NANC_ECOLI
ID NANC_ECOLI Reviewed; 238 AA.
AC P69856; P39372; Q2M602;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Probable N-acetylneuraminic acid outer membrane channel protein NanC;
DE AltName: Full=NanR-regulated channel;
DE AltName: Full=Porin NanC;
DE Flags: Precursor;
GN Name=nanC; Synonyms=yjhA; OrderedLocusNames=b4311, JW5778;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
RN [2]
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 [3]
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 [4]
RP FUNCTION, AND TRANSCRIPTIONAL REGULATION.
RX PubMed=15743943; DOI=10.1128/jb.187.6.1959-1965.2005;
RA Condemine G., Berrier C., Plumbridge J., Ghazi A.;
RT "Function and expression of an N-acetylneuraminic acid-inducible outer
RT membrane channel in Escherichia coli.";
RL J. Bacteriol. 187:1959-1965(2005).
RN [5]
RP INDUCTION.
RX PubMed=23935044; DOI=10.1128/jb.00692-13;
RA Kalivoda K.A., Steenbergen S.M., Vimr E.R.;
RT "Control of the Escherichia coli sialoregulon by transcriptional repressor
RT NanR.";
RL J. Bacteriol. 195:4689-4701(2013).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 24-238, TOPOLOGY, AND SUBUNIT.
RX PubMed=19796645; DOI=10.1016/j.jmb.2009.09.054;
RA Wirth C., Condemine G., Boiteux C., Berneche S., Schirmer T., Peneff C.M.;
RT "NanC crystal structure, a model for outer-membrane channels of the acidic
RT sugar-specific KdgM porin family.";
RL J. Mol. Biol. 394:718-731(2009).
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 (Probable). NanC proteins form high-
CC conductance channels which are open at low membrane potentials and
CC which have a weak anion selectivity. {ECO:0000269|PubMed:15743943,
CC ECO:0000305}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:19796645}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane.
CC -!- INDUCTION: Induced by N-acetylneuraminate and modulated by N-
CC acetylglucosamine. This regulation occurs via the NanR and NagC
CC regulators. NanC expression is also activated by the regulators cyclic
CC AMP-catabolite activator protein, OmpR, and CpxR.
CC {ECO:0000269|PubMed:15743943, ECO:0000269|PubMed:23935044}.
CC -!- SIMILARITY: Belongs to the oligogalacturonate-specific porin KdgM (TC
CC 1.B.35) family. NanC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA97207.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U14003; AAA97207.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC77267.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE78304.1; -; Genomic_DNA.
DR PIR; S56536; S56536.
DR RefSeq; NP_418731.2; NC_000913.3.
DR RefSeq; WP_001295734.1; NZ_SSZK01000071.1.
DR PDB; 2WJQ; X-ray; 2.00 A; A=24-238.
DR PDB; 2WJR; X-ray; 1.80 A; A=25-238.
DR PDBsum; 2WJQ; -.
DR PDBsum; 2WJR; -.
DR AlphaFoldDB; P69856; -.
DR SMR; P69856; -.
DR BioGRID; 4259375; 217.
DR STRING; 511145.b4311; -.
DR DrugBank; DB04147; Dodecyldimethylamine N-oxide.
DR TCDB; 1.B.35.2.1; the oligogalacturonate-specific porin (kdgm) family.
DR PaxDb; P69856; -.
DR PRIDE; P69856; -.
DR EnsemblBacteria; AAC77267; AAC77267; b4311.
DR EnsemblBacteria; BAE78304; BAE78304; BAE78304.
DR GeneID; 66671806; -.
DR GeneID; 946843; -.
DR KEGG; ecj:JW5778; -.
DR KEGG; eco:b4311; -.
DR PATRIC; fig|1411691.4.peg.2382; -.
DR EchoBASE; EB2290; -.
DR eggNOG; COG1452; Bacteria.
DR HOGENOM; CLU_081853_2_0_6; -.
DR OMA; YFKRNSG; -.
DR PhylomeDB; P69856; -.
DR BioCyc; EcoCyc:G7921-MON; -.
DR BioCyc; MetaCyc:G7921-MON; -.
DR EvolutionaryTrace; P69856; -.
DR PRO; PR:P69856; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0045203; C:integral component of cell outer membrane; IDA:EcoliWiki.
DR GO; GO:0046930; C:pore complex; IEA:UniProtKB-KW.
DR GO; GO:0015478; F:oligosaccharide transporting porin activity; IMP:EcoliWiki.
DR GO; GO:0015288; F:porin activity; IMP:EcoliWiki.
DR GO; GO:0015136; F:sialic acid transmembrane transporter activity; IMP:EcoliWiki.
DR GO; GO:0015772; P:oligosaccharide transport; IMP:EcoliWiki.
DR InterPro; IPR009331; Oligogalacturonate-sp_porin.
DR PANTHER; PTHR38105; PTHR38105; 1.
DR Pfam; PF06178; KdgM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell outer membrane; Ion transport; Membrane; Porin;
KW Reference proteome; Signal; Sugar transport; Transmembrane;
KW 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_0000016601"
FT TOPO_DOM 24
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:19796645"
FT TRANSMEM 25..33
FT TOPO_DOM 34..37
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:19796645"
FT TRANSMEM 38..48
FT TOPO_DOM 49..52
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:19796645"
FT TRANSMEM 53..64
FT TOPO_DOM 65..75
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:19796645"
FT TRANSMEM 76..87
FT TOPO_DOM 88..91
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:19796645"
FT TRANSMEM 92..102
FT TOPO_DOM 103..105
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:19796645"
FT TRANSMEM 106..118
FT TOPO_DOM 119..122
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:19796645"
FT TRANSMEM 123..134
FT TOPO_DOM 135..149
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:19796645"
FT TRANSMEM 150..160
FT TOPO_DOM 161..164
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:19796645"
FT TRANSMEM 165..176
FT TOPO_DOM 177..187
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:19796645"
FT TRANSMEM 188..198
FT TOPO_DOM 199..203
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:19796645"
FT TRANSMEM 204..212
FT TOPO_DOM 213..227
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:19796645"
FT TRANSMEM 228..236
FT TOPO_DOM 237..238
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:19796645"
FT STRAND 26..33
FT /evidence="ECO:0007829|PDB:2WJR"
FT TURN 34..37
FT /evidence="ECO:0007829|PDB:2WJR"
FT STRAND 38..48
FT /evidence="ECO:0007829|PDB:2WJR"
FT STRAND 52..64
FT /evidence="ECO:0007829|PDB:2WJR"
FT STRAND 77..84
FT /evidence="ECO:0007829|PDB:2WJR"
FT STRAND 86..103
FT /evidence="ECO:0007829|PDB:2WJR"
FT STRAND 106..120
FT /evidence="ECO:0007829|PDB:2WJR"
FT STRAND 123..136
FT /evidence="ECO:0007829|PDB:2WJR"
FT STRAND 150..160
FT /evidence="ECO:0007829|PDB:2WJR"
FT STRAND 162..179
FT /evidence="ECO:0007829|PDB:2WJR"
FT STRAND 185..198
FT /evidence="ECO:0007829|PDB:2WJR"
FT STRAND 200..212
FT /evidence="ECO:0007829|PDB:2WJR"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:2WJR"
FT STRAND 222..225
FT /evidence="ECO:0007829|PDB:2WJR"
FT STRAND 228..236
FT /evidence="ECO:0007829|PDB:2WJR"
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
