.
DR IntAct; P69801; 1.
DR STRING; 511145.b1818; -.
DR TCDB; 4.A.6.1.1; the pts mannose-fructose-sorbose (man) family.
DR jPOST; P69801; -.
DR PaxDb; P69801; -.
DR PRIDE; P69801; -.
DR EnsemblBacteria; AAC74888; AAC74888; b1818.
DR EnsemblBacteria; BAA15625; BAA15625; BAA15625.
DR GeneID; 66674293; -.
DR GeneID; 946332; -.
DR KEGG; ecj:JW1807; -.
DR KEGG; eco:b1818; -.
DR PATRIC; fig|1411691.4.peg.433; -.
DR EchoBASE; EB0563; -.
DR eggNOG; COG3715; Bacteria.
DR HOGENOM; CLU_069101_0_0_6; -.
DR InParanoid; P69801; -.
DR OMA; LSWIHVS; -.
DR PhylomeDB; P69801; -.
DR BioCyc; EcoCyc:MANY-MON; -.
DR BioCyc; MetaCyc:MANY-MON; -.
DR PRO; PR:P69801; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:1902495; C:transmembrane transporter complex; IPI:ComplexPortal.
DR GO; GO:0022870; F:protein-N(PI)-phosphohistidine-mannose phosphotransferase system transporter activity; IDA:EcoCyc.
DR GO; GO:0098708; P:glucose import across plasma membrane; IDA:EcoCyc.
DR GO; GO:0015761; P:mannose transmembrane transport; IDA:EcoCyc.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IDA:ComplexPortal.
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 3D-structure; Cell inner membrane; Cell membrane; Formylation; Membrane;
KW Phosphotransferase system; Reference proteome; Sugar transport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..266
FT /note="PTS system mannose-specific EIIC component"
FT /id="PRO_0000186646"
FT TOPO_DOM 1..4
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:31209249,
FT ECO:0000305|PubMed:32710850"
FT INTRAMEM 5..43
FT /evidence="ECO:0000305|PubMed:32710850"
FT TOPO_DOM 44..46
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:32710850"
FT INTRAMEM 47..86
FT /evidence="ECO:0000305|PubMed:32710850"
FT TOPO_DOM 87..90
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:32710850"
FT TRANSMEM 91..124
FT /evidence="ECO:0000305|PubMed:32710850"
FT TOPO_DOM 125..132
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:32710850"
FT TRANSMEM 133..160
FT /evidence="ECO:0000305|PubMed:32710850"
FT TOPO_DOM 161..176
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:32710850"
FT TRANSMEM 177..200
FT /evidence="ECO:0000305|PubMed:32710850"
FT TOPO_DOM 201..207
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:32710850"
FT TRANSMEM 208..218
FT /evidence="ECO:0000305|PubMed:32710850"
FT TOPO_DOM 219..224
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:32710850"
FT TRANSMEM 225..242
FT /evidence="ECO:0000305|PubMed:32710850"
FT TOPO_DOM 243..266
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15919996,
FT ECO:0000269|PubMed:31209249, ECO:0000269|PubMed:8774730,
FT ECO:0000305|PubMed:32710850, ECO:0000305|PubMed:7811395"
FT DOMAIN 3..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:0000305|PubMed:2951378"
FT MUTAGEN 65
FT /note="N->P: Significantly impairs the mannose transport
FT capacity."
FT /evidence="ECO:0000269|PubMed:31209249"
FT HELIX 5..24
FT /evidence="ECO:0007829|PDB:7DYR"
FT HELIX 32..43
FT /evidence="ECO:0007829|PDB:7DYR"
FT HELIX 46..60
FT /evidence="ECO:0007829|PDB:7DYR"
FT HELIX 74..86
FT /evidence="ECO:0007829|PDB:7DYR"
FT TURN 87..89
FT /evidence="ECO:0007829|PDB:7DYR"
FT HELIX 92..97
FT /evidence="ECO:0007829|PDB:7DYR"
FT HELIX 99..116
FT /evidence="ECO:0007829|PDB:7DYR"
FT HELIX 118..128
FT /evidence="ECO:0007829|PDB:7DYR"
FT TURN 129..131
FT /evidence="ECO:0007829|PDB:7DYR"
FT HELIX 133..142
FT /evidence="ECO:0007829|PDB:7DYR"
FT HELIX 144..160
FT /evidence="ECO:0007829|PDB:7DYR"
FT TURN 161..163
FT /evidence="ECO:0007829|PDB:7DYR"
FT HELIX 166..170
FT /evidence="ECO:0007829|PDB:7DYR"
FT HELIX 177..201
FT /evidence="ECO:0007829|PDB:7DYR"
FT TURN 205..207
FT /evidence="ECO:0007829|PDB:7DYR"
FT HELIX 208..219
FT /evidence="ECO:0007829|PDB:7DYR"
FT HELIX 224..240
FT /evidence="ECO:0007829|PDB:7DYR"
FT TURN 243..245
FT /evidence="ECO:0007829|PDB:7DYR"
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
