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Protein

Probable glutamate/gamma-aminobutyrate antiporter

Gene

gadC

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Involved in glutamate-dependent acid resistance. Imports glutamate inside the cell while simultaneously exporting to the periplasm the GABA produced by GadA and GadB. The gad system helps to maintain a near-neutral intracellular pH when cells are exposed to extremely acidic conditions. The ability to survive transit through the acidic conditions of the stomach is essential for successful colonization of the mammalian host by commensal and pathogenic bacteria.

GO - Molecular functioni

GO - Biological processi

  • intracellular pH elevation Source: EcoCyc
  • L-alpha-amino acid transmembrane transport Source: GOC
  • L-amino acid transport Source: GOC
Complete GO annotation...

Keywords - Biological processi

Amino-acid transport, Antiport, Transport

Enzyme and pathway databases

BioCyciEcoCyc:XASA-MONOMER.
ECOL316407:JW1487-MONOMER.
MetaCyc:XASA-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable glutamate/gamma-aminobutyrate antiporter
Alternative name(s):
Extreme acid sensitivity protein
Gene namesi
Name:gadC
Synonyms:acsA, xasA
Ordered Locus Names:b1492, JW1487
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12456. gadC.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1414CytoplasmicSequence analysisAdd
BLAST
Transmembranei15 – 3521HelicalSequence analysisAdd
BLAST
Topological domaini36 – 416PeriplasmicSequence analysis
Transmembranei42 – 6221HelicalSequence analysisAdd
BLAST
Topological domaini63 – 9331CytoplasmicSequence analysisAdd
BLAST
Transmembranei94 – 11421HelicalSequence analysisAdd
BLAST
Topological domaini115 – 12713PeriplasmicSequence analysisAdd
BLAST
Transmembranei128 – 14821HelicalSequence analysisAdd
BLAST
Topological domaini149 – 1579CytoplasmicSequence analysis
Transmembranei158 – 17821HelicalSequence analysisAdd
BLAST
Topological domaini179 – 20022PeriplasmicSequence analysisAdd
BLAST
Transmembranei201 – 22121HelicalSequence analysisAdd
BLAST
Topological domaini222 – 23918CytoplasmicSequence analysisAdd
BLAST
Transmembranei240 – 26021HelicalSequence analysisAdd
BLAST
Topological domaini261 – 29131PeriplasmicSequence analysisAdd
BLAST
Transmembranei292 – 31221HelicalSequence analysisAdd
BLAST
Topological domaini313 – 33523CytoplasmicSequence analysisAdd
BLAST
Transmembranei336 – 35621HelicalSequence analysisAdd
BLAST
Topological domaini357 – 36610PeriplasmicSequence analysis
Transmembranei367 – 38721HelicalSequence analysisAdd
BLAST
Topological domaini388 – 41225CytoplasmicSequence analysisAdd
BLAST
Transmembranei413 – 43321HelicalSequence analysisAdd
BLAST
Topological domaini434 – 44512PeriplasmicSequence analysisAdd
BLAST
Transmembranei446 – 46621HelicalSequence analysisAdd
BLAST
Topological domaini467 – 51145CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB-KW
  • plasma membrane Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 511511Probable glutamate/gamma-aminobutyrate antiporterPRO_0000213040Add
BLAST

Proteomic databases

PaxDbiP63235.
PRIDEiP63235.

Expressioni

Inductioni

By acidic conditions. Expression is regulated by a complex system involving RpoS, cAMP, CRP, EvgAS, H-NS, GadE, GadW and GadX. The level of involvement for each regulator varies depending upon the growth phase and the medium.6 Publications

Interactioni

Protein-protein interaction databases

BioGridi4260789. 7 interactions.
DIPiDIP-48121N.
STRINGi511145.b1492.

Structurei

Secondary structure

1
511
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi15 – 217Combined sources
Helixi23 – 264Combined sources
Helixi29 – 313Combined sources
Helixi32 – 365Combined sources
Helixi37 – 404Combined sources
Helixi41 – 5212Combined sources
Helixi54 – 6512Combined sources
Turni68 – 703Combined sources
Helixi75 – 839Combined sources
Helixi85 – 10218Combined sources
Helixi104 – 11512Combined sources
Turni116 – 1194Combined sources
Helixi121 – 1233Combined sources
Helixi129 – 14618Combined sources
Beta strandi149 – 1513Combined sources
Helixi152 – 1554Combined sources
Helixi157 – 1626Combined sources
Helixi165 – 17814Combined sources
Turni201 – 2066Combined sources
Helixi207 – 2148Combined sources
Helixi217 – 2204Combined sources
Helixi222 – 2243Combined sources
Beta strandi225 – 2284Combined sources
Turni231 – 2333Combined sources
Helixi234 – 25724Combined sources
Helixi262 – 2643Combined sources
Beta strandi267 – 2693Combined sources
Helixi271 – 2799Combined sources
Beta strandi280 – 2823Combined sources
Helixi284 – 2885Combined sources
Helixi289 – 30820Combined sources
Helixi311 – 3155Combined sources
Helixi318 – 3214Combined sources
Helixi322 – 3243Combined sources
Beta strandi326 – 3283Combined sources
Beta strandi334 – 3363Combined sources
Helixi340 – 35718Combined sources
Beta strandi358 – 3614Combined sources
Helixi362 – 39534Combined sources
Beta strandi401 – 4033Combined sources
Helixi410 – 42920Combined sources
Beta strandi437 – 4404Combined sources
Helixi445 – 46521Combined sources
Beta strandi478 – 4803Combined sources
Beta strandi484 – 4863Combined sources
Turni496 – 4983Combined sources
Beta strandi501 – 5077Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4DJIX-ray3.19A/B1-511[»]
4DJKX-ray3.10A/B1-511[»]
ProteinModelPortaliP63235.
SMRiP63235. Positions 10-509.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105E5D. Bacteria.
COG0531. LUCA.
HOGENOMiHOG000058004.
InParanoidiP63235.
OMAiNPELAHN.
OrthoDBiEOG6V1M10.
PhylomeDBiP63235.

Family and domain databases

InterProiIPR002293. AA/rel_permease1.
IPR004759. Glu_antiport.
[Graphical view]
PANTHERiPTHR11785. PTHR11785. 1 hit.
PfamiPF13520. AA_permease_2. 1 hit.
[Graphical view]
PIRSFiPIRSF006060. AA_transporter. 1 hit.
TIGRFAMsiTIGR00910. 2A0307_GadC. 1 hit.

Sequencei

Sequence statusi: Complete.

P63235-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATSVQTGKA KQLTLLGFFA ITASMVMAVY EYPTFATSGF SLVFFLLLGG
60 70 80 90 100
ILWFIPVGLC AAEMATVDGW EEGGVFAWVS NTLGPRWGFA AISFGYLQIA
110 120 130 140 150
IGFIPMLYFV LGALSYILKW PALNEDPITK TIAALIILWA LALTQFGGTK
160 170 180 190 200
YTARIAKVGF FAGILLPAFI LIALAAIYLH SGAPVAIEMD SKTFFPDFSK
210 220 230 240 250
VGTLVVFVAF ILSYMGVEAS ATHVNEMSNP GRDYPLAMLL LMVAAICLSS
260 270 280 290 300
VGGLSIAMVI PGNEINLSAG VMQTFTVLMS HVAPEIEWTV RVISALLLLG
310 320 330 340 350
VLAEIASWIV GPSRGMYVTA QKNLLPAAFA KMNKNGVPVT LVISQLVITS
360 370 380 390 400
IALIILTNTG GGNNMSFLIA LALTVVIYLC AYFMLFIGYI VLVLKHPDLK
410 420 430 440 450
RTFNIPGGKG VKLVVAIVGL LTSIMAFIVS FLPPDNIQGD STDMYVELLV
460 470 480 490 500
VSFLVVLALP FILYAVHDRK GKANTGVTLE PINSQNAPKG HFFLHPRARS
510
PHYIVMNDKK H
Length:511
Mass (Da):55,077
Last modified:October 11, 2004 - v1
Checksum:i85DF72B82816CE33
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC74565.1.
AP009048 Genomic DNA. Translation: BAA15156.2.
U13204 Genomic DNA. Translation: AAB17694.1.
PIRiG64902.
RefSeqiNP_416009.1. NC_000913.3.
WP_000246019.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74565; AAC74565; b1492.
BAA15156; BAA15156; BAA15156.
GeneIDi946057.
KEGGiecj:JW1487.
eco:b1492.
PATRICi32118278. VBIEscCol129921_1559.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC74565.1.
AP009048 Genomic DNA. Translation: BAA15156.2.
U13204 Genomic DNA. Translation: AAB17694.1.
PIRiG64902.
RefSeqiNP_416009.1. NC_000913.3.
WP_000246019.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4DJIX-ray3.19A/B1-511[»]
4DJKX-ray3.10A/B1-511[»]
ProteinModelPortaliP63235.
SMRiP63235. Positions 10-509.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260789. 7 interactions.
DIPiDIP-48121N.
STRINGi511145.b1492.

Proteomic databases

PaxDbiP63235.
PRIDEiP63235.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74565; AAC74565; b1492.
BAA15156; BAA15156; BAA15156.
GeneIDi946057.
KEGGiecj:JW1487.
eco:b1492.
PATRICi32118278. VBIEscCol129921_1559.

Organism-specific databases

EchoBASEiEB2350.
EcoGeneiEG12456. gadC.

Phylogenomic databases

eggNOGiENOG4105E5D. Bacteria.
COG0531. LUCA.
HOGENOMiHOG000058004.
InParanoidiP63235.
OMAiNPELAHN.
OrthoDBiEOG6V1M10.
PhylomeDBiP63235.

Enzyme and pathway databases

BioCyciEcoCyc:XASA-MONOMER.
ECOL316407:JW1487-MONOMER.
MetaCyc:XASA-MONOMER.

Miscellaneous databases

PROiP63235.

Family and domain databases

InterProiIPR002293. AA/rel_permease1.
IPR004759. Glu_antiport.
[Graphical view]
PANTHERiPTHR11785. PTHR11785. 1 hit.
PfamiPF13520. AA_permease_2. 1 hit.
[Graphical view]
PIRSFiPIRSF006060. AA_transporter. 1 hit.
TIGRFAMsiTIGR00910. 2A0307_GadC. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], SEQUENCE REVISION.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. "A glutamate-dependent acid resistance gene in Escherichia coli."
    Hersh B.M., Farooq F.T., Barstad D.N., Blankenhorn D.L., Slonczewski J.L.
    J. Bacteriol. 178:3978-3981(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 402-490.
    Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
  5. "The response to stationary-phase stress conditions in Escherichia coli: role and regulation of the glutamic acid decarboxylase system."
    De Biase D., Tramonti A., Bossa F., Visca P.
    Mol. Microbiol. 32:1198-1211(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: TRANSCRIPTIONAL REGULATION.
    Strain: ATCC 11246.
  6. "Functional characterization and regulation of gadX, a gene encoding an AraC/XylS-like transcriptional activator of the Escherichia coli glutamic acid decarboxylase system."
    Tramonti A., Visca P., De Canio M., Falconi M., De Biase D.
    J. Bacteriol. 184:2603-2613(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: TRANSCRIPTIONAL REGULATION.
    Strain: ATCC 11246.
  7. "Escherichia coli gene expression responsive to levels of the response regulator EvgA."
    Masuda N., Church G.M.
    J. Bacteriol. 184:6225-6234(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: TRANSCRIPTIONAL REGULATION.
    Strain: K12 / MG1655 / ATCC 47076.
  8. "The glutamate-dependent acid resistance system of Escherichia coli and Shigella flexneri is inhibited in vitro by L-trans-pyrrolidine-2,4-dicarboxylic acid."
    Waterman S.R., Small P.L.C.
    FEMS Microbiol. Lett. 224:119-125(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INHIBITION BY L-PDC.
    Strain: K12.
  9. "Transcriptional expression of Escherichia coli glutamate-dependent acid resistance genes gadA and gadBC in an hns rpoS mutant."
    Waterman S.R., Small P.L.C.
    J. Bacteriol. 185:4644-4647(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: TRANSCRIPTIONAL REGULATION.
  10. "Regulatory network of acid resistance genes in Escherichia coli."
    Masuda N., Church G.M.
    Mol. Microbiol. 48:699-712(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: TRANSCRIPTIONAL REGULATION.
    Strain: K12 / MG1655 / ATCC 47076.
  11. "GadE (YhiE) activates glutamate decarboxylase-dependent acid resistance in Escherichia coli K-12."
    Ma Z., Gong S., Richard H., Tucker D.L., Conway T., Foster J.W.
    Mol. Microbiol. 49:1309-1320(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: TRANSCRIPTIONAL REGULATION.
    Strain: K12.
  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] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
    Strain: K12 / MG1655 / ATCC 47076.

Entry informationi

Entry nameiGADC_ECOLI
AccessioniPrimary (citable) accession number: P63235
Secondary accession number(s): P39183
, P76131, P77384, Q54152
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: February 17, 2016
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The glutamate analog L-trans-pyrrolidine-2,4-dicarboxylic acid (L-PDC) blocks the uptake of glutamate by selective inhibition.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.