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PTFC_BACAM
ID   PTFC_BACAM              Reviewed;         304 AA.
AC   P41029;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Fructose permease IIC component;
DE   AltName: Full=PTS system fructose-specific EIIC component;
DE   Flags: Fragment;
GN   Name=fruA;
OS   Bacillus amyloliquefaciens (Bacillus velezensis).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus amyloliquefaciens group.
OX   NCBI_TaxID=1390;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 23844 / P;
RX   PubMed=7578273; DOI=10.1016/0167-4889(95)00101-w;
RA   Hoang V., Hofemeister J.;
RT   "Bacillus amyloliquefaciens possesses a second type I signal peptidase with
RT   extensive sequence similarity to other Bacillus SPases.";
RL   Biochim. Biophys. Acta 1269:64-68(1995).
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. This system is involved in
CC       fructose transport (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC       ProRule:PRU00427}; Multi-pass membrane protein {ECO:0000255|PROSITE-
CC       ProRule:PRU00427}.
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; Z33640; CAA83920.1; -; Genomic_DNA.
DR   PIR; S59965; S59965.
DR   AlphaFoldDB; P41029; -.
DR   STRING; 692420.BAMF_1514; -.
DR   PRIDE; P41029; -.
DR   eggNOG; COG1299; Bacteria.
DR   eggNOG; COG1445; Bacteria.
DR   eggNOG; COG1762; Bacteria.
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:0005351; F:carbohydrate:proton symporter activity; IEA:InterPro.
DR   GO; GO:0008982; F:protein-N(PI)-phosphohistidine-sugar phosphotransferase activity; IEA:InterPro.
DR   GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR   InterPro; IPR013014; PTS_EIIC_2.
DR   InterPro; IPR006327; PTS_IIC_fruc.
DR   TIGRFAMs; TIGR01427; PTS_IIC_fructo; 1.
DR   PROSITE; PS51104; PTS_EIIC_TYPE_2; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Membrane; Phosphotransferase system; Sugar transport;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           <1..304
FT                   /note="Fructose permease IIC component"
FT                   /id="PRO_0000186507"
FT   TRANSMEM        20..40
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT   TRANSMEM        62..82
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT   TRANSMEM        98..118
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT   TRANSMEM        140..160
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT   TRANSMEM        181..201
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT   TRANSMEM        214..234
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT   TRANSMEM        238..258
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT   TRANSMEM        277..297
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT   DOMAIN          <1..304
FT                   /note="PTS EIIC type-2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT   NON_TER         1
SQ   SEQUENCE   304 AA;  31736 MW;  6FE90E921A7CF489 CRC64;
     IHSADPKDPT YNTFAAALNF IGSDNALKLI VAVLAGFIAM SIADRPGFAP GMVGGFMATQ
     ANAGFLGGLI AGFLAGYVVI LLKKLFVFIP QSLDGLKPVL IYPLLGIFIT GVLMQFVINT
     PVAAFMNFLT NWLESLGTGN LVLMGIILGG MMAIDMGGPL NKAAFTFGIA MIDAGNYAPH
     AAIMAGGMVP PLGIALATTF FRHKFSKRDR EAGITCYFMG AAFVTEGAIP FAAADLRVIP
     AAVIGSAVAG GLTEFFRVTL PAPHGGVFVA FITNHPLLYL LSIVIGAIVT AVILGIIKKP
     VEEK
 
 
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