METP_BACSU
ID METP_BACSU Reviewed; 222 AA.
AC O32168;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Methionine import system permease protein MetP;
GN Name=metP; Synonyms=yusB; OrderedLocusNames=BSU32740;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [2]
RP FUNCTION IN METHIONINE AND METHIONINE SULFOXIDE TRANSPORT, AND INDUCTION.
RC STRAIN=168;
RX PubMed=14990259; DOI=10.1016/j.resmic.2003.11.008;
RA Hullo M.-F., Auger S., Dassa E., Danchin A., Martin-Verstraete I.;
RT "The metNPQ operon of Bacillus subtilis encodes an ABC permease
RT transporting methionine sulfoxide, D- and L-methionine.";
RL Res. Microbiol. 155:80-86(2004).
CC -!- FUNCTION: Part of the ABC transporter complex MetNPQ involved in
CC methionine import. Responsible for the translocation of the substrate
CC across the membrane (Probable). It has also been shown to be involved
CC in methionine sulfoxide transport. {ECO:0000269|PubMed:14990259,
CC ECO:0000305}.
CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins (MetN),
CC two transmembrane proteins (MetP) and a solute-binding protein (MetQ).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
CC -!- INDUCTION: Repressed by methionine via the S-box system.
CC {ECO:0000269|PubMed:14990259}.
CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC permease family. CysTW subfamily. {ECO:0000305}.
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DR EMBL; AL009126; CAB15263.1; -; Genomic_DNA.
DR PIR; C70020; C70020.
DR RefSeq; NP_391153.1; NC_000964.3.
DR RefSeq; WP_003228593.1; NZ_JNCM01000033.1.
DR AlphaFoldDB; O32168; -.
DR SMR; O32168; -.
DR STRING; 224308.BSU32740; -.
DR TCDB; 3.A.1.24.2; the atp-binding cassette (abc) superfamily.
DR PaxDb; O32168; -.
DR PRIDE; O32168; -.
DR EnsemblBacteria; CAB15263; CAB15263; BSU_32740.
DR GeneID; 936709; -.
DR KEGG; bsu:BSU32740; -.
DR PATRIC; fig|224308.179.peg.3547; -.
DR eggNOG; COG2011; Bacteria.
DR InParanoid; O32168; -.
DR OMA; MTWSEMQ; -.
DR PhylomeDB; O32168; -.
DR BioCyc; BSUB:BSU32740-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0006865; P:amino acid transport; IBA:GO_Central.
DR GO; GO:0048473; P:D-methionine transport; IBA:GO_Central.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR CDD; cd06261; TM_PBP2; 1.
DR Gene3D; 1.10.3720.10; -; 1.
DR InterPro; IPR000515; MetI-like.
DR InterPro; IPR035906; MetI-like_sf.
DR Pfam; PF00528; BPD_transp_1; 1.
DR SUPFAM; SSF161098; SSF161098; 1.
DR PROSITE; PS50928; ABC_TM1; 1.
PE 1: Evidence at protein level;
KW Amino-acid transport; Cell membrane; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..222
FT /note="Methionine import system permease protein MetP"
FT /id="PRO_0000383644"
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 73..93
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 97..117
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 195..215
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 18..212
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
SQ SEQUENCE 222 AA; 23756 MW; 7EA50D635BD2F261 CRC64;
MFEKYFPNVD LTELWNATYE TLYMTLISLL FAFVIGVILG LLLFLTSKGS LWQNKAVNSV
IAAVVNIFRS IPFLILIILL LGFTKFLVGT ILGPNAALPA LVIGSAPFYA RLVEIALREV
DKGVIEAAKS MGAKTSTIIF KVLIPESMPA LISGITVTAI ALIGSTAIAG AIGSGGLGNL
AYVEGYQSNN ADVTFVATVF ILIIVFIIQI IGDLITNIID KR
