METI_ECOLI
ID METI_ECOLI Reviewed; 217 AA.
AC P31547;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=D-methionine transport system permease protein MetI;
GN Name=metI; Synonyms=yaeE; OrderedLocusNames=b0198, JW0194;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RA Miyamoto K.;
RL Submitted (APR-1993) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Takemoto K., Mori H., Murayama N., Kataoka K., Yano M., Itoh T.,
RA Yamamoto Y., Inokuchi H., Miki T., Hatada E., Fukuda R., Ichihara S.,
RA Mizuno T., Makino K., Nakata A., Yura T., Sampei G., Mizobuchi K.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 4.0
RT - 6.0 min (189,987 - 281,416bp) region.";
RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
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 [6]
RP FUNCTION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=12169620; DOI=10.1128/jb.184.17.4930-4932.2002;
RA Gal J., Szvetnik A., Schnell R., Kalman M.;
RT "The metD D-methionine transporter locus of Escherichia coli is an ABC
RT transporter gene cluster.";
RL J. Bacteriol. 184:4930-4932(2002).
RN [7]
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 [8]
RP RECEPTOR FOR CDI TOXIN ENTRY INTO TARGET CELL CYTOPLASM (MICROBIAL
RP INFECTION), AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=26305955; DOI=10.1073/pnas.1512124112;
RA Willett J.L., Gucinski G.C., Fatherree J.P., Low D.A., Hayes C.S.;
RT "Contact-dependent growth inhibition toxins exploit multiple independent
RT cell-entry pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:11341-11346(2015).
CC -!- FUNCTION: Part of the binding-protein-dependent transport system for D-
CC methionine and the toxic methionine analog alpha-methyl-methionine.
CC Probably responsible for the translocation of the substrate across the
CC membrane. {ECO:0000269|PubMed:12169620}.
CC -!- FUNCTION: (Microbial infection) Probably transports the toxic C-
CC terminal region of CdiA from E.coli strain MHI813 across the inner
CC membrane to the cytoplasm, where CdiA has a toxic effect. Toxin
CC transport is strain-specific, mutations in this gene do not confer
CC resistance to several other tested CdiA toxins.
CC {ECO:0000269|PubMed:26305955}.
CC -!- INTERACTION:
CC P31547; P30750: metN; NbExp=5; IntAct=EBI-8769561, EBI-541886;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC {ECO:0000305|PubMed:15919996}.
CC -!- DISRUPTION PHENOTYPE: Disruption confers resistance to cellular
CC contact-dependent growth inhibition (CDI) CdiA of E.coli strain MHI813,
CC but not to several other tested CdiA toxins.
CC {ECO:0000269|PubMed:26305955}.
CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC permease family. CysTW subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA03658.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; D15061; BAA03658.1; ALT_INIT; Genomic_DNA.
DR EMBL; U70214; AAB08626.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73309.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA77875.1; -; Genomic_DNA.
DR PIR; F64744; F64744.
DR RefSeq; NP_414740.1; NC_000913.3.
DR RefSeq; WP_001294600.1; NZ_STEB01000032.1.
DR PDB; 3DHW; X-ray; 3.70 A; A/B/E/F=1-217.
DR PDB; 3TUI; X-ray; 2.90 A; A/B/E/F=1-217.
DR PDB; 3TUJ; X-ray; 4.00 A; A/B=1-217.
DR PDB; 3TUZ; X-ray; 3.40 A; A/B/E/F=1-217.
DR PDB; 6CVL; X-ray; 2.95 A; A/B=1-215.
DR PDBsum; 3DHW; -.
DR PDBsum; 3TUI; -.
DR PDBsum; 3TUJ; -.
DR PDBsum; 3TUZ; -.
DR PDBsum; 6CVL; -.
DR AlphaFoldDB; P31547; -.
DR SMR; P31547; -.
DR BioGRID; 4259754; 9.
DR ComplexPortal; CPX-2114; Methionine ABC transporter complex.
DR DIP; DIP-11198N; -.
DR IntAct; P31547; 2.
DR STRING; 511145.b0198; -.
DR TCDB; 3.A.1.24.1; the atp-binding cassette (abc) superfamily.
DR jPOST; P31547; -.
DR PaxDb; P31547; -.
DR PRIDE; P31547; -.
DR EnsemblBacteria; AAC73309; AAC73309; b0198.
DR EnsemblBacteria; BAA77875; BAA77875; BAA77875.
DR GeneID; 67416275; -.
DR GeneID; 944894; -.
DR KEGG; ecj:JW0194; -.
DR KEGG; eco:b0198; -.
DR PATRIC; fig|1411691.4.peg.2080; -.
DR EchoBASE; EB1688; -.
DR eggNOG; COG2011; Bacteria.
DR HOGENOM; CLU_077375_0_1_6; -.
DR InParanoid; P31547; -.
DR OMA; TFWSAIF; -.
DR PhylomeDB; P31547; -.
DR BioCyc; EcoCyc:METI-MON; -.
DR BioCyc; MetaCyc:METI-MON; -.
DR BRENDA; 7.4.2.11; 2026.
DR EvolutionaryTrace; P31547; -.
DR PRO; PR:P31547; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0055052; C:ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; IDA:EcoCyc.
DR GO; GO:0005887; C:integral component of plasma membrane; ISM:EcoCyc.
DR GO; GO:0016020; C:membrane; IDA:ComplexPortal.
DR GO; GO:1990197; C:methionine-importing ABC transporter complex; IPI:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0015191; F:L-methionine transmembrane transporter activity; IDA:EcoCyc.
DR GO; GO:0006865; P:amino acid transport; IBA:GO_Central.
DR GO; GO:0048473; P:D-methionine transport; IMP:CACAO.
DR GO; GO:1903692; P:methionine import across plasma membrane; IDA:ComplexPortal.
DR CDD; cd06261; TM_PBP2; 1.
DR Gene3D; 1.10.3720.10; -; 1.
DR InterPro; IPR000515; MetI-like.
DR InterPro; IPR035906; MetI-like_sf.
DR Pfam; PF00528; BPD_transp_1; 1.
DR SUPFAM; SSF161098; SSF161098; 1.
DR PROSITE; PS50928; ABC_TM1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid transport; Cell inner membrane; Cell membrane;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..217
FT /note="D-methionine transport system permease protein MetI"
FT /id="PRO_0000060098"
FT TOPO_DOM 1..19
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 41..57
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 79..80
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 81..101
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 102..151
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 173..185
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 186..206
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 207..217
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
FT DOMAIN 13..204
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT HELIX 3..40
FT /evidence="ECO:0007829|PDB:3TUI"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:3TUI"
FT HELIX 50..64
FT /evidence="ECO:0007829|PDB:3TUI"
FT HELIX 68..74
FT /evidence="ECO:0007829|PDB:3TUI"
FT HELIX 76..83
FT /evidence="ECO:0007829|PDB:3TUI"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:3TUI"
FT HELIX 89..112
FT /evidence="ECO:0007829|PDB:3TUI"
FT HELIX 118..125
FT /evidence="ECO:0007829|PDB:3TUI"
FT HELIX 130..136
FT /evidence="ECO:0007829|PDB:3TUI"
FT HELIX 138..163
FT /evidence="ECO:0007829|PDB:3TUI"
FT TURN 164..168
FT /evidence="ECO:0007829|PDB:3TUI"
FT HELIX 171..180
FT /evidence="ECO:0007829|PDB:3TUI"
FT HELIX 186..211
FT /evidence="ECO:0007829|PDB:3TUI"
SQ SEQUENCE 217 AA; 23256 MW; EC1A22D772468EA8 CRC64;
MSEPMMWLLV RGVWETLAMT FVSGFFGFVI GLPVGVLLYV TRPGQIIANA KLYRTVSAIV
NIFRSIPFII LLVWMIPFTR VIVGTSIGLQ AAIVPLTVGA APFIARMVEN ALLEIPTGLI
EASRAMGATP MQIVRKVLLP EALPGLVNAA TITLITLVGY SAMGGAVGAG GLGQIGYQYG
YIGYNATVMN TVLVLLVILV YLIQFAGDRI VRAVTRK
