PTND_ECOLI
ID PTND_ECOLI Reviewed; 283 AA.
AC P69805; P08188;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=PTS system mannose-specific EIID component {ECO:0000303|PubMed:2999119};
DE AltName: Full=EII-M-Man {ECO:0000303|PubMed:2951378};
DE AltName: Full=EIID-Man {ECO:0000303|PubMed:2999119};
DE AltName: Full=Mannose permease IID component {ECO:0000303|PubMed:2999119};
GN Name=manZ; Synonyms=gptB, ptsM; OrderedLocusNames=b1819, JW1808;
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 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 [6]
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 [7]
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 [8]
RP TOPOLOGY.
RA Huber F., Erni B.;
RT "Topology of the Escherichia coli mannose transporter.";
RL Protein Sci. 4 Suppl. 1:111-111(1995).
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, AND TOPOLOGY.
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:0000269|PubMed:15919996,
CC ECO:0000269|PubMed:31209249, ECO:0000269|PubMed:8774730}; Multi-pass
CC membrane protein {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 EIID domain, with its homologous EIIC domain, forms the PTS
CC system translocation channel and contains part of its specific
CC substrate-binding site. {ECO:0000255|PROSITE-ProRule:PRU00431}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA24445.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA15631.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; J02699; AAA24445.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC74889.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA15631.1; ALT_INIT; Genomic_DNA.
DR PIR; A30288; WQECMM.
DR RefSeq; NP_416333.4; NC_000913.3.
DR RefSeq; WP_000228655.1; NZ_STEB01000009.1.
DR PDB; 6K1H; EM; 3.52 A; C/F/Z=1-283.
DR PDB; 7DYR; EM; 2.28 A; C/F/Z=1-283.
DR PDBsum; 6K1H; -.
DR PDBsum; 7DYR; -.
DR AlphaFoldDB; P69805; -.
DR SMR; P69805; -.
DR BioGRID; 4259146; 324.
DR ComplexPortal; CPX-5968; D-mannose-specific enzyme II complex.
DR IntAct; P69805; 1.
DR STRING; 511145.b1819; -.
DR TCDB; 4.A.6.1.1; the pts mannose-fructose-sorbose (man) family.
DR jPOST; P69805; -.
DR PaxDb; P69805; -.
DR PRIDE; P69805; -.
DR EnsemblBacteria; AAC74889; AAC74889; b1819.
DR EnsemblBacteria; BAA15631; BAA15631; BAA15631.
DR GeneID; 66674292; -.
DR GeneID; 946342; -.
DR KEGG; ecj:JW1808; -.
DR KEGG; eco:b1819; -.
DR PATRIC; fig|511145.12.peg.1896; -.
DR EchoBASE; EB0564; -.
DR eggNOG; COG3716; Bacteria.
DR HOGENOM; CLU_060742_2_0_6; -.
DR InParanoid; P69805; -.
DR PhylomeDB; P69805; -.
DR BioCyc; EcoCyc:MANZ-MON; -.
DR BioCyc; MetaCyc:MANZ-MON; -.
DR PRO; PR:P69805; -.
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; IPR004704; PTS_IID_man.
DR Pfam; PF03613; EIID-AGA; 1.
DR TIGRFAMs; TIGR00828; EIID-AGA; 1.
DR PROSITE; PS51108; PTS_EIID; 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..283
FT /note="PTS system mannose-specific EIID component"
FT /id="PRO_0000186650"
FT TOPO_DOM 1..14
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:31209249,
FT ECO:0000305|PubMed:32710850, ECO:0000305|PubMed:7811395"
FT INTRAMEM 15..52
FT /evidence="ECO:0000305|PubMed:32710850"
FT TOPO_DOM 53..59
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:32710850"
FT INTRAMEM 60..92
FT /evidence="ECO:0000305|PubMed:32710850"
FT TOPO_DOM 93..100
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:32710850"
FT TRANSMEM 101..140
FT /evidence="ECO:0000305|PubMed:32710850"
FT TOPO_DOM 141..144
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:32710850"
FT TRANSMEM 145..173
FT /evidence="ECO:0000305|PubMed:32710850"
FT TOPO_DOM 174..183
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:32710850"
FT TRANSMEM 184..209
FT /evidence="ECO:0000305|PubMed:32710850"
FT TOPO_DOM 210..241
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:32710850"
FT TRANSMEM 242..255
FT /evidence="ECO:0000305|PubMed:32710850"
FT TOPO_DOM 256..261
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:32710850"
FT TRANSMEM 262..280
FT /evidence="ECO:0000305|PubMed:32710850"
FT TOPO_DOM 281..283
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:15919996,
FT ECO:0000269|PubMed:31209249, ECO:0000269|PubMed:8774730,
FT ECO:0000305|PubMed:32710850"
FT DOMAIN 11..281
FT /note="PTS EIID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00431"
FT MOD_RES 1
FT /note="N-formylmethionine"
FT /evidence="ECO:0000305|PubMed:2951378"
FT HELIX 16..24
FT /evidence="ECO:0007829|PDB:7DYR"
FT HELIX 25..27
FT /evidence="ECO:0007829|PDB:7DYR"
FT STRAND 28..31
FT /evidence="ECO:0007829|PDB:7DYR"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:7DYR"
FT HELIX 39..45
FT /evidence="ECO:0007829|PDB:7DYR"
FT HELIX 47..53
FT /evidence="ECO:0007829|PDB:7DYR"
FT HELIX 60..68
FT /evidence="ECO:0007829|PDB:7DYR"
FT HELIX 80..95
FT /evidence="ECO:0007829|PDB:7DYR"
FT TURN 100..102
FT /evidence="ECO:0007829|PDB:7DYR"
FT HELIX 104..123
FT /evidence="ECO:0007829|PDB:7DYR"
FT TURN 124..126
FT /evidence="ECO:0007829|PDB:7DYR"
FT HELIX 127..141
FT /evidence="ECO:0007829|PDB:7DYR"
FT HELIX 145..176
FT /evidence="ECO:0007829|PDB:7DYR"
FT HELIX 177..179
FT /evidence="ECO:0007829|PDB:7DYR"
FT HELIX 184..207
FT /evidence="ECO:0007829|PDB:7DYR"
FT STRAND 215..218
FT /evidence="ECO:0007829|PDB:7DYR"
FT TURN 222..224
FT /evidence="ECO:0007829|PDB:7DYR"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:7DYR"
FT HELIX 231..238
FT /evidence="ECO:0007829|PDB:7DYR"
FT HELIX 242..256
FT /evidence="ECO:0007829|PDB:7DYR"
FT HELIX 261..277
FT /evidence="ECO:0007829|PDB:7DYR"
SQ SEQUENCE 283 AA; 30955 MW; E29ED1D7040AE67D CRC64;
MVDTTQTTTE KKLTQSDIRG VFLRSNLFQG SWNFERMQAL GFCFSMVPAI RRLYPENNEA
RKQAIRRHLE FFNTQPFVAA PILGVTLALE EQRANGAEID DGAINGIKVG LMGPLAGVGD
PIFWGTVRPV FAALGAGIAM SGSLLGPLLF FILFNLVRLA TRYYGVAYGY SKGIDIVKDM
GGGFLQKLTE GASILGLFVM GALVNKWTHV NIPLVVSRIT DQTGKEHVTT VQTILDQLMP
GLVPLLLTFA CMWLLRKKVN PLWIIVGFFV IGIAGYACGL LGL
