METQ_ECOLI
ID METQ_ECOLI Reviewed; 271 AA.
AC P28635;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=D-methionine-binding lipoprotein MetQ;
DE Flags: Precursor;
GN Name=metQ; Synonyms=yaeC; OrderedLocusNames=b0197, JW0193;
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.;
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].
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 127-271.
RC STRAIN=K12;
RX PubMed=1459951; DOI=10.1128/jb.174.24.8016-8022.1992;
RA Gervais F.G., Drapeau G.R.;
RT "Identification, cloning, and characterization of rcsF, a new regulator
RT gene for exopolysaccharide synthesis that suppresses the division mutation
RT ftsZ84 in Escherichia coli K-12.";
RL J. Bacteriol. 174:8016-8022(1992).
RN [7]
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).
CC -!- FUNCTION: This protein is a component of a D-methionine permease, a
CC binding protein-dependent, ATP-driven transport system.
CC {ECO:0000269|PubMed:12169620}.
CC -!- INTERACTION:
CC P28635; P0AAF3: araG; NbExp=3; IntAct=EBI-1114713, EBI-559586;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: The MetNIQ system is also to be able to transport the
CC toxic methionine analog alpha-methyl-methionine.
CC -!- SIMILARITY: Belongs to the NlpA lipoprotein family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA24507.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; D15061; BAA03657.1; -; Genomic_DNA.
DR EMBL; U70214; AAB08625.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73308.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA77874.1; -; Genomic_DNA.
DR EMBL; L04474; AAA24507.1; ALT_FRAME; Genomic_DNA.
DR PIR; E64744; E64744.
DR RefSeq; NP_414739.1; NC_000913.3.
DR RefSeq; WP_000874226.1; NZ_SSZK01000004.1.
DR PDB; 4YAH; X-ray; 1.60 A; X=1-271.
DR PDB; 6CVL; X-ray; 2.95 A; E=34-259.
DR PDBsum; 4YAH; -.
DR PDBsum; 6CVL; -.
DR AlphaFoldDB; P28635; -.
DR SMR; P28635; -.
DR BioGRID; 4263377; 24.
DR BioGRID; 849293; 1.
DR ComplexPortal; CPX-2114; Methionine ABC transporter complex.
DR DIP; DIP-11196N; -.
DR IntAct; P28635; 10.
DR STRING; 511145.b0197; -.
DR TCDB; 3.A.1.24.1; the atp-binding cassette (abc) superfamily.
DR SWISS-2DPAGE; P28635; -.
DR jPOST; P28635; -.
DR PaxDb; P28635; -.
DR PRIDE; P28635; -.
DR EnsemblBacteria; AAC73308; AAC73308; b0197.
DR EnsemblBacteria; BAA77874; BAA77874; BAA77874.
DR GeneID; 67416274; -.
DR GeneID; 944893; -.
DR KEGG; ecj:JW0193; -.
DR KEGG; eco:b0197; -.
DR PATRIC; fig|1411691.4.peg.2081; -.
DR EchoBASE; EB1467; -.
DR eggNOG; COG1464; Bacteria.
DR HOGENOM; CLU_067080_0_0_6; -.
DR InParanoid; P28635; -.
DR OMA; YQDDAES; -.
DR PhylomeDB; P28635; -.
DR BioCyc; EcoCyc:METQ-MON; -.
DR BioCyc; MetaCyc:METQ-MON; -.
DR PRO; PR:P28635; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0046658; C:anchored component of plasma membrane; TAS:EcoCyc.
DR GO; GO:0055052; C:ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; IDA:EcoCyc.
DR GO; GO:0016020; C:membrane; IDA:ComplexPortal.
DR GO; GO:1990197; C:methionine-importing ABC transporter complex; IPI:ComplexPortal.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; ISM:EcoCyc.
DR GO; GO:0048473; P:D-methionine transport; IMP:CACAO.
DR GO; GO:1903692; P:methionine import across plasma membrane; IDA:ComplexPortal.
DR InterPro; IPR004872; Lipoprotein_NlpA.
DR PANTHER; PTHR30429; PTHR30429; 1.
DR Pfam; PF03180; Lipoprotein_9; 1.
DR PIRSF; PIRSF002854; MetQ; 1.
DR TIGRFAMs; TIGR00363; TIGR00363; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid transport; Cell membrane; Lipoprotein; Membrane;
KW Palmitate; Reference proteome; Signal; Transport.
FT SIGNAL 1..22
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 23..271
FT /note="D-methionine-binding lipoprotein MetQ"
FT /id="PRO_0000019739"
FT LIPID 23
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 23
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CONFLICT 200
FT /note="V -> L (in Ref. 6; AAA24507)"
FT /evidence="ECO:0000305"
FT STRAND 32..38
FT /evidence="ECO:0007829|PDB:4YAH"
FT HELIX 41..57
FT /evidence="ECO:0007829|PDB:4YAH"
FT STRAND 60..70
FT /evidence="ECO:0007829|PDB:4YAH"
FT HELIX 71..77
FT /evidence="ECO:0007829|PDB:4YAH"
FT STRAND 80..88
FT /evidence="ECO:0007829|PDB:4YAH"
FT HELIX 89..99
FT /evidence="ECO:0007829|PDB:4YAH"
FT STRAND 103..108
FT /evidence="ECO:0007829|PDB:4YAH"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:4YAH"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:4YAH"
FT STRAND 132..136
FT /evidence="ECO:0007829|PDB:4YAH"
FT HELIX 139..151
FT /evidence="ECO:0007829|PDB:4YAH"
FT HELIX 167..169
FT /evidence="ECO:0007829|PDB:4YAH"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:4YAH"
FT STRAND 178..182
FT /evidence="ECO:0007829|PDB:4YAH"
FT HELIX 184..186
FT /evidence="ECO:0007829|PDB:4YAH"
FT HELIX 187..190
FT /evidence="ECO:0007829|PDB:4YAH"
FT STRAND 196..201
FT /evidence="ECO:0007829|PDB:4YAH"
FT HELIX 203..206
FT /evidence="ECO:0007829|PDB:4YAH"
FT HELIX 207..209
FT /evidence="ECO:0007829|PDB:4YAH"
FT HELIX 213..216
FT /evidence="ECO:0007829|PDB:4YAH"
FT STRAND 218..220
FT /evidence="ECO:0007829|PDB:4YAH"
FT STRAND 229..234
FT /evidence="ECO:0007829|PDB:4YAH"
FT HELIX 235..237
FT /evidence="ECO:0007829|PDB:4YAH"
FT HELIX 241..250
FT /evidence="ECO:0007829|PDB:4YAH"
FT HELIX 253..262
FT /evidence="ECO:0007829|PDB:4YAH"
FT TURN 263..265
FT /evidence="ECO:0007829|PDB:4YAH"
SQ SEQUENCE 271 AA; 29432 MW; B50CBC6FB5CD2BF7 CRC64;
MAFKFKTFAA VGALIGSLAL VGCGQDEKDP NHIKVGVIVG AEQQVAEVAQ KVAKDKYGLD
VELVTFNDYV LPNEALSKGD IDANAFQHKP YLDQQLKDRG YKLVAVGNTF VYPIAGYSKK
IKSLDELQDG SQVAVPNDPT NLGRSLLLLQ KVGLIKLKDG VGLLPTVLDV VENPKNLKIV
ELEAPQLPRS LDDAQIALAV INTTYASQIG LTPAKDGIFV EDKESPYVNL IVTREDNKDA
ENVKKFVQAY QSDEVYEAAN KVFNGGAVKG W