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NANC_ECOL6
ID   NANC_ECOL6              Reviewed;         238 AA.
AC   Q8CVG4;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 2.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Probable N-acetylneuraminic acid outer membrane channel protein NanC;
DE            Short=Porin NanC;
DE   Flags: Precursor;
GN   Name=nanC; OrderedLocusNames=c5389;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: Outer membrane channel protein allowing the entry of N-
CC       acetylneuraminic acid (Neu5Ac, the most abundant sialic acid on host
CC       cell surfaces) into the bacteria. NanC proteins form high-conductance
CC       channels which are open at low membrane potentials and which have a
CC       weak anion selectivity (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the oligogalacturonate-specific porin KdgM (TC
CC       1.B.35) family. NanC subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAN83811.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE014075; AAN83811.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_001304536.1; NC_004431.1.
DR   AlphaFoldDB; Q8CVG4; -.
DR   SMR; Q8CVG4; -.
DR   STRING; 199310.c5389; -.
DR   EnsemblBacteria; AAN83811; AAN83811; c5389.
DR   KEGG; ecc:c5389; -.
DR   eggNOG; COG1452; Bacteria.
DR   HOGENOM; CLU_081853_2_0_6; -.
DR   OMA; YFKRNSG; -.
DR   Proteomes; UP000001410; Chromosome.
DR   GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046930; C:pore complex; IEA:UniProtKB-KW.
DR   GO; GO:0015288; F:porin activity; IEA:UniProtKB-KW.
DR   GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR   GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR   InterPro; IPR009331; Oligogalacturonate-sp_porin.
DR   PANTHER; PTHR38105; PTHR38105; 1.
DR   Pfam; PF06178; KdgM; 1.
PE   3: Inferred from homology;
KW   Cell outer membrane; Ion transport; Membrane; Porin; Signal;
KW   Sugar transport; Transmembrane; Transmembrane beta strand; Transport.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..238
FT                   /note="Probable N-acetylneuraminic acid outer membrane
FT                   channel protein NanC"
FT                   /id="PRO_0000016603"
FT   TOPO_DOM        24
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        25..33
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        34..37
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        38..48
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        49..52
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        53..64
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        65..75
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        76..87
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        88..91
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        92..102
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        103..105
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        106..118
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        119..122
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        123..134
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        135..149
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        150..160
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        161..164
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        165..176
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        177..187
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        188..198
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        199..203
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        204..212
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        213..227
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        228..236
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        237..238
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   238 AA;  27902 MW;  07B99134FEC0D42C CRC64;
     MKKAKILSGV LLLCFSSPLI SQAATLDVRG GYRSGSHAYE TRLKVSEGWQ NGWWASMESN
     TWNTIHDNKK ENAALNDVQV EVNYAIKLDD QWTVRPGMLT HFSSNGTRYG PYVKLSWDAT
     KDLKFGIRYR YDWKAYRQQD LSGDMSRDNV HRWDGYVTYH INSDFTFAWQ TTLYSKQNDY
     RYANHKKWAT ENAFVLQYHM TPDITPYIEY DYLDRQGVYN GRDNLSENSY RIGVSFKL
 
 
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