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ASPP_BACSU
ID   ASPP_BACSU              Reviewed;         520 AA.
AC   O07002;
DT   01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=Aspartate-proton symporter;
DE   AltName: Full=L-aspartate transporter;
GN   Name=yveA; OrderedLocusNames=BSU34470;
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;
RA   Denizot F.;
RL   Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
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   INDUCTION.
RX   PubMed=11739774; DOI=10.1099/00221287-147-12-3413;
RA   Pereira Y., Petit-Glatron M.-F., Chambert R.;
RT   "yveB, encoding endolevanase LevB, is part of the sacB-yveB-yveA
RT   levansucrase tricistronic operon in Bacillus subtilis.";
RL   Microbiology 147:3413-3419(2001).
RN   [4]
RP   CHARACTERIZATION.
RC   STRAIN=168;
RX   PubMed=12730183; DOI=10.1128/jb.185.10.3218-3222.2003;
RA   Lorca G., Winnen B., Saier M.H. Jr.;
RT   "Identification of the L-aspartate transporter in Bacillus subtilis.";
RL   J. Bacteriol. 185:3218-3222(2003).
CC   -!- FUNCTION: Uptake of L-aspartate with the concomitant import of a
CC       proton. Can also transport aspartate hydroxamate and L-glutamate with
CC       lower affinity and efficiency.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- INDUCTION: Induced by sucrose. {ECO:0000269|PubMed:11739774}.
CC   -!- MISCELLANEOUS: Allows enhanced growth with L-aspartate as a sole source
CC       nitrogen source.
CC   -!- MISCELLANEOUS: Inhibited by carbonyl cyanide m-chlorophenylhydrazone
CC       and carbonyl cyanide 4-trifluoro-methoxyphenylhydrazone.
CC   -!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC)
CC       superfamily. AGT (TC 2.A.3.11) family. {ECO:0000305}.
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DR   EMBL; Z94043; CAB08050.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB15452.1; -; Genomic_DNA.
DR   PIR; D70035; D70035.
DR   RefSeq; NP_391327.1; NC_000964.3.
DR   RefSeq; WP_003228228.1; NZ_JNCM01000033.1.
DR   AlphaFoldDB; O07002; -.
DR   SMR; O07002; -.
DR   STRING; 224308.BSU34470; -.
DR   TCDB; 2.A.3.11.1; the amino acid-polyamine-organocation (apc) family.
DR   PaxDb; O07002; -.
DR   PRIDE; O07002; -.
DR   EnsemblBacteria; CAB15452; CAB15452; BSU_34470.
DR   GeneID; 938612; -.
DR   KEGG; bsu:BSU34470; -.
DR   PATRIC; fig|224308.179.peg.3734; -.
DR   eggNOG; COG0531; Bacteria.
DR   InParanoid; O07002; -.
DR   OMA; PCTATIV; -.
DR   PhylomeDB; O07002; -.
DR   BioCyc; BSUB:BSU34470-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:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR   GO; GO:0006865; P:amino acid transport; IEA:UniProtKB-KW.
DR   InterPro; IPR002293; AA/rel_permease1.
DR   Pfam; PF13520; AA_permease_2; 1.
PE   1: Evidence at protein level;
KW   Amino-acid transport; Cell membrane; Membrane; Reference proteome; Symport;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..520
FT                   /note="Aspartate-proton symporter"
FT                   /id="PRO_0000054283"
FT   TRANSMEM        13..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        49..69
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        85..105
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        130..150
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        161..181
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        201..221
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        232..252
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        281..301
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        345..365
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        366..386
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        402..422
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        425..445
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        460..480
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        482..502
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   520 AA;  56989 MW;  0583CB56FE6D37D9 CRC64;
     MSKQGNFQKS MSLFDLILIG MGAIFGSAWL FAVSNVASKA GPSGAFSWIL GGAIILLIGL
     VYAELGAALP RTGGIIRYPV YSHGHLVGYL ISFVTIVAYT SLISIEVTAV RQYVAYWFPG
     LTIKGSDSPT ISGWILQFAL LCLFFLLNYW SVKTFAKANF IISIFKYIVP ITIIIVLIFH
     FQPENLSVQG FAPFGFTGIQ AAISTGGVMF AYLGLHPIVS VAGEVQNPKR NIPIALIICI
     IVSTIIYTVL QVTFIGAIPT ETLKHGWPAI GREFSLPFKD IAVMLGLGWL ATLVILDAIL
     SPGGNGNIFM NTTSRLVYAW ARNGTLFGIF SKVNKDTGTP RASLWLSFAL SIFWTLPFPS
     WNALVNVCSV ALILSYAIAP ISSAALRVNA KDLNRPFYLK GMSIIGPLSF IFTAFIVYWS
     GWKTVSWLLG SQLVMFLIYL CFSKYTPKED VSLAQQLKSA WWLIGFYIMM LIFSYIGSFG
     HGLGIISNPV DLILVAIGSL AIYYWAKYTG LPKAAIDYDK
 
 
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