ID   METN_STRT2              Reviewed;         355 AA.
AC   Q5M5Z2;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 122.
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};
GN   Name=metN {ECO:0000255|HAMAP-Rule:MF_01719}; OrderedLocusNames=stu0301;
OS   Streptococcus thermophilus (strain ATCC BAA-250 / LMG 18311).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=264199;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-250 / LMG 18311;
RX   PubMed=15543133; DOI=10.1038/nbt1034;
RA   Bolotin A., Quinquis B., Renault P., Sorokin A., Ehrlich S.D.,
RA   Kulakauskas S., Lapidus A., Goltsman E., Mazur M., Pusch G.D., Fonstein M.,
RA   Overbeek R., Kyprides N., Purnelle B., Prozzi D., Ngui K., Masuy D.,
RA   Hancy F., Burteau S., Boutry M., Delcour J., Goffeau A., Hols P.;
RT   "Complete sequence and comparative genome analysis of the dairy bacterium
RT   Streptococcus thermophilus.";
RL   Nat. Biotechnol. 22:1554-1558(2004).
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; CP000023; AAV60023.1; -; Genomic_DNA.
DR   RefSeq; WP_011225469.1; NC_006448.1.
DR   AlphaFoldDB; Q5M5Z2; -.
DR   SMR; Q5M5Z2; -.
DR   STRING; 264199.stu0301; -.
DR   EnsemblBacteria; AAV60023; AAV60023; stu0301.
DR   GeneID; 66898225; -.
DR   KEGG; stl:stu0301; -.
DR   eggNOG; COG1135; Bacteria.
DR   HOGENOM; CLU_000604_1_3_9; -.
DR   OMA; VFITHEI; -.
DR   Proteomes; UP000001170; 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; Reference proteome; Translocase; Transport.
FT   CHAIN           1..355
FT                   /note="Methionine import ATP-binding protein MetN"
FT                   /id="PRO_0000270426"
FT   DOMAIN          8..250
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01719"
FT   BINDING         42..49
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01719"
SQ   SEQUENCE   355 AA;  38764 MW;  6DD20EF3C9DE2CD8 CRC64;
     MSNVIIDLKN IDITFTQKRR TIQAVKDVSI QIEKGDIYGI VGYSGAGKST LVRAINLLQV
     PTAGKITIGE DVTFEDGKVQ LTTKELRQKR QTIGMIFQHF NLMAQKTAYE NVAFALRHSK
     LSNEEKDKKI RGLLELVDLA DRAENYPAQL SGGQKQRVAI ARALANDPEI LISDESTSAL
     DPKTTKQILS LLQDLNKKLG LTVVMITHEM QIVKDICNRV AVMQNGQLLE EGSVLDIFSN
     PQEDLTQEFI ETAAGIEDAL AKINAQPLVK NLPASALLVQ LKYVGSSTDR PLLTEIFKDF
     GVSGNILYGN VEILGDTPVG ELVVVLDGDS DKVIAALKAI ENAGVSLRVL KKGAQ