ID   METN_LACLN              Reviewed;         368 AA.
AC   D8KFN1; A2RI53; Q9RLV5;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 1.
DT   03-AUG-2022, entry version 56.
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=LLNZ_01785;
OS   Lactococcus lactis subsp. cremoris (strain NZ9000).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus; Lactococcus cremoris subsp. cremoris.
OX   NCBI_TaxID=746361;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NZ9000;
RX   PubMed=10647818; DOI=10.3109/10425179909033942;
RA   Aungpraphapornchai P., Griffin H.G., Gasson M.J.;
RT   "Cloning, DNA sequence analysis, and deletion of a gene encoding diacetyl-
RT   acetoin reductase from Lactococcus lactis.";
RL   DNA Seq. 10:163-172(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NZ9000;
RX   PubMed=20639323; DOI=10.1128/jb.00533-10;
RA   Linares D.M., Kok J., Poolman B.;
RT   "Genome sequences of Lactococcus lactis MG1363 (revised) and NZ9000 and
RT   comparative physiological studies.";
RL   J. Bacteriol. 192:5806-5812(2010).
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; AJ012388; CAB59828.1; -; Genomic_DNA.
DR   EMBL; CP002094; ADJ59361.1; -; Genomic_DNA.
DR   RefSeq; WP_011834402.1; NC_017949.1.
DR   AlphaFoldDB; D8KFN1; -.
DR   SMR; D8KFN1; -.
DR   KEGG; lln:LLNZ_01785; -.
DR   PATRIC; fig|746361.3.peg.350; -.
DR   HOGENOM; CLU_000604_1_3_9; -.
DR   OMA; VFITHEI; -.
DR   OrthoDB; 1058434at2; -.
DR   BioCyc; LLAC746361:LLNZ_RS01765-MON; -.
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..368
FT                   /note="Methionine import ATP-binding protein MetN"
FT                   /id="PRO_0000402183"
FT   DOMAIN          5..260
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01719"
FT   BINDING         41..48
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01719"
SQ   SEQUENCE   368 AA;  40987 MW;  340707169683EB26 CRC64;
     MTAIIELNNL SVQFHQKGRL VTAVKNATLH IEKGDIYGVI GYSGAGKSTL VRTINLLQKP
     TEGQIVINGE KIFDSENPVK FTGAKLREFR QKIGMIFQHF NLLSEKTVFN NVAFALQHSQ
     IEDKNGKKRY LTKKEKNDKV TELLKLVDLA DLSDKYPAQL SGGQKQRVAI ARALANDPEI
     LISDEGTSAL DPKTTNQILD LLKSLHEKLG ITVVLITHEM QVVKEIANKV AVMQNGEIIE
     QNSLIDIFAQ PKEALTKQFI ETTSSVNRFI ASLSKTELLA QLADDEELIH LDYSGSELED
     PVVSDITKKF DVTTNIFYGN VELLQGQPFG SLVLTLKGSS EHRAAAKAYF VERHLKFEVL
     GKIERTVD