METN_ECOLI
ID METN_ECOLI Reviewed; 343 AA.
AC P30750; P77517; Q47615;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 4.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Methionine import ATP-binding protein MetN {ECO:0000255|HAMAP-Rule:MF_01719};
DE EC=7.4.2.11 {ECO:0000255|HAMAP-Rule:MF_01719, ECO:0000269|PubMed:12169620, ECO:0000269|PubMed:12218041, ECO:0000269|PubMed:12819857};
GN Name=metN {ECO:0000255|HAMAP-Rule:MF_01719, ECO:0000303|PubMed:12218041};
GN Synonyms=abc; OrderedLocusNames=b0199, JW0195;
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., Inokuchi H.;
RT "Nucleotide sequence of 5'flanking region of the ribosomal RNA gene (rrnH)
RT in E. coli.";
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], AND SEQUENCE REVISION TO
RP 106.
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-231.
RC STRAIN=TAP90 / ATCC 47037;
RX PubMed=7904973; DOI=10.1016/0378-1119(93)90470-n;
RA Allikmets R., Gerrard B.C., Court D., Dean M.C.;
RT "Cloning and organization of the abc and mdl genes of Escherichia coli:
RT relationship to eukaryotic multidrug resistance.";
RL Gene 136:231-236(1993).
RN [7]
RP FUNCTION IN METHIONINE TRANSPORT, AND CATALYTIC ACTIVITY.
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 [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RX PubMed=12218041; DOI=10.1128/jb.184.19.5513-5517.2002;
RA Merlin C., Gardiner G., Durand S., Masters M.;
RT "The Escherichia coli metD locus encodes an ABC transporter which includes
RT Abc (MetN), YaeE (MetI), and YaeC (MetQ).";
RL J. Bacteriol. 184:5513-5517(2002).
RN [9]
RP FUNCTION IN METHIONINE AND FORMYL-L-METHIONINE TRANSPORT, CATALYTIC
RP ACTIVITY, AND INDUCTION.
RC STRAIN=K12;
RX PubMed=12819857; DOI=10.1007/s00203-003-0561-4;
RA Zhang Z., Feige J.N., Chang A.B., Anderson I.J., Brodianski V.M.,
RA Vitreschak A.G., Gelfand M.S., Saier M.H. Jr.;
RT "A transporter of Escherichia coli specific for L- and D-methionine is the
RT prototype for a new family within the ABC superfamily.";
RL Arch. Microbiol. 180:88-100(2003).
RN [10]
RP FUNCTION, ATPASE ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=25678706; DOI=10.1074/jbc.m114.603365;
RA Yang J.G., Rees D.C.;
RT "The allosteric regulatory mechanism of the Escherichia coli MetNI
RT methionine ATP binding cassette (ABC) transporter.";
RL J. Biol. Chem. 290:9135-9140(2015).
RN [11] {ECO:0007744|PDB:3DHW, ECO:0007744|PDB:3DHX}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 246-343 IN COMPLEX WITH METI,
RP FUNCTION, ATPASE ACTIVITY, ACTIVITY REGULATION, SUBUNIT, DOMAIN, AND
RP MUTAGENESIS OF GLU-166.
RX PubMed=18621668; DOI=10.1126/science.1157987;
RA Kadaba N.S., Kaiser J.T., Johnson E., Lee A., Rees D.C.;
RT "The high-affinity E. coli methionine ABC transporter: structure and
RT allosteric regulation.";
RL Science 321:250-253(2008).
RN [12] {ECO:0007744|PDB:3TUI, ECO:0007744|PDB:3TUJ, ECO:0007744|PDB:3TUZ}
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) IN COMPLEXES WITH METI; ADP AND
RP SELENOMETHIONINE, AND ACTIVITY REGULATION.
RX PubMed=22095702; DOI=10.1002/pro.765;
RA Johnson E., Nguyen P.T., Yeates T.O., Rees D.C.;
RT "Inward facing conformations of the MetNI methionine ABC transporter:
RT Implications for the mechanism of transinhibition.";
RL Protein Sci. 21:84-96(2012).
RN [13] {ECO:0007744|PDB:6CVL}
RP X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF MUTANT GLN-166/ALA-295 IN COMPLEX
RP WITH METI AND METQ, FUNCTION, ACTIVITY REGULATION, SUBUNIT, AND MUTAGENESIS
RP OF ASN-295.
RC STRAIN=K12;
RX PubMed=30352853; DOI=10.1073/pnas.1811003115;
RA Nguyen P.T., Lai J.Y., Lee A.T., Kaiser J.T., Rees D.C.;
RT "Noncanonical role for the binding protein in substrate uptake by the MetNI
RT methionine ATP Binding Cassette (ABC) transporter.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:E10596-E10604(2018).
CC -!- FUNCTION: Part of the ABC transporter complex MetNIQ involved in
CC methionine import (PubMed:12169620, PubMed:12218041, PubMed:12819857,
CC PubMed:18621668, PubMed:30352853). Responsible for energy coupling to
CC the transport system (PubMed:18621668, PubMed:25678706). It has also
CC been shown to be involved in formyl-L-methionine transport
CC (PubMed:12819857). {ECO:0000269|PubMed:12169620,
CC ECO:0000269|PubMed:12218041, ECO:0000269|PubMed:12819857,
CC ECO:0000269|PubMed:18621668, ECO:0000269|PubMed:25678706,
CC ECO:0000269|PubMed:30352853}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + L-methionine(out) = ADP + H(+) + L-methionine(in)
CC + phosphate; Xref=Rhea:RHEA:29779, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57844, ChEBI:CHEBI:456216; EC=7.4.2.11;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01719,
CC ECO:0000269|PubMed:12819857};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-methionine(out) + H2O = ADP + D-methionine(in) + H(+)
CC + phosphate; Xref=Rhea:RHEA:29767, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57932, ChEBI:CHEBI:456216; EC=7.4.2.11;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01719,
CC ECO:0000269|PubMed:12169620, ECO:0000269|PubMed:12218041,
CC ECO:0000269|PubMed:12819857};
CC -!- ACTIVITY REGULATION: ATPase activity is inhibited by intracellular L-
CC methionine (PubMed:18621668, PubMed:22095702, PubMed:25678706,
CC PubMed:30352853). Binding of methionine to the dimerized C-terminal
CC regulatory domain stabilizes an inward-facing, ATPase-inactive
CC conformation of the transporter, and as a consequence, the rate of ATP
CC hydrolysis decreases (PubMed:18621668, PubMed:22095702,
CC PubMed:30352853). ADP is a competitive inhibitor (PubMed:25678706).
CC {ECO:0000269|PubMed:18621668, ECO:0000269|PubMed:22095702,
CC ECO:0000269|PubMed:25678706, ECO:0000269|PubMed:30352853}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=330 uM for ATP {ECO:0000269|PubMed:25678706};
CC KM=325 uM for ATP (in the presence of 50 uM L-methionine)
CC {ECO:0000269|PubMed:25678706};
CC KM=1490 uM for ATP (in the presence of 120 uM ADP)
CC {ECO:0000269|PubMed:25678706};
CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins (MetN),
CC two transmembrane proteins (MetI) and a solute-binding protein (MetQ).
CC {ECO:0000255|HAMAP-Rule:MF_01719, ECO:0000269|PubMed:12218041,
CC ECO:0000269|PubMed:18621668, ECO:0000269|PubMed:30352853}.
CC -!- INTERACTION:
CC P30750; P16433: hycG; NbExp=6; IntAct=EBI-541886, EBI-541977;
CC P30750; P31547: metI; NbExp=5; IntAct=EBI-541886, EBI-8769561;
CC P30750; P0A9F1: mntR; NbExp=4; IntAct=EBI-541886, EBI-541895;
CC P30750; P39353: yjhC; NbExp=3; IntAct=EBI-541886, EBI-542024;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01719, ECO:0000305}; Peripheral membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_01719, ECO:0000305}.
CC -!- INDUCTION: Repressed by MetJ. {ECO:0000269|PubMed:12819857}.
CC -!- DOMAIN: Contains a regulatory C-terminal extension (C2) with a
CC ferredoxin-like fold. The C2 domains from each MetN subunit in a
CC transporter dimerize to form an eight-stranded beta sheet.
CC {ECO:0000269|PubMed:18621668}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. Methionine
CC importer (TC 3.A.1.24) family. {ECO:0000255|HAMAP-Rule:MF_01719,
CC ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC36869.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAA03659.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; D15061; BAA03659.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U70214; AAB08627.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73310.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA77876.2; -; Genomic_DNA.
DR EMBL; L08626; AAC36869.1; ALT_FRAME; Unassigned_DNA.
DR PIR; G64744; G64744.
DR RefSeq; NP_414741.1; NC_000913.3.
DR RefSeq; WP_000594006.1; NZ_SSZK01000004.1.
DR PDB; 3DHW; X-ray; 3.70 A; C/D/G/H=1-343.
DR PDB; 3DHX; X-ray; 2.10 A; A/B=246-343.
DR PDB; 3TUI; X-ray; 2.90 A; C/D/G/H=1-343.
DR PDB; 3TUJ; X-ray; 4.00 A; C/D=1-343.
DR PDB; 3TUZ; X-ray; 3.40 A; C/D/G/H=1-343.
DR PDB; 6CVL; X-ray; 2.95 A; C/D=1-343.
DR PDBsum; 3DHW; -.
DR PDBsum; 3DHX; -.
DR PDBsum; 3TUI; -.
DR PDBsum; 3TUJ; -.
DR PDBsum; 3TUZ; -.
DR PDBsum; 6CVL; -.
DR AlphaFoldDB; P30750; -.
DR SMR; P30750; -.
DR BioGRID; 4259755; 38.
DR BioGRID; 849296; 39.
DR ComplexPortal; CPX-2114; Methionine ABC transporter complex.
DR DIP; DIP-9027N; -.
DR IntAct; P30750; 57.
DR STRING; 511145.b0199; -.
DR TCDB; 3.A.1.24.1; the atp-binding cassette (abc) superfamily.
DR jPOST; P30750; -.
DR PaxDb; P30750; -.
DR PRIDE; P30750; -.
DR EnsemblBacteria; AAC73310; AAC73310; b0199.
DR EnsemblBacteria; BAA77876; BAA77876; BAA77876.
DR GeneID; 944896; -.
DR KEGG; ecj:JW0195; -.
DR KEGG; eco:b0199; -.
DR PATRIC; fig|1411691.4.peg.2079; -.
DR EchoBASE; EB1578; -.
DR eggNOG; COG1135; Bacteria.
DR HOGENOM; CLU_000604_1_3_6; -.
DR InParanoid; P30750; -.
DR OMA; VFITHEI; -.
DR PhylomeDB; P30750; -.
DR BioCyc; EcoCyc:ABC-MON; -.
DR BioCyc; MetaCyc:ABC-MON; -.
DR BRENDA; 7.4.2.11; 2026.
DR EvolutionaryTrace; P30750; -.
DR PRO; PR:P30750; -.
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:0009276; C:Gram-negative-bacterium-type cell wall; IEA:InterPro.
DR GO; GO:0016020; C:membrane; IDA:ComplexPortal.
DR GO; GO:1990197; C:methionine-importing ABC transporter complex; IPI:ComplexPortal.
DR GO; GO:0033232; F:ABC-type D-methionine transporter activity; IDA:EcoliWiki.
DR GO; GO:0005524; F:ATP binding; IDA:EcoliWiki.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:EcoliWiki.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IDA:EcoCyc.
DR GO; GO:0015191; F:L-methionine transmembrane transporter activity; IDA:EcoCyc.
DR GO; GO:0048473; P:D-methionine transport; IMP:CACAO.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR GO; GO:1903692; P:methionine import across plasma membrane; IDA:ComplexPortal.
DR CDD; cd03258; ABC_MetN_methionine_transporter; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR026253; ABC_MetN.
DR InterPro; IPR012692; ABC_MetN_proteobac.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR045865; ACT-like_dom_sf.
DR InterPro; IPR041701; MetN_ABC.
DR InterPro; IPR018449; NIL_domain.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR43166:SF5; PTHR43166:SF5; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR Pfam; PF09383; NIL; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00930; NIL; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF55021; SSF55021; 1.
DR TIGRFAMs; TIGR02314; ABC_MetN; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR PROSITE; PS51264; METN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Allosteric enzyme; Amino-acid transport; ATP-binding;
KW Cell inner membrane; Cell membrane; Membrane; Nucleotide-binding;
KW Reference proteome; Translocase; Transport.
FT CHAIN 1..343
FT /note="Methionine import ATP-binding protein MetN"
FT /id="PRO_0000092503"
FT DOMAIN 2..241
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01719"
FT REGION 265..343
FT /note="C2 domain"
FT /evidence="ECO:0000305|PubMed:18621668"
FT BINDING 40..46
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:22095702"
FT BINDING 278..283
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /ligand_note="allosteric inhibitor"
FT /evidence="ECO:0000269|PubMed:22095702"
FT BINDING 295..296
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /ligand_note="allosteric inhibitor"
FT /evidence="ECO:0000269|PubMed:22095702"
FT MUTAGEN 166
FT /note="E->Q: Exhibits little ATPase activity."
FT /evidence="ECO:0000269|PubMed:18621668"
FT MUTAGEN 295
FT /note="N->A: Reduces the binding of L-methionine to
FT undetectable levels."
FT /evidence="ECO:0000269|PubMed:30352853"
FT CONFLICT 165
FT /note="D -> V (in Ref. 6; AAC36869)"
FT /evidence="ECO:0000305"
FT STRAND 2..12
FT /evidence="ECO:0007829|PDB:3TUI"
FT STRAND 14..28
FT /evidence="ECO:0007829|PDB:3TUI"
FT STRAND 33..37
FT /evidence="ECO:0007829|PDB:3TUI"
FT HELIX 44..51
FT /evidence="ECO:0007829|PDB:3TUI"
FT STRAND 58..64
FT /evidence="ECO:0007829|PDB:3TUI"
FT HELIX 74..81
FT /evidence="ECO:0007829|PDB:3TUI"
FT STRAND 84..87
FT /evidence="ECO:0007829|PDB:3TUI"
FT HELIX 99..109
FT /evidence="ECO:0007829|PDB:3TUI"
FT HELIX 114..127
FT /evidence="ECO:0007829|PDB:3TUI"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:3TUI"
FT TURN 138..140
FT /evidence="ECO:0007829|PDB:3TUI"
FT HELIX 143..154
FT /evidence="ECO:0007829|PDB:3TUI"
FT TURN 155..157
FT /evidence="ECO:0007829|PDB:3TUI"
FT STRAND 160..166
FT /evidence="ECO:0007829|PDB:3TUI"
FT TURN 167..170
FT /evidence="ECO:0007829|PDB:3TUI"
FT HELIX 173..189
FT /evidence="ECO:0007829|PDB:3TUI"
FT STRAND 193..199
FT /evidence="ECO:0007829|PDB:3TUI"
FT HELIX 201..207
FT /evidence="ECO:0007829|PDB:3TUI"
FT STRAND 209..215
FT /evidence="ECO:0007829|PDB:3TUI"
FT STRAND 218..221
FT /evidence="ECO:0007829|PDB:3TUI"
FT HELIX 225..229
FT /evidence="ECO:0007829|PDB:3TUI"
FT HELIX 235..244
FT /evidence="ECO:0007829|PDB:3TUI"
FT HELIX 251..256
FT /evidence="ECO:0007829|PDB:3DHX"
FT STRAND 258..260
FT /evidence="ECO:0007829|PDB:3DHX"
FT STRAND 265..276
FT /evidence="ECO:0007829|PDB:3DHX"
FT STRAND 278..280
FT /evidence="ECO:0007829|PDB:3TUZ"
FT HELIX 282..289
FT /evidence="ECO:0007829|PDB:3DHX"
FT STRAND 293..304
FT /evidence="ECO:0007829|PDB:3DHX"
FT STRAND 307..318
FT /evidence="ECO:0007829|PDB:3DHX"
FT HELIX 320..332
FT /evidence="ECO:0007829|PDB:3DHX"
FT STRAND 336..343
FT /evidence="ECO:0007829|PDB:3DHX"
SQ SEQUENCE 343 AA; 37788 MW; 2FC796C605216FB3 CRC64;
MIKLSNITKV FHQGTRTIQA LNNVSLHVPA GQIYGVIGAS GAGKSTLIRC VNLLERPTEG
SVLVDGQELT TLSESELTKA RRQIGMIFQH FNLLSSRTVF GNVALPLELD NTPKDEVKRR
VTELLSLVGL GDKHDSYPSN LSGGQKQRVA IARALASNPK VLLCDEATSA LDPATTRSIL
ELLKDINRRL GLTILLITHE MDVVKRICDC VAVISNGELI EQDTVSEVFS HPKTPLAQKF
IQSTLHLDIP EDYQERLQAE PFTDCVPMLR LEFTGQSVDA PLLSETARRF NVNNNIISAQ
MDYAGGVKFG IMLTEMHGTQ QDTQAAIAWL QEHHVKVEVL GYV
