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MELD_BACSU
ID   MELD_BACSU              Reviewed;         303 AA.
AC   O34706; Q795Q8;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Melibiose/raffinose/stachyose import permease protein MelD {ECO:0000305};
GN   Name=melD {ECO:0000303|PubMed:31138628}; Synonyms=amyD;
GN   OrderedLocusNames=BSU30280;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9387221; DOI=10.1099/00221287-143-11-3431;
RA   Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.;
RT   "Sequencing and functional annotation of the Bacillus subtilis genes in the
RT   200 kb rrnB-dnaB region.";
RL   Microbiology 143:3431-3441(1997).
RN   [2]
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   [3]
RP   FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, INDUCTION, AND DISRUPTION
RP   PHENOTYPE.
RC   STRAIN=168 / KM0;
RX   PubMed=31138628; DOI=10.1128/jb.00109-19;
RA   Morabbi Heravi K., Watzlawick H., Altenbuchner J.;
RT   "The melREDCA operon encodes a utilization system for the raffinose family
RT   of oligosaccharides in Bacillus subtilis.";
RL   J. Bacteriol. 201:E00109-E00109(2019).
CC   -!- FUNCTION: Part of the ABC transporter complex MelEDC-MsmX involved in
CC       melibiose, raffinose and stachyose import. Probably responsible for the
CC       translocation of the substrate across the membrane.
CC       {ECO:0000269|PubMed:31138628}.
CC   -!- SUBUNIT: The complex is composed of two ATP-binding proteins (MsmX),
CC       two transmembrane proteins (MelC and MelD) and a solute-binding protein
CC       (MelE). {ECO:0000269|PubMed:31138628}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:31138628};
CC       Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
CC   -!- INDUCTION: Repressed by the transcriptional regulator MelR. Induced by
CC       melibiose and raffinose. {ECO:0000269|PubMed:31138628}.
CC   -!- DISRUPTION PHENOTYPE: Deletion of the gene abolishes induction in the
CC       presence of melibiose and raffinose. {ECO:0000269|PubMed:31138628}.
CC   -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC       permease family. {ECO:0000305}.
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DR   EMBL; AF008220; AAC00385.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB15006.1; -; Genomic_DNA.
DR   PIR; E69585; E69585.
DR   RefSeq; NP_390906.1; NC_000964.3.
DR   RefSeq; WP_009968010.1; NZ_JNCM01000036.1.
DR   AlphaFoldDB; O34706; -.
DR   SMR; O34706; -.
DR   STRING; 224308.BSU30280; -.
DR   PaxDb; O34706; -.
DR   EnsemblBacteria; CAB15006; CAB15006; BSU_30280.
DR   GeneID; 937258; -.
DR   KEGG; bsu:BSU30280; -.
DR   PATRIC; fig|224308.179.peg.3284; -.
DR   eggNOG; COG1175; Bacteria.
DR   InParanoid; O34706; -.
DR   OMA; QSMSTFM; -.
DR   PhylomeDB; O34706; -.
DR   BioCyc; BSUB:BSU30280-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015774; P:polysaccharide transport; IEA:UniProtKB-KW.
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   Cell membrane; Membrane; Polysaccharide transport; Reference proteome;
KW   Sugar transport; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..303
FT                   /note="Melibiose/raffinose/stachyose import permease
FT                   protein MelD"
FT                   /id="PRO_0000387965"
FT   TRANSMEM        21..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        83..103
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        117..137
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        167..187
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        210..232
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        275..295
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          79..291
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
SQ   SEQUENCE   303 AA;  34163 MW;  C0AE12A5DB5D2737 CRC64;
     MSEIARDVHV KQVKPKKQSS LWWMYIPALL SVLVFMIYPF VKGTLITFTN WNGFSQVYQW
     VGFAQYERLF SDPDTWHILK NTLHYGLGST FFQNVVGLLY ALLLNQSIKT KAVTRTIVYL
     PVMISPLIMG YIWYFFFSYD GGALNDLLGV FGISPINALA SPSLNPWIIV MINTYQYVGI
     AMVVYLAGLQ SIPKDYYEAA QMDGAKQGQQ FFTITLPLLM PSITINIVIN IIGGLKLFDV
     IIALTAGGPG NASQSMSTFM YDLYFKRQDA GYAATQGIFM AFVILIISFC ALAYFKRKET
     EMS
 
 
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