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YWBA_BACSU
ID   YWBA_BACSU              Reviewed;         444 AA.
AC   P39584;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=Putative permease IIC component YwbA;
DE   AltName: Full=Putative PTS system EIIC component;
GN   Name=ywbA; OrderedLocusNames=BSU38390; ORFNames=ipa-16d;
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=7934828; DOI=10.1111/j.1365-2958.1993.tb01963.x;
RA   Glaser P., Kunst F., Arnaud M., Coudart M.P., Gonzales W., Hullo M.-F.,
RA   Ionescu M., Lubochinsky B., Marcelino L., Moszer I., Presecan E.,
RA   Santana M., Schneider E., Schweizer J., Vertes A., Rapoport G., Danchin A.;
RT   "Bacillus subtilis genome project: cloning and sequencing of the 97 kb
RT   region from 325 degrees to 333 degrees.";
RL   Mol. Microbiol. 10:371-384(1993).
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).
CC   -!- FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase
CC       system (PTS), a major carbohydrate active -transport system, catalyzes
CC       the phosphorylation of incoming sugar substrates concomitant with their
CC       translocation across the cell membrane. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC       ProRule:PRU00428}; Multi-pass membrane protein {ECO:0000255|PROSITE-
CC       ProRule:PRU00428}.
CC   -!- DOMAIN: The EIIC domain forms the PTS system translocation channel and
CC       contains the specific substrate-binding site.
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DR   EMBL; X73124; CAA51572.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB15865.1; -; Genomic_DNA.
DR   PIR; S39671; S39671.
DR   RefSeq; NP_391718.1; NC_000964.3.
DR   RefSeq; WP_003242539.1; NZ_JNCM01000034.1.
DR   AlphaFoldDB; P39584; -.
DR   SMR; P39584; -.
DR   STRING; 224308.BSU38390; -.
DR   PaxDb; P39584; -.
DR   PRIDE; P39584; -.
DR   EnsemblBacteria; CAB15865; CAB15865; BSU_38390.
DR   GeneID; 937331; -.
DR   KEGG; bsu:BSU38390; -.
DR   PATRIC; fig|224308.179.peg.4155; -.
DR   eggNOG; COG1455; Bacteria.
DR   InParanoid; P39584; -.
DR   OMA; ASFDIMA; -.
DR   PhylomeDB; P39584; -.
DR   BioCyc; BSUB:BSU38390-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:0008982; F:protein-N(PI)-phosphohistidine-sugar phosphotransferase activity; IEA:InterPro.
DR   GO; GO:1901264; P:carbohydrate derivative transport; IBA:GO_Central.
DR   GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:InterPro.
DR   InterPro; IPR003352; PTS_EIIC.
DR   InterPro; IPR004501; PTS_EIIC_3.
DR   InterPro; IPR004796; PTS_IIC_cello.
DR   Pfam; PF02378; PTS_EIIC; 1.
DR   PIRSF; PIRSF006351; PTS_EIIC-Cellobiose; 1.
DR   TIGRFAMs; TIGR00359; cello_pts_IIC; 1.
DR   TIGRFAMs; TIGR00410; lacE; 1.
DR   PROSITE; PS51105; PTS_EIIC_TYPE_3; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Membrane; Reference proteome; Sugar transport; Transferase;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..444
FT                   /note="Putative permease IIC component YwbA"
FT                   /id="PRO_0000186712"
FT   TRANSMEM        31..51
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
FT   TRANSMEM        72..92
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
FT   TRANSMEM        104..124
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
FT   TRANSMEM        138..158
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
FT   TRANSMEM        187..207
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
FT   TRANSMEM        223..243
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
FT   TRANSMEM        246..266
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
FT   TRANSMEM        291..311
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
FT   TRANSMEM        349..371
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
FT   TRANSMEM        402..422
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
FT   DOMAIN          8..421
FT                   /note="PTS EIIC type-3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
SQ   SEQUENCE   444 AA;  47648 MW;  D3964B3795274C7D CRC64;
     MSTFTRVMEE KIMPVAGKIA GQRHLSALRD GIILTMPLII IGSVFLILTS LPIPGYADFM
     ASVFGNEWAD KLGYPVNASF DIMAMIAAFG IAYRLAESYG VDALSAGAIS IAAFLLATPF
     EVPFTPHGST ESIMVGGGIP ITLLGSKGLF VAMLIALFST EIYRYIIQKN IVFKMPDGVP
     PAVSKSFVAL IPGFIIVLLV WLARLLIEMT PFQSLHNVVG DLLGTPLSIL GGSLGGSLIA
     EFVQMLLWSC GIHGASIIGG IMAPIWYGAM DANRLAFQAG EALPSIFTTQ FFQIWINVGG
     SGATLALVLT MLVRSRSKQM KQLGRLGIGP ALFNINEPII FGMPIVMNPL LIVPFIIAPL
     LTITATYIGM STGLVARPAG IAVPWTMPPL ISGYLATGGK VSGAVMQLVN LLITCAIYYP
     FFRIWDHQKW REESAVESGD KNVM
 
 
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