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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
 
 
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