METN2_SALTI
ID METN2_SALTI Reviewed; 338 AA.
AC Q8Z8R5; Q7C8C5;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Methionine import ATP-binding protein MetN 2 {ECO:0000255|HAMAP-Rule:MF_01719};
DE EC=7.4.2.11 {ECO:0000255|HAMAP-Rule:MF_01719};
GN Name=metN2 {ECO:0000255|HAMAP-Rule:MF_01719};
GN OrderedLocusNames=STY0559, t2349;
OS Salmonella typhi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(2003).
CC -!- FUNCTION: Part of the ABC transporter complex MetNIQ involved in
CC methionine import. Responsible for energy coupling to the transport
CC system. {ECO:0000255|HAMAP-Rule:MF_01719}.
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 -!- 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 -!- 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}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01719}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01719}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. Methionine
CC importer (TC 3.A.1.24) family. {ECO:0000255|HAMAP-Rule:MF_01719}.
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DR EMBL; AL513382; CAD04996.1; -; Genomic_DNA.
DR EMBL; AE014613; AAO69941.1; -; Genomic_DNA.
DR RefSeq; NP_455106.1; NC_003198.1.
DR RefSeq; WP_000569655.1; NZ_WSUR01000008.1.
DR AlphaFoldDB; Q8Z8R5; -.
DR SMR; Q8Z8R5; -.
DR STRING; 220341.16501781; -.
DR EnsemblBacteria; AAO69941; AAO69941; t2349.
DR KEGG; stt:t2349; -.
DR KEGG; sty:STY0559; -.
DR PATRIC; fig|220341.7.peg.560; -.
DR eggNOG; COG1135; Bacteria.
DR HOGENOM; CLU_000604_1_3_6; -.
DR OMA; VIRKICH; -.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0033232; F:ABC-type D-methionine transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; 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 PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR PROSITE; PS51264; METN; 1.
PE 3: Inferred from homology;
KW Amino-acid transport; ATP-binding; Cell inner membrane; Cell membrane;
KW Membrane; Nucleotide-binding; Translocase; Transport.
FT CHAIN 1..338
FT /note="Methionine import ATP-binding protein MetN 2"
FT /id="PRO_0000270380"
FT DOMAIN 2..242
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01719"
FT BINDING 39..46
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01719"
SQ SEQUENCE 338 AA; 36378 MW; E8D943D23DA38FBD CRC64;
MIEIEKVCVD FTAGRGTPTR AVDDVSLHIA AGEIFGIVGT SGAGKSTLLR TLNALTRPSQ
GRVNVNGVEI SALDGKALRQ ARQRIGMIFQ HFNLMHTRTV AKNVAFSLKA AGWERSKIAP
RVAEILTLVG LADKANCFPV QLSGGQKQRV GIARAIANHP DVLLCDEPTS ALDLETSATI
LALLRQINAQ LGITIVLITH EMNVIKSICD RVAVMSGGKV VESGEVFDVF AHPQHAFTQQ
LVSHTLNLTL PERLREHLPG QLLKILFIGD SAEQPVLSEV AIKFGVAVNI LHGKIEYIGE
RALGILVVQL TAPHNPTAVA AAVEHIRQRT AQVEVIRG
