NANT_ECOLI
ID NANT_ECOLI Reviewed; 496 AA.
AC P41036; P76675; Q2M8Y9;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Sialic acid transporter NanT {ECO:0000255|HAMAP-Rule:MF_01238, ECO:0000305};
DE AltName: Full=Sialic acid permease {ECO:0000255|HAMAP-Rule:MF_01238, ECO:0000305};
DE AltName: Full=Sialic acid/H(+) symporter {ECO:0000255|HAMAP-Rule:MF_01238, ECO:0000305};
GN Name=nanT {ECO:0000255|HAMAP-Rule:MF_01238, ECO:0000303|PubMed:7592358};
GN OrderedLocusNames=b3224, JW3193;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7592358; DOI=10.1128/jb.177.20.6005-6010.1995;
RA Martinez J., Steenbergen S., Vimr E.;
RT "Derived structure of the putative sialic acid transporter from Escherichia
RT coli predicts a novel sugar permease domain.";
RL J. Bacteriol. 177:6005-6010(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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-50.
RC STRAIN=JE1011;
RA Kawakami B., Kudo T., Narahashi Y., Horikoshi K.;
RT "Nucleotide sequence of the N-acetylneuraminate lyase gene of Escherichia
RT coli.";
RL Agric. Biol. Chem. 50:2155-2158(1986).
RN [5]
RP TOPOLOGY [LARGE SCALE ANALYSIS], AND SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [6]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=22167185; DOI=10.1074/jbc.m111.281030;
RA Mulligan C., Leech A.P., Kelly D.J., Thomas G.H.;
RT "The membrane proteins SiaQ and SiaM form an essential stoichiometric
RT complex in the sialic acid tripartite ATP-independent periplasmic (TRAP)
RT transporter SiaPQM (VC1777-1779) from Vibrio cholerae.";
RL J. Biol. Chem. 287:3598-3608(2012).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=23848303; DOI=10.1111/1574-6968.12213;
RA Hopkins A.P., Hawkhead J.A., Thomas G.H.;
RT "Transport and catabolism of the sialic acids N-glycolylneuraminic acid and
RT 3-keto-3-deoxy-D-glycero-D-galactonononic acid by Escherichia coli K-12.";
RL FEMS Microbiol. Lett. 347:14-22(2013).
RN [8]
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).
CC -!- FUNCTION: Catalyzes the proton-dependent transport of sialic acid
CC (PubMed:22167185, PubMed:23848303). Can transport the common sialic
CC acid N-acetylneuraminic acid (Neu5Ac) and the related sialic acids N-
CC glycolylneuraminic acid (Neu5Gc) and 3-keto-3-deoxy-D-glycero-D-
CC galactonononic acid (KDN) (PubMed:23848303). Functions as a
CC bidirectional transporter in vitro (PubMed:22167185).
CC {ECO:0000269|PubMed:22167185, ECO:0000269|PubMed:23848303}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(in) + N-acetylneuraminate(in) = H(+)(out) + N-
CC acetylneuraminate(out); Xref=Rhea:RHEA:28987, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:35418; Evidence={ECO:0000255|HAMAP-Rule:MF_01238,
CC ECO:0000269|PubMed:22167185, ECO:0000269|PubMed:23848303};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01238, ECO:0000269|PubMed:15919996}; Multi-pass membrane
CC protein {ECO:0000255|HAMAP-Rule:MF_01238}.
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: Deletion mutant is unable to grow in the presence
CC of Neu5Ac, Neu5Gc or KDN. {ECO:0000269|PubMed:23848303}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Sialate:H(+)
CC symporter (SHS) (TC 2.A.1.12) family. {ECO:0000255|HAMAP-Rule:MF_01238,
CC ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA58026.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAA86827.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U19539; AAA86827.1; ALT_INIT; Genomic_DNA.
DR EMBL; U18997; AAA58026.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC76256.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE77267.1; -; Genomic_DNA.
DR EMBL; D00067; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; B65114; B65114.
DR RefSeq; NP_417691.4; NC_000913.3.
DR RefSeq; WP_000108454.1; NZ_LN832404.1.
DR AlphaFoldDB; P41036; -.
DR BioGRID; 4262439; 9.
DR STRING; 511145.b3224; -.
DR TCDB; 2.A.1.12.1; the major facilitator superfamily (mfs).
DR jPOST; P41036; -.
DR PaxDb; P41036; -.
DR PRIDE; P41036; -.
DR EnsemblBacteria; AAC76256; AAC76256; b3224.
DR EnsemblBacteria; BAE77267; BAE77267; BAE77267.
DR GeneID; 947740; -.
DR KEGG; ecj:JW3193; -.
DR KEGG; eco:b3224; -.
DR PATRIC; fig|1411691.4.peg.3504; -.
DR EchoBASE; EB4145; -.
DR eggNOG; COG2814; Bacteria.
DR HOGENOM; CLU_001265_46_8_6; -.
DR InParanoid; P41036; -.
DR OMA; HWLLLTY; -.
DR PhylomeDB; P41036; -.
DR BioCyc; EcoCyc:NANT-MON; -.
DR BioCyc; MetaCyc:NANT-MON; -.
DR PRO; PR:P41036; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0005351; F:carbohydrate:proton symporter activity; IDA:EcoCyc.
DR GO; GO:0046943; F:carboxylic acid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015136; F:sialic acid transmembrane transporter activity; IDA:EcoCyc.
DR GO; GO:0015538; F:sialic acid:proton symporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046942; P:carboxylic acid transport; IBA:GO_Central.
DR GO; GO:0015739; P:sialic acid transport; IDA:EcoCyc.
DR Gene3D; 1.20.1250.20; -; 2.
DR HAMAP; MF_01238; MFS_NanT; 1.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR004742; SA_transporter.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR TIGRFAMs; TIGR00891; 2A0112; 1.
DR PROSITE; PS50850; MFS; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Membrane; Reference proteome;
KW Sugar transport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..496
FT /note="Sialic acid transporter NanT"
FT /id="PRO_0000050311"
FT TOPO_DOM 1..21
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:15919996"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01238"
FT TOPO_DOM 43..57
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:15919996"
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01238"
FT TOPO_DOM 79..91
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:15919996"
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01238"
FT TOPO_DOM 113..147
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:15919996"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01238"
FT TOPO_DOM 169
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:15919996"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01238"
FT TOPO_DOM 191..223
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:15919996"
FT TRANSMEM 224..244
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01238"
FT TOPO_DOM 245..246
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:15919996"
FT TRANSMEM 247..267
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01238"
FT TOPO_DOM 268..277
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:15919996"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01238"
FT TOPO_DOM 299..312
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:15919996"
FT TRANSMEM 313..333
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01238"
FT TOPO_DOM 334..354
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:15919996"
FT TRANSMEM 355..375
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01238"
FT TOPO_DOM 376..405
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:15919996"
FT TRANSMEM 406..426
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01238"
FT TOPO_DOM 427..430
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:15919996"
FT TRANSMEM 431..451
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01238"
FT TOPO_DOM 452..496
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
FT CONFLICT 221
FT /note="E -> A (in Ref. 1; AAA86827)"
FT /evidence="ECO:0000305"
FT CONFLICT 441
FT /note="S -> R (in Ref. 1; AAA86827)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 496 AA; 53551 MW; D81DB24F7AD6A4CA CRC64;
MSTTTQNIPW YRHLNRAQWR AFSAAWLGYL LDGFDFVLIA LVLTEVQGEF GLTTVQAASL
ISAAFISRWF GGLMLGAMGD RYGRRLAMVT SIVLFSAGTL ACGFAPGYIT MFIARLVIGM
GMAGEYGSSA TYVIESWPKH LRNKASGFLI SGFSVGAVVA AQVYSLVVPV WGWRALFFIG
ILPIIFALWL RKNIPEAEDW KEKHAGKAPV RTMVDILYRG EHRIANIVMT LAAATALWFC
FAGNLQNAAI VAVLGLLCAA IFISFMVQSA GKRWPTGVML MVVVLFAFLY SWPIQALLPT
YLKTDLAYNP HTVANVLFFS GFGAAVGCCV GGFLGDWLGT RKAYVCSLLA SQLLIIPVFA
IGGANVWVLG LLLFFQQMLG QGIAGILPKL IGGYFDTDQR AAGLGFTYNV GALGGALAPI
IGALIAQRLD LGTALASLSF SLTFVVILLI GLDMPSRVQR WLRPEALRTH DAIDGKPFSG
AVPFGSAKND LVKTKS
