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PTKC_ECOLI
ID   PTKC_ECOLI              Reviewed;         451 AA.
AC   P69831; P37189; P76411;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=PTS system galactitol-specific EIIC component {ECO:0000303|PubMed:7772602};
DE   AltName: Full=EIIC-Gat {ECO:0000303|PubMed:7772602};
DE   AltName: Full=Galactitol permease IIC component {ECO:0000303|PubMed:7772602};
GN   Name=gatC; OrderedLocusNames=b2092, JW2076;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=EC3132;
RX   PubMed=7772602; DOI=10.1016/0167-4781(95)00053-j;
RA   Nobelmann B., Lengeler J.W.;
RT   "Sequence of the gat operon for galactitol utilization from a wild-type
RT   strain EC3132 of Escherichia coli.";
RL   Biochim. Biophys. Acta 1262:69-72(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA   Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA   Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA   Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA   Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA   Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA   Horiuchi T.;
RT   "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT   the 40.1-50.0 min region on the linkage map.";
RL   DNA Res. 3:379-392(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [4]
RP   SEQUENCE REVISION.
RC   STRAIN=K12 / MG1655 / ATCC 700926;
RX   PubMed=22081388; DOI=10.1128/jb.06087-11;
RA   Freddolino P.L., Amini S., Tavazoie S.;
RT   "Newly identified genetic variations in common Escherichia coli MG1655
RT   stock cultures.";
RL   J. Bacteriol. 194:303-306(2012).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [6]
RP   SUBUNIT, AND SUBCELLULAR LOCATION.
RC   STRAIN=BL21-DE3;
RX   PubMed=16079137; DOI=10.1074/jbc.m506479200;
RA   Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L.,
RA   von Heijne G., Daley D.O.;
RT   "Protein complexes of the Escherichia coli cell envelope.";
RL   J. Biol. Chem. 280:34409-34419(2005).
RN   [7]
RP   SUBCELLULAR LOCATION.
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=15919996; DOI=10.1126/science.1109730;
RA   Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT   "Global topology analysis of the Escherichia coli inner membrane
RT   proteome.";
RL   Science 308:1321-1323(2005).
RN   [8]
RP   FUNCTION, AND INDUCTION.
RX   PubMed=8955298; DOI=10.1128/jb.178.23.6790-6795.1996;
RA   Nobelmann B., Lengeler J.W.;
RT   "Molecular analysis of the gat genes from Escherichia coli and of their
RT   roles in galactitol transport and metabolism.";
RL   J. Bacteriol. 178:6790-6795(1996).
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. The enzyme II complex composed
CC       of GatA, GatB and GatC is involved in galactitol transport.
CC       {ECO:0000269|PubMed:8955298}.
CC   -!- SUBUNIT: Forms a complex with one each of subunit of GatA, GatB and 2
CC       subunits of GatC. {ECO:0000269|PubMed:16079137}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|PROSITE-
CC       ProRule:PRU00427, ECO:0000269|PubMed:15919996,
CC       ECO:0000269|PubMed:16079137}; Multi-pass membrane protein
CC       {ECO:0000255|PROSITE-ProRule:PRU00427, ECO:0000269|PubMed:15919996,
CC       ECO:0000269|PubMed:16079137}.
CC   -!- INDUCTION: Constitutively expressed. {ECO:0000269|PubMed:8955298}.
CC   -!- DOMAIN: The EIIC domain forms the PTS system translocation channel and
CC       contains the specific substrate-binding site. {ECO:0000255|PROSITE-
CC       ProRule:PRU00427}.
CC   -!- CAUTION: A pseudogene in strain MG1655 / ATCC 700926 due to a recent
CC       laboratory-derived single nucleotide insertion, but not its parent
CC       MG1655 / ATCC 47076. {ECO:0000305|PubMed:22081388}.
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DR   EMBL; X79837; CAA56230.1; -; Genomic_DNA.
DR   EMBL; U00096; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AP009048; BAA15955.1; -; Genomic_DNA.
DR   PIR; C64976; C64976.
DR   PIR; S55905; S55905.
DR   RefSeq; WP_000490679.1; NZ_STEB01000002.1.
DR   AlphaFoldDB; P69831; -.
DR   BioGRID; 4260430; 14.
DR   ComplexPortal; CPX-5942; Galactitol-specific enzyme II complex.
DR   STRING; 316407.1736809; -.
DR   TCDB; 4.A.5.1.1; the pts galactitol (gat) family.
DR   jPOST; P69831; -.
DR   PaxDb; P69831; -.
DR   PRIDE; P69831; -.
DR   EnsemblBacteria; BAA15955; BAA15955; BAA15955.
DR   KEGG; ecj:JW2076; -.
DR   PATRIC; fig|1411691.4.peg.158; -.
DR   EchoBASE; EB2315; -.
DR   eggNOG; COG3775; Bacteria.
DR   HOGENOM; CLU_040393_0_0_6; -.
DR   InParanoid; P69831; -.
DR   OMA; VFDMGWP; -.
DR   PhylomeDB; P69831; -.
DR   BioCyc; MetaCyc:MON-124142; -.
DR   BRENDA; 2.7.1.200; 2026.
DR   PRO; PR:P69831; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:1902495; C:transmembrane transporter complex; IC:ComplexPortal.
DR   GO; GO:0015577; F:galactitol transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0019402; P:galactitol metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0015796; P:galactitol transmembrane transport; IC:ComplexPortal.
DR   GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IC:ComplexPortal.
DR   InterPro; IPR013853; GatC.
DR   InterPro; IPR013014; PTS_EIIC_2.
DR   InterPro; IPR004703; PTS_sugar-sp_permease.
DR   PANTHER; PTHR37324; PTHR37324; 1.
DR   Pfam; PF03611; EIIC-GAT; 1.
DR   PIRSF; PIRSF006304; GatC; 1.
DR   TIGRFAMs; TIGR00827; EIIC-GAT; 1.
DR   PROSITE; PS51104; PTS_EIIC_TYPE_2; 1.
PE   1: Evidence at protein level;
KW   Cell inner membrane; Cell membrane; Galactitol metabolism; Membrane;
KW   Phosphotransferase system; Reference proteome; Sugar transport;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..451
FT                   /note="PTS system galactitol-specific EIIC component"
FT                   /id="PRO_0000186570"
FT   TRANSMEM        9..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT   TRANSMEM        41..61
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT   TRANSMEM        92..112
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT   TRANSMEM        138..158
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT   TRANSMEM        218..238
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT   TRANSMEM        305..325
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT   TRANSMEM        329..349
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT   TRANSMEM        357..377
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT   TRANSMEM        392..412
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT   TRANSMEM        415..435
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT   DOMAIN          6..435
FT                   /note="PTS EIIC type-2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT   CONFLICT        187..203
FT                   /note="MGPIAVLVDAIIEKIPG -> LGPNCGAGGCYHRENPS (in Ref. 1;
FT                   CAA56230)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        399..451
FT                   /note="QGGSPITWLLIQVFSPQNIPGFIIIGAIYLTGIFMTWRRARGFIKQEKVVLA
FT                   E -> TGRFSHYLVTDSGFSPQIFPVSLLSAQFI (in Ref. 1; CAA56230)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   451 AA;  48365 MW;  B843BB6BDE721F13 CRC64;
     MFSEVMRYIL DLGPTVMLPI VIIIFSKILG MKAGDCFKAG LHIGIGFVGI GLVIGLMLDS
     IGPAAKAMAE NFDLNLHVVD VGWPGSSPMT WASQIALVAI PIAILVNVAM LLTRMTRVVN
     VDIWNIWHMT FTGALLHLAT GSWMIGMAGV VIHAAFVYKL GDWFARDTRN FFELEGIAIP
     HGTSAYMGPI AVLVDAIIEK IPGVNRIKFS ADDIQRKFGP FGEPVTVGFV MGLIIGILAG
     YDVKGVLQLA VKTAAVMLLM PRVIKPIMDG LTPIAKQARS RLQAKFGGQE FLIGLDPALL
     LGHTAVVSAS LIFIPLTILI AVCVPGNQVL PFGDLATIGF FVAMAVAVHR GNLFRTLISG
     VIIMSITLWI ATQTIGLHTQ LAANAGALKA GGMVASMDQG GSPITWLLIQ VFSPQNIPGF
     IIIGAIYLTG IFMTWRRARG FIKQEKVVLA E
 
 
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