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Reviewed, UniProtKB/Swiss-Prot P13738 (NHAA_ECOLI)

Last modified November 3, 2009. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Na(+)/H(+) antiporter nhaA
Alternative name(s):
    Sodium/proton antiporter nhaA
Gene names
Name: nhaA
Synonyms: ant
Ordered Locus Names: b0019, JW0018
OrganismEscherichia coli (strain K12) [Complete proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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Protein attributes

Sequence length388 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Na+/H+ antiporter that extrudes sodium in exchange for external protons. Catalyzes the exchange of 2 H+ per Na+. Can mediate sodium uptake when a transmembrane pH gradient is applied. Active at alkaline pH. Activity is strongly down-regulated below pH 6.5. Ref.7

Subunit structure

Monomer and homodimer. Ref.11 Ref.13

Subcellular location

Cell inner membrane; Multi-pass membrane protein. HAMAP MF_01844

Induction

Transcription stimulated by high Na+ concentrations. HAMAP MF_01844

Sequence similarities

Belongs to the nhaA Na(+)/H(+) (TC 2.A.33) antiporter family. [View classification]

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 388388Na(+)/H(+) antiporter nhaA HAMAP MF_01844
PRO_0000052410

Regions

Topological domain1 – 1111Cytoplasmic Ref.12
Transmembrane12 – 30191 HAMAP MF_01844
Topological domain31 – 5828Periplasmic Ref.12
Transmembrane59 – 85272 HAMAP MF_01844
Topological domain86 – 949Cytoplasmic Ref.12
Transmembrane95 – 116223 HAMAP MF_01844
Topological domain117 – 1204Periplasmic Ref.12
Transmembrane121 – 143234 HAMAP MF_01844
Topological domain144 – 1496Cytoplasmic Ref.12
Transmembrane150 – 175265 HAMAP MF_01844
Topological domain176 – 1816Periplasmic Ref.12
Transmembrane182 – 200196 HAMAP MF_01844
Topological domain201 – 2044Cytoplasmic Ref.12
Transmembrane205 – 218147 HAMAP MF_01844
Topological domain219 – 2224Periplasmic Ref.12
Transmembrane223 – 236148 HAMAP MF_01844
Topological domain237 – 24610Cytoplasmic Ref.12
Transmembrane247 – 271259 HAMAP MF_01844
Topological domain272 – 28918Periplasmic Ref.12
Transmembrane290 – 3112210 HAMAP MF_01844
Topological domain312 – 32615Cytoplasmic Ref.12
Transmembrane327 – 3502411 HAMAP MF_01844
Topological domain351 – 3566Periplasmic Ref.12
Transmembrane357 – 3822612 HAMAP MF_01844
Topological domain383 – 3886Cytoplasmic Ref.12
Region45 – 5814Important for dimerization HAMAP MF_01844

Sites

Site1331Essential for antiport activity HAMAP MF_01844
Site163 – 1642Essential for antiport activity HAMAP MF_01844
Site1631Essential for antiport activity HAMAP MF_01844
Site2411Important for pH sensor Probable
Site2491Important for pH sensor Probable
Site2521Important for pH sensor Probable

Experimental info

Mutagenesis1331D → N: Loss of antiport activity. Abolishes ability to grow on high salt medium. Ref.8 Ref.9
Mutagenesis1631D → C: Loss of antiport activity. Ref.11 Ref.8 Ref.9
Mutagenesis1631D → N: Loss of antiport activity. Abolishes ability to grow on high salt medium. Ref.11 Ref.8 Ref.9
Mutagenesis1641D → N: Loss of antiport activity. Abolishes ability to grow on high salt medium. Ref.8 Ref.9
Mutagenesis2251H → A: Loss of antiport activity. Abolishes ability to grow at alkaline pH. Ref.11 Ref.8 Ref.10
Mutagenesis2251H → C or S: Slightly reduced antiport activity. No effect on pH sensitivity. Ref.11 Ref.8 Ref.10
Mutagenesis2251H → D or R: Shifts threshold for pH-sensitive inactivation. Ref.11 Ref.8 Ref.10
Mutagenesis3381G → S: Loss of pH-sensitivity. Ref.11 Ref.8

Secondary structure

1 ..................................................................... 388
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P13738-1 [UniParc].

Last modified February 1, 1996. Version 3.
Checksum: B508B1D2E5EE9130

FASTA38841,356
        10         20         30         40         50         60 
MKHLHRFFSS DASGGIILII AAILAMIMAN SGATSGWYHD FLETPVQLRV GSLEINKNML 

        70         80         90        100        110        120 
LWINDALMAV FFLLVGLEVK RELMQGSLAS LRQAAFPVIA AIGGMIVPAL LYLAFNYADP 

       130        140        150        160        170        180 
ITREGWAIPA ATDIAFALGV LALLGSRVPL ALKIFLMALA IIDDLGAIII IALFYTNDLS 

       190        200        210        220        230        240 
MASLGVAAVA IAVLAVLNLC GARRTGVYIL VGVVLWTAVL KSGVHATLAG VIVGFFIPLK 

       250        260        270        280        290        300 
EKHGRSPAKR LEHVLHPWVA YLILPLFAFA NAGVSLQGVT LDGLTSILPL GIIAGLLIGK 

       310        320        330        340        350        360 
PLGISLFCWL ALRLKLAHLP EGTTYQQIMV VGILCGIGFT MSIFIASLAF GSVDPELINW 

       370        380 
AKLGILVGSI SSAVIGYSWL RVRLRPSV

« Hide

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References

« Hide 'large scale' references
[1]"Sequencing of the gene ant which affects the Na+/H+ antiporter activity in Escherichia coli."
Karpel R., Olami Y., Taglicht D., Schuldiner S., Padan E.
J. Biol. Chem. 263:10408-10414(1988) [PubMed: 2839489] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]Padan E.
Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[3]"Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region."
Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K., Mizobuchi K., Nakata A.
Nucleic Acids Res. 20:3305-3308(1992) [PubMed: 1630901] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12.
[4]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[5]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]"Expression of a sodium proton antiporter (NhaA) in Escherichia coli is induced by Na+ and Li+ ions."
Karpel R., Alon T., Glaser G., Schuldiner S., Padan E.
J. Biol. Chem. 266:21753-21759(1991) [PubMed: 1657980] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28.
[7]"Overproduction and purification of a functional Na+/H+ antiporter coded by nhaA (ant) from Escherichia coli."
Taglicht D., Padan E., Schuldiner S.
J. Biol. Chem. 266:11289-11294(1991) [PubMed: 1645730] [Abstract]
Cited for: FUNCTION, PARTIAL PROTEIN SEQUENCE.
[8]"Histidine-226 is part of the pH sensor of NhaA, a Na+/H+ antiporter in Escherichia coli."
Gerchman Y., Olami Y., Rimon A., Taglicht D., Schuldiner S., Padan E.
Proc. Natl. Acad. Sci. U.S.A. 90:1212-1216(1993) [PubMed: 8381959] [Abstract]
Cited for: MUTAGENESIS OF HISTIDINE RESIDUES.
[9]"Essential aspartic acid residues, Asp-133, Asp-163 and Asp-164, in the transmembrane helices of a Na+/H+ antiporter (NhaA) from Escherichia coli."
Inoue H., Noumi T., Tsuchiya T., Kanazawa H.
FEBS Lett. 363:264-268(1995) [PubMed: 7737413] [Abstract]
Cited for: MUTAGENESIS OF ASP-133; ASP-163 AND ASP-164.
[10]"Replacements of histidine 226 of NhaA-Na+/H+ antiporter of Escherichia coli. Cysteine (H226C) or serine (H226S) retain both normal activity and pH sensitivity, aspartate (H226D) shifts the pH profile toward basic pH, and alanine (H226A) inactivates the carrier at all pH values."
Rimon A., Gerchman Y., Olami Y., Schuldiner S., Padan E.
J. Biol. Chem. 270:26813-26817(1995) [PubMed: 7592922] [Abstract]
Cited for: MUTAGENESIS OF HIS-225.
[11]"Oligomerization of NhaA, the Na+/H+ antiporter of Escherichia coli in the membrane and its functional and structural consequences."
Gerchman Y., Rimon A., Venturi M., Padan E.
Biochemistry 40:3403-3412(2001) [PubMed: 11258962] [Abstract]
Cited for: SUBUNIT, MUTAGENESIS OF ASP-163; HIS-225 AND GLY-338.
[12]"Global topology analysis of the Escherichia coli inner membrane proteome."
Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.
Science 308:1321-1323(2005) [PubMed: 15919996] [Abstract]
Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
Strain: K12 / MG1655 / ATCC 47076.
[13]"Monomers of the NhaA Na+/H+ antiporter of Escherichia coli are fully functional yet dimers are beneficial under extreme stress conditions at alkaline pH in the presence of Na+ or Li+."
Rimon A., Tzubery T., Padan E.
J. Biol. Chem. 282:26810-26821(2007) [PubMed: 17635927] [Abstract]
Cited for: SUBUNIT.
[14]"Structure of a Na+/H+ antiporter and insights into mechanism of action and regulation by pH."
Hunte C., Screpanti E., Venturi M., Rimon A., Padan E., Michel H.
Nature 435:1197-1202(2005) [PubMed: 15988517] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.45 ANGSTROMS).
+Additional computationally mapped references.

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Cross-references

Sequence databases

J03879 Genomic DNA. Translation: AAA23448.2.
U00096 Genomic DNA. Translation: AAC73130.1.
AP009048 Genomic DNA. Translation: BAB96592.1.
S67239 Genomic DNA. Translation: AAB20348.1.
PIRC64722.
RefSeqAP_000683.1.
NP_414560.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1ZCDX-ray3.45A/B1-388[»]
3FI1electron microscopy7.00A/B9-384[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:10335N.
STRINGP13738.

Protein family/group databases

TCDB2.A.33.1.1. NhaA Na+:H+ antiporter (NhaA) family.

Genome annotation databases

GeneID944758.
GenomeReviewsGene locus JW0018 in contig AP009048_GR.
Gene locus b0019 in contig U00096_GR.
KEGGecj:JW0018.
eco:b0019.

Organism-specific databases

EchoBASEEB0646.
EcoGeneEG10652. nhaA.
CMRSearch...

Phylogenomic databases

HOGENOMP13738.
OMAQKAIFPA.

Enzyme and pathway databases

BioCycEcoCyc:NHAA-MON.

Gene expression databases

GenevestigatorP13738.

Family and domain databases

HAMAPMF_01844.
[Tree]
InterProIPR004670. NhaA.
[Graphical view]
PfamPF06965. Na_H_antiport_1. 1 hit.
[Graphical view]
TIGRFAMsTIGR00773. NhaA. 1 hit.
ProtoNetSearch...

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Entry information

Entry nameNHAA_ECOLI
AccessionPrimary (citable) accession number: P13738
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: February 1, 1996
Last modified: November 3, 2009
This is version 95 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents