NANC_SHIFL
ID NANC_SHIFL Reviewed; 238 AA.
AC P69858; P39372;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=Probable N-acetylneuraminic acid outer membrane channel protein NanC;
DE Short=Porin NanC;
DE Flags: Precursor;
GN Name=nanC; OrderedLocusNames=SF4211, S4468;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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=AAN45631.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAP19417.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE005674; AAN45631.2; ALT_INIT; Genomic_DNA.
DR EMBL; AE014073; AAP19417.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_001295734.1; NZ_WPGW01000210.1.
DR AlphaFoldDB; P69858; -.
DR SMR; P69858; -.
DR STRING; 198214.SF4211; -.
DR EnsemblBacteria; AAN45631; AAN45631; SF4211.
DR EnsemblBacteria; AAP19417; AAP19417; S4468.
DR GeneID; 66671806; -.
DR KEGG; sfx:S4468; -.
DR PATRIC; fig|623.156.peg.2789; -.
DR HOGENOM; CLU_081853_2_0_6; -.
DR OrthoDB; 1240612at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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_0000016604"
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
