ID   METN1_STAAN             Reviewed;         341 AA.
AC   Q7A7E3;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=Methionine import ATP-binding protein MetN 1 {ECO:0000255|HAMAP-Rule:MF_01719};
DE            EC=7.4.2.11 {ECO:0000255|HAMAP-Rule:MF_01719};
GN   Name=metN1 {ECO:0000255|HAMAP-Rule:MF_01719}; OrderedLocusNames=SA0420;
OS   Staphylococcus aureus (strain N315).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=158879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N315;
RX   PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA   Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA   Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA   Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA   Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA   Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA   Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA   Hiramatsu K.;
RT   "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL   Lancet 357:1225-1240(2001).
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 membrane {ECO:0000255|HAMAP-Rule:MF_01719};
CC       Peripheral membrane protein {ECO:0000255|HAMAP-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; BA000018; BAB41650.1; -; Genomic_DNA.
DR   PIR; G89811; G89811.
DR   RefSeq; WP_000569281.1; NC_002745.2.
DR   AlphaFoldDB; Q7A7E3; -.
DR   SMR; Q7A7E3; -.
DR   EnsemblBacteria; BAB41650; BAB41650; BAB41650.
DR   KEGG; sau:SA0420; -.
DR   HOGENOM; CLU_000604_1_3_9; -.
DR   OMA; VFITHEI; -.
DR   Proteomes; UP000000751; 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 membrane; Membrane;
KW   Nucleotide-binding; Translocase; Transport.
FT   CHAIN           1..341
FT                   /note="Methionine import ATP-binding protein MetN 1"
FT                   /id="PRO_0000270399"
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;  38521 MW;  439E244043B71A9C CRC64;
     MIEFRQVSKS FHKKKQTIDA LKDVSFTVNR NDIFGVIGYS GAGKSTLVRL VNHLEAASNG
     QVIVDGHDIT NYSEKGMREI KKDIGMIFQH FNLLNSATVF KNVAMPLILS KKSKTEIKQR
     VTEMLEFVGL SDKKDQFPDE LSGGQKQRVA IARALVTNPK ILLCDEATSA LDPATTASIL
     TLLKNVNQTF GITIMMITHE MRVIKDICNR VAVMEKGQVV ETGTVKEVFS HPKTTIAQNF
     VSTVIQTEPS TSLIRRLNDE QVGGFKDYKI FVEETQVTQP IINDLIQICG REVKILFSSM
     SEIQGNTVCY MWLRFNIDQQ FDDTAINQYF KEKNIQFEEV H