(data stored in ACNUC7421 zone)

SWISSPROT: D6Z9R7_SEGRD

ID   D6Z9R7_SEGRD            Unreviewed;       351 AA.
AC   D6Z9R7;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 57.
DE   RecName: Full=Methionine import ATP-binding protein MetN {ECO:0000256|HAMAP-Rule:MF_01719};
DE            EC=3.6.3.- {ECO:0000256|HAMAP-Rule:MF_01719};
GN   Name=metN {ECO:0000256|HAMAP-Rule:MF_01719};
GN   OrderedLocusNames=Srot_0103 {ECO:0000313|EMBL:ADG96594.1};
OS   Segniliparus rotundus (strain ATCC BAA-972 / CDC 1076 / CIP 108378 /
OS   DSM 44985 / JCM 13578).
OC   Bacteria; Actinobacteria; Corynebacteriales; Segniliparaceae;
OC   Segniliparus.
OX   NCBI_TaxID=640132 {ECO:0000313|EMBL:ADG96594.1, ECO:0000313|Proteomes:UP000002247};
RN   [1] {ECO:0000313|EMBL:ADG96594.1, ECO:0000313|Proteomes:UP000002247}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-972 / CDC 1076 / CIP 108378 / DSM 44985 / JCM 13578
RC   {ECO:0000313|Proteomes:UP000002247};
RX   PubMed=21304703; DOI=10.4056/sigs.791633;
RA   Sikorski J., Lapidus A., Copeland A., Misra M., Glavina Del Rio T.,
RA   Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Jando M.,
RA   Schneider S., Bruce D., Goodwin L., Pitluck S., Liolios K.,
RA   Mikhailova N., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Chertkov O., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Brettin T., Detter J.C., Han C., Rohde M., Goker M.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA   Klenk H.P.;
RT   "Complete genome sequence of Segniliparus rotundus type strain (CDC
RT   1076).";
RL   Stand. Genomic Sci. 2:203-211(2010).
CC   -!- FUNCTION: Part of the ABC transporter complex MetNIQ involved in
CC       methionine import. Responsible for energy coupling to the
CC       transport system. {ECO:0000256|HAMAP-Rule:MF_01719,
CC       ECO:0000256|SAAS:SAAS01165801}.
CC   -!- SUBUNIT: The complex is composed of two ATP-binding proteins
CC       (MetN), two transmembrane proteins (MetI) and a solute-binding
CC       protein (MetQ). {ECO:0000256|HAMAP-Rule:MF_01719,
CC       ECO:0000256|SAAS:SAAS01165800}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_01719}; Peripheral membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_01719}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. Methionine
CC       importer (TC 3.A.1.24) family. {ECO:0000256|HAMAP-Rule:MF_01719,
CC       ECO:0000256|SAAS:SAAS00548293}.
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DR   EMBL; CP001958; ADG96594.1; -; Genomic_DNA.
DR   RefSeq; WP_013137050.1; NC_014168.1.
DR   STRING; 640132.Srot_0103; -.
DR   EnsemblBacteria; ADG96594; ADG96594; Srot_0103.
DR   KEGG; srt:Srot_0103; -.
DR   eggNOG; ENOG4108JEI; Bacteria.
DR   eggNOG; COG1135; LUCA.
DR   KO; K02071; -.
DR   OMA; LIRLINC; -.
DR   OrthoDB; 1058434at2; -.
DR   BioCyc; SROT640132:G1GLH-103-MONOMER; -.
DR   Proteomes; UP000002247; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015424; F:amino acid-transporting ATPase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0015821; P:methionine transport; IEA:InterPro.
DR   CDD; cd03258; ABC_MetN_methionine_transporte; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR026253; ABC_MetN.
DR   InterPro; IPR003439; ABC_transporter-like.
DR   InterPro; IPR017871; ABC_transporter_CS.
DR   InterPro; IPR017908; ABC_transprt_methionine_MetN_C.
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   SUPFAM; SSF52540; SSF52540; 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;
DR   PRODOM; D6Z9R7.
DR   SWISS-2DPAGE; D6Z9R7.
KW   Amino-acid transport {ECO:0000256|HAMAP-Rule:MF_01719,
KW   ECO:0000256|SAAS:SAAS00433007};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01719, ECO:0000256|PROSITE-
KW   ProRule:PRU00434, ECO:0000256|SAAS:SAAS00035635};
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_01719};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01719,
KW   ECO:0000256|SAAS:SAAS00433023};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002247};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01719,
KW   ECO:0000256|SAAS:SAAS00432985};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01719,
KW   ECO:0000256|SAAS:SAAS00433044};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01719,
KW   ECO:0000256|PROSITE-ProRule:PRU00434, ECO:0000256|SAAS:SAAS00035551};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002247};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_01719,
KW   ECO:0000256|SAAS:SAAS00433037}.
FT   DOMAIN       13    252       ABC transporter. {ECO:0000259|PROSITE:
FT                                PS50893}.
FT   DOMAIN      249    351       METN. {ECO:0000259|PROSITE:PS51264}.
FT   NP_BIND      49     56       ATP. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00434}.
SQ   SEQUENCE   351 AA;  36976 MW;  C480424546E9A5D1 CRC64;
     MTQNTAASGG TSIRFENVSK TFASGKRLVT AVDNVSLDIP SGEIFAMIGY SGAGKSTLLR
     MINGLERPTS GRVLVGGAEV SSLPERQLRA IRADVGMVFQ QFNLFRSRTV AGNVAYPLKV
     AGWPAAKRAA RVAELLDFVG LADKAKHYPD QLSGGQKQRV GVARALASGP SVLLADEATS
     ALDPETTKDV LGLLRSVNTE FGVTIVAITH SMSVVRALAD RVAVLANGAV VETGTVFDIF
     ANPRSDISRN FVSTVLRHAP DSQDLARIAR RHAGTIVSVE IRDDVQIGRL LSEAARGGVG
     FEVVHGGVSS LQSRVFGNLS LELQGPPEGV ARLVGELKAA TKTIVAQEAL P
//

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