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PTSBC_BACSU
ID   PTSBC_BACSU             Reviewed;         461 AA.
AC   P05306;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 3.
DT   03-AUG-2022, entry version 163.
DE   RecName: Full=PTS system sucrose-specific EIIBC component;
DE   AltName: Full=EIIBC-Scr;
DE            Short=EII-Scr;
DE   Includes:
DE     RecName: Full=Sucrose-specific phosphotransferase enzyme IIB component;
DE              EC=2.7.1.-;
DE     AltName: Full=PTS system sucrose-specific EIIB component;
DE   Includes:
DE     RecName: Full=Sucrose permease IIC component;
DE     AltName: Full=PTS system sucrose-specific EIIC component;
GN   Name=sacP; OrderedLocusNames=BSU38050; ORFNames=ipa-49d;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3122206; DOI=10.1073/pnas.84.24.8773;
RA   Fouet A., Arnaud M., Klier A., Rapoport G.;
RT   "Bacillus subtilis sucrose-specific enzyme II of the phosphotransferase
RT   system: expression in Escherichia coli and homology to enzymes II from
RT   enteric bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 84:8773-8777(1987).
RN   [2]
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   [3]
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   [4]
RP   SEQUENCE REVISION.
RX   PubMed=10568751; DOI=10.1101/gr.9.11.1116;
RA   Medigue C., Rose M., Viari A., Danchin A.;
RT   "Detecting and analyzing DNA sequencing errors: toward a higher quality of
RT   the Bacillus subtilis genome sequence.";
RL   Genome Res. 9:1116-1127(1999).
RN   [5]
RP   SEQUENCE REVISION TO 200 AND 202.
RX   PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA   Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA   Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT   "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT   168 reference genome a decade later.";
RL   Microbiology 155:1758-1775(2009).
CC   -!- FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase
CC       system (sugar PTS), a major carbohydrate active -transport system,
CC       catalyzes the phosphorylation of incoming sugar substrates
CC       concomitantly with their translocation across the cell membrane. This
CC       system is involved in sucrose transport. {ECO:0000250}.
CC   -!- FUNCTION: Acts as both a kinase and a phosphatase on SacT.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC       ProRule:PRU00426}; Multi-pass membrane protein {ECO:0000255|PROSITE-
CC       ProRule:PRU00426}.
CC   -!- DOMAIN: The EIIB domain is phosphorylated by phospho-EIIA on a
CC       cysteinyl or histidyl residue, depending on the transported sugar.
CC       Then, it transfers the phosphoryl group to the sugar substrate
CC       concomitantly with the sugar uptake processed by the EIIC domain.
CC   -!- DOMAIN: The EIIC domain forms the PTS system translocation channel and
CC       contains the specific substrate-binding site.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA22727.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=CAA51605.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; J03006; AAA22727.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; X73124; CAA51605.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; AL009126; CAB15831.3; -; Genomic_DNA.
DR   PIR; A39938; A39938.
DR   RefSeq; NP_391684.3; NC_000964.3.
DR   RefSeq; WP_003227426.1; NZ_JNCM01000034.1.
DR   AlphaFoldDB; P05306; -.
DR   SMR; P05306; -.
DR   STRING; 224308.BSU38050; -.
DR   TCDB; 4.A.1.2.9; the pts glucose-glucoside (glc) family.
DR   PaxDb; P05306; -.
DR   PRIDE; P05306; -.
DR   EnsemblBacteria; CAB15831; CAB15831; BSU_38050.
DR   GeneID; 937266; -.
DR   KEGG; bsu:BSU38050; -.
DR   PATRIC; fig|224308.179.peg.4119; -.
DR   eggNOG; COG1263; Bacteria.
DR   eggNOG; COG1264; Bacteria.
DR   OMA; EFGANPY; -.
DR   PhylomeDB; P05306; -.
DR   BioCyc; BSUB:BSU38050-MON; -.
DR   BRENDA; 2.7.1.211; 658.
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:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008982; F:protein-N(PI)-phosphohistidine-sugar phosphotransferase activity; IEA:InterPro.
DR   GO; GO:0090563; F:protein-phosphocysteine-sugar phosphotransferase activity; IBA:GO_Central.
DR   GO; GO:0090589; F:protein-phosphocysteine-trehalose phosphotransferase system transporter activity; IBA:GO_Central.
DR   GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IBA:GO_Central.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0015771; P:trehalose transport; IBA:GO_Central.
DR   CDD; cd00212; PTS_IIB_glc; 1.
DR   Gene3D; 3.30.1360.60; -; 1.
DR   InterPro; IPR036878; Glu_permease_IIB.
DR   InterPro; IPR018113; PTrfase_EIIB_Cys.
DR   InterPro; IPR003352; PTS_EIIC.
DR   InterPro; IPR013013; PTS_EIIC_1.
DR   InterPro; IPR001996; PTS_IIB_1.
DR   InterPro; IPR010973; PTS_IIBC_sucr.
DR   InterPro; IPR004719; PTS_maltose/Glc_sub_IIC.
DR   Pfam; PF00367; PTS_EIIB; 1.
DR   Pfam; PF02378; PTS_EIIC; 1.
DR   SUPFAM; SSF55604; SSF55604; 1.
DR   TIGRFAMs; TIGR00826; EIIB_glc; 1.
DR   TIGRFAMs; TIGR00852; pts-Glc; 1.
DR   TIGRFAMs; TIGR01996; PTS-II-BC-sucr; 1.
DR   PROSITE; PS51098; PTS_EIIB_TYPE_1; 1.
DR   PROSITE; PS01035; PTS_EIIB_TYPE_1_CYS; 1.
DR   PROSITE; PS51103; PTS_EIIC_TYPE_1; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Kinase; Membrane; Phosphotransferase system;
KW   Reference proteome; Sugar transport; Transferase; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..461
FT                   /note="PTS system sucrose-specific EIIBC component"
FT                   /id="PRO_0000186667"
FT   TRANSMEM        112..132
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT   TRANSMEM        148..168
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT   TRANSMEM        178..198
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT   TRANSMEM        208..228
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT   TRANSMEM        248..268
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT   TRANSMEM        289..309
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT   TRANSMEM        329..349
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT   TRANSMEM        359..379
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT   TRANSMEM        387..407
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT   TRANSMEM        430..450
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT   DOMAIN          1..87
FT                   /note="PTS EIIB type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00421"
FT   DOMAIN          107..461
FT                   /note="PTS EIIC type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT   ACT_SITE        26
FT                   /note="Phosphocysteine intermediate; for EIIB activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00421"
FT   CONFLICT        202
FT                   /note="P -> D (in Ref. 1; AAA22727 and 2; CAA51605)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   461 AA;  49397 MW;  BE51888438A9ABDC CRC64;
     MDYKETAKRL IELLGGKENI ISAAHCATRL RLVMKDESKI DQAQVEELDG VKGAFSSSGQ
     YQIIFGTGLV NKVFDAFSKE ADIEREEHVN HQDAAKEKLN PAARFAKTLS NIFVPIIPAI
     VASGLLMGLL GMINAFHWMS KDSALLQLLD MFSSAAFIFL PILIGVSASK EFGSNPYLGA
     VIGGIMIHPN LLNPWGLAEA TPDYMHLFGF DIALLGYQGT VIPVLLAVYV MSKVEKWTRK
     VVPHAVDLLV TPFVTVIVTG FVAFIAIGPL GRALGSGITV ALTYVYDHAG FVAGLIFGGT
     YSLIVLTGVH HSFHAIEAGL IADIGKNYLL PIWSMANVAQ GGAGLAVFFM AKKAKTKEIA
     LPAAFSAFLG ITEPVIFGVN LRYRKPFIAA MIGGALGGAY VVFTHVAANA YGLTGIPMIA
     IAAPFGFSNL IHYLIGMAIA AVSAFIAAFV MKINEDEERK K
 
 
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