NANC_ECO57
ID NANC_ECO57 Reviewed; 238 AA.
AC P69857; P39372;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Probable N-acetylneuraminic acid outer membrane channel protein NanC;
DE Short=Porin NanC;
DE Flags: Precursor;
GN Name=nanC; OrderedLocusNames=Z5907, ECs5270;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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=AAG59493.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB38693.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE005174; AAG59493.1; ALT_INIT; Genomic_DNA.
DR EMBL; BA000007; BAB38693.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_313297.2; NC_002695.1.
DR RefSeq; WP_001295734.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P69857; -.
DR SMR; P69857; -.
DR STRING; 155864.EDL933_5644; -.
DR EnsemblBacteria; AAG59493; AAG59493; Z5907.
DR EnsemblBacteria; BAB38693; BAB38693; ECs_5270.
DR GeneID; 66671806; -.
DR GeneID; 913696; -.
DR KEGG; ece:Z5907; -.
DR KEGG; ecs:ECs_5270; -.
DR PATRIC; fig|386585.9.peg.5504; -.
DR eggNOG; COG1452; Bacteria.
DR HOGENOM; CLU_081853_2_0_6; -.
DR OMA; YFKRNSG; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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; Reference proteome;
KW Signal; Sugar transport; Transmembrane; Transmembrane beta strand;
KW 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_0000016602"
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; 27888 MW; 52B992EF95AD62F7 CRC64;
MKKAKILSGV LLLCFSSPLI SQAATLDVRG GYRSGSHAYE TRLKVSEGWQ NGWWASMESN
TWNTIHDNKK ENAALNDVQV EVNYAIKLDD QWTVRPGMLT HFSSNGTRYG PYVKLSWDAT
KDLNFGIRYR YDWKAYRQQD LSGDMSRDNV HRWDGYVTYH INSDFTFAWQ TTLYSKQNDY
RYANHKKWAT ENAFVLQYHM TPDITPYIEY DYLDRQGVYN GRDNLSENSY RIGVSFKL
