ID   METN_HAES1              Reviewed;         345 AA.
AC   Q0I5E9;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 106.
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=HS_1533;
OS   Haemophilus somnus (strain 129Pt) (Histophilus somni).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Histophilus.
OX   NCBI_TaxID=205914;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=129Pt;
RX   PubMed=17172329; DOI=10.1128/jb.01422-06;
RA   Challacombe J.F., Duncan A.J., Brettin T.S., Bruce D., Chertkov O.,
RA   Detter J.C., Han C.S., Misra M., Richardson P., Tapia R., Thayer N.,
RA   Xie G., Inzana T.J.;
RT   "Complete genome sequence of Haemophilus somnus (Histophilus somni) strain
RT   129Pt and comparison to Haemophilus ducreyi 35000HP and Haemophilus
RT   influenzae Rd.";
RL   J. Bacteriol. 189:1890-1898(2007).
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; CP000436; ABI25801.1; -; Genomic_DNA.
DR   RefSeq; WP_011609679.1; NC_008309.1.
DR   AlphaFoldDB; Q0I5E9; -.
DR   SMR; Q0I5E9; -.
DR   STRING; 205914.HS_1533; -.
DR   EnsemblBacteria; ABI25801; ABI25801; HS_1533.
DR   KEGG; hso:HS_1533; -.
DR   eggNOG; COG1135; Bacteria.
DR   HOGENOM; CLU_000604_1_3_6; -.
DR   OMA; VFITHEI; -.
DR   GO; GO:0009276; C:Gram-negative-bacterium-type cell wall; IEA:InterPro.
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; IPR012692; ABC_MetN_proteobac.
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   TIGRFAMs; TIGR02314; ABC_MetN; 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..345
FT                   /note="Methionine import ATP-binding protein MetN"
FT                   /id="PRO_0000270308"
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   345 AA;  37860 MW;  EA64ADE9F0E54C75 CRC64;
     MIKLKNISKV FNVSGKNLTA LDNVSLEVPQ GQICGVIGAS GAGKSTLIRC INLLERPTSG
     SVIVDNTDLT QLSDNELIHA RRHIGMIFQH FNLLSSRTVF DNVALPLELE KTDKTQIKQK
     VDALLNLVGL YDKKDVYPAN LSGGQKQRVA IARALANSPK VLLCDEATSA LDPATTQSIL
     KLLKEINRTL GITILLITHE MDVVKRICDQ VAVINKGQLI EQGSVGDIFS NPKTLLAQEF
     IHSTFHINLP EEYMENLSAT PKHAKSYPII KFEFTGRSVD APLLSQASKQ FGVDLSILSS
     QIDYAGEVKF GFVIAEVEGE EEAITQTKIY LMENNVRVEV LGYVG