ID   METN_BACSU              Reviewed;         341 AA.
AC   O32169;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 133.
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:14990259};
GN   Name=metN {ECO:0000255|HAMAP-Rule:MF_01719, ECO:0000303|PubMed:14990259};
GN   Synonyms=yusC; OrderedLocusNames=BSU32750;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [2]
RP   FUNCTION IN METHIONINE AND METHIONINE SULFOXIDE TRANSPORT, CATALYTIC
RP   ACTIVITY, AND INDUCTION.
RC   STRAIN=168;
RX   PubMed=14990259; DOI=10.1016/j.resmic.2003.11.008;
RA   Hullo M.-F., Auger S., Dassa E., Danchin A., Martin-Verstraete I.;
RT   "The metNPQ operon of Bacillus subtilis encodes an ABC permease
RT   transporting methionine sulfoxide, D- and L-methionine.";
RL   Res. Microbiol. 155:80-86(2004).
CC   -!- FUNCTION: Part of the ABC transporter complex MetNPQ involved in
CC       methionine import (PubMed:14990259). Responsible for energy coupling to
CC       the transport system (Probable). It has also been shown to be involved
CC       in methionine sulfoxide transport (PubMed:14990259).
CC       {ECO:0000269|PubMed:14990259, ECO:0000305}.
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:14990259};
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:14990259};
CC   -!- SUBUNIT: The complex is composed of two ATP-binding proteins (MetN),
CC       two transmembrane proteins (MetP) and a solute-binding protein (MetQ).
CC       {ECO:0000255|HAMAP-Rule:MF_01719}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01719};
CC       Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01719}.
CC   -!- INDUCTION: Repressed by methionine via the S-box system.
CC       {ECO:0000269|PubMed:14990259}.
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; AL009126; CAB15264.1; -; Genomic_DNA.
DR   PIR; D70020; D70020.
DR   RefSeq; NP_391154.1; NC_000964.3.
DR   RefSeq; WP_003242531.1; NZ_JNCM01000033.1.
DR   AlphaFoldDB; O32169; -.
DR   SMR; O32169; -.
DR   IntAct; O32169; 1.
DR   MINT; O32169; -.
DR   STRING; 224308.BSU32750; -.
DR   TCDB; 3.A.1.24.2; the atp-binding cassette (abc) superfamily.
DR   PaxDb; O32169; -.
DR   PRIDE; O32169; -.
DR   EnsemblBacteria; CAB15264; CAB15264; BSU_32750.
DR   GeneID; 936700; -.
DR   KEGG; bsu:BSU32750; -.
DR   PATRIC; fig|224308.179.peg.3548; -.
DR   eggNOG; COG1135; Bacteria.
DR   InParanoid; O32169; -.
DR   OMA; VIRKICH; -.
DR   PhylomeDB; O32169; -.
DR   BioCyc; BSUB:BSU32750-MON; -.
DR   Proteomes; UP000001570; 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; 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   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   1: Evidence at protein level;
KW   Amino-acid transport; ATP-binding; Cell membrane; Membrane;
KW   Nucleotide-binding; Reference proteome; Translocase; Transport.
FT   CHAIN           1..341
FT                   /note="Methionine import ATP-binding protein MetN"
FT                   /id="PRO_0000270247"
FT   DOMAIN          2..241
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01719"
FT   BINDING         38..45
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01719"
SQ   SEQUENCE   341 AA;  37886 MW;  37DDC75528723311 CRC64;
     MINLQDVSKV YKSKHGDVNA VQNVSLSIKK GEIFGIIGYS GAGKSSLIRL LNGLEKPTSG
     TVEVAGTKIN EVNGRGLRKA RHEISMIFQH FNLLWSRTVR DNIMFPLEIA GVKKSERIKR
     ANELIKLVGL EGKEKSYPSQ LSGGQKQRVG IARALANNPK VLLCDEATSA LDPQTTDSIL
     DLLSDINERL GLTIVLITHE MHVIRKICNR VAVMENGKVV EEGEVLDVFK NPKEQMTKRF
     VQQVTEPEET KETLQHLLDD TASGKMVQLT FVGESAEQPL ITEMIRNFNV SVNILQGKIS
     QTKDGAYGSL FIHIDGDEEE VQNVIRFIND KQVKAEVITN V