ID NANX_ECOLI Reviewed; 405 AA.
AC P39352; Q2M633;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 27-MAR-2024, entry version 151.
DE RecName: Full=Sialic acid transporter NanX {ECO:0000305};
GN Name=nanX {ECO:0000303|PubMed:32669363}; Synonyms=yjhB;
GN OrderedLocusNames=b4279, JW5768;
OS Escherichia coli (strain K12).
OC Bacteria; Pseudomonadota; 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 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 [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=32542330; DOI=10.1042/bsr20200927;
RA Kentache T., Thabault L., Peracchi A., Frederick R., Bommer G.T.,
RA Van Schaftingen E.;
RT "The putative Escherichia coli dehydrogenase YjhC metabolises two
RT dehydrated forms of N-acetylneuraminate produced by some sialidases.";
RL Biosci. Rep. 40:0-0(2020).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / BW25113;
RX PubMed=32669363; DOI=10.1074/jbc.ra120.014454;
RA Bell A., Severi E., Lee M., Monaco S., Latousakis D., Angulo J.,
RA Thomas G.H., Naismith J.H., Juge N.;
RT "Uncovering a novel molecular mechanism for scavenging sialic acids in
RT bacteria.";
RL J. Biol. Chem. 295:13724-13736(2020).
CC -!- FUNCTION: Probably transports across the inner membrane the two
CC dehydrated forms of N-acetylneuraminate (Neu5Ac), 2,7-anhydro-N-
CC acetylneuraminate (2,7-AN) and 2-deoxy-2,3-didehydro-N-
CC acetylneuraminate (2,3-EN). {ECO:0000269|PubMed:32542330,
CC ECO:0000269|PubMed:32669363}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000305|PubMed:32542330}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- INDUCTION: Negatively regulated by the transcriptional repressor NanR.
CC Induced by N-acetylneuraminate, via inactivation of NanR.
CC {ECO:0000269|PubMed:23935044}.
CC -!- DISRUPTION PHENOTYPE: Inactivation of the gene in NanR-deficient cells
CC prevents the growth on 2,7-AN and 2,3-EN (PubMed:32542330). Deletion of
CC the gene in strain BW25113 results in loss of growth on 2,7-AN but not
CC on Neu5Ac (PubMed:32669363). {ECO:0000269|PubMed:32542330,
CC ECO:0000269|PubMed:32669363}.
CC -!- MISCELLANEOUS: Bell et al. show that this transporter allows the growth
CC of E.coli strain BW25113 on 2,7-AN as a sole carbon source
CC (PubMed:32669363). However, Kentache et al. show that it allows the
CC growth of E.coli on 2,7-AN and 2,3-EN, which are produced during the
CC degradation of sialoconjugates by sialidases from other bacteria,
CC provided the repressor NanR has been inactivated (PubMed:32542330).
CC {ECO:0000269|PubMed:32542330, ECO:0000269|PubMed:32669363}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar
CC transporter (TC 2.A.1.1) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA97175.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U14003; AAA97175.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC77235.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE78273.1; -; Genomic_DNA.
DR PIR; S56504; S56504.
DR RefSeq; NP_418699.4; NC_000913.3.
DR RefSeq; WP_000179691.1; NZ_SSUV01000014.1.
DR AlphaFoldDB; P39352; -.
DR SMR; P39352; -.
DR BioGRID; 4262721; 207.
DR STRING; 511145.b4279; -.
DR PaxDb; 511145-b4279; -.
DR EnsemblBacteria; AAC77235; AAC77235; b4279.
DR GeneID; 948807; -.
DR KEGG; ecj:JW5768; -.
DR KEGG; eco:b4279; -.
DR PATRIC; fig|1411691.4.peg.2424; -.
DR EchoBASE; EB2432; -.
DR eggNOG; COG2814; Bacteria.
DR HOGENOM; CLU_001265_46_8_6; -.
DR InParanoid; P39352; -.
DR OMA; DFVTYPF; -.
DR OrthoDB; 4474610at2; -.
DR PhylomeDB; P39352; -.
DR BioCyc; EcoCyc:YJHB-MONOMER; -.
DR BioCyc; MetaCyc:YJHB-MONOMER; -.
DR PRO; PR:P39352; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0046943; F:carboxylic acid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:1905039; P:carboxylic acid transmembrane transport; IGC:EcoCyc.
DR GO; GO:0046942; P:carboxylic acid transport; IBA:GO_Central.
DR CDD; cd17316; MFS_SV2_like; 1.
DR Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 1.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR PANTHER; PTHR23508; CARBOXYLIC ACID TRANSPORTER PROTEIN HOMOLOG; 1.
DR PANTHER; PTHR23508:SF2; METABOLITE TRANSPORT PROTEIN YJHB-RELATED; 1.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; MFS general substrate transporter; 1.
DR PROSITE; PS50850; MFS; 1.
PE 2: Evidence at transcript level;
KW Cell inner membrane; Cell membrane; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..405
FT /note="Sialic acid transporter NanX"
FT /id="PRO_0000050487"
FT TOPO_DOM 1..20
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 21..41
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 42..53
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 54..74
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 75..80
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 81..101
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 102
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 103..123
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 124..139
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 140..160
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 161..164
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 165..185
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 186..214
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 215..235
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 236..250
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 251..271
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 272..282
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 283..303
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 304..307
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 308..328
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 329..344
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 345..365
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 366..371
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 372..392
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 393..405
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 405 AA; 44104 MW; A8F45D9298EB09EE CRC64;
MATAWYKQVN PPQRKALFSA WLGYVFDGFD FMMIFYILHI IKADLGITDI QATLIGTVAF
IARPIGGGFF GAMADKYGRK PMMMWAIFIY SVGTGLSGIA TNLYMLAVCR FIVGLGMSGE
YACASTYAVE SWPKNLQSKA SAFLVSGFSV GNIIAAQIIP QFAEVYGWRN SFFIGLLPVL
LVLWIRKSAP ESQEWIEDKY KDKSTFLSVF RKPHLSISMI VFLVCFCLFG ANWPINGLLP
SYLADNGVNT VVISTLMTIA GLGTLTGTIF FGFVGDKIGV KKAFVVGLIT SFIFLCPLFF
ISVKNSSLIG LCLFGLMFTN LGIAGLVPKF IYDYFPTKLR GLGTGLIYNL GATGGMAAPV
LATYISGYYG LGVSLFIVTV AFSALLILLV GFDIPGKIYK LSVAK
//
