RegulonDB RegulonDB 11.1: Gene Form
   

nhaB gene in Escherichia coli K-12 genome


Gene local context to scale (view description)

nhaB fadR dsbB FadR e14 prophage; C0293 DksA-ppGpp DksA-ppGpp fadRp2 fadRp2 fadRp1 fadRp1 nhaBp7 nhaBp7 dsbBp6 dsbBp6

Gene      
Name: nhaB    Texpresso search in the literature
Synonym(s): ECK1174, EG11392, b1186
Genome position(nucleotides): 1233176 <-- 1234717
Strand: reverse
Sequence: Get nucleotide sequence FastaFormat
GC content %:  
 52.85
External database links:  
ASAP:
 ABE-0003984
CGSC:
 30269
ECHOBASE:
 EB1365
ECOLIHUB:
 nhaB
OU-MICROARRAY:
 b1186
STRING:
 511145.b1186
COLOMBOS: nhaB


Product      
Name: Na+:H+ antiporter NhaB
Synonym(s): NhaB
Sequence: Get amino acid sequence Fasta Format
Cellular location: inner membrane
Molecular weight: 56.728
Isoelectric point: 6.351
Motif(s):
 
Type Positions Sequence Comment
1 -> 511 MEISWGRALWRNFLGQSPDWYKLALIIFLIVNPLIFLISPFVAGWLLVAEFIFTLAMALKCYPLLPGGLLAIEAVFIGMTSAEHVREEVAANLEVLLLLMFMVAGIYFMKQLLLFIFTRLLLSIRSKMLLSLSFCVAAAFLSAFLDALTVVAVVISVAVGFYGIYHRVASSRTEDTDLQDDSHIDKHYKVVLEQFRGFLRSLMMHAGVGTALGGVMTMVGEPQNLIIAKAAGWHFGDFFLRMSPVTVPVLICGLLTCLLVEKLRWFGYGETLPEKVREVLQQFDDQSRHQRTRQDKIRLIVQAIIGVWLVTALALHLAEVGLIGLSVIILATSLTGVTDEHAIGKAFTESLPFTALLTVFFSVVAVIIDQQLFSPIIQFVLQASEHAQLSLFYIFNGLLSSISDNVFVGTIYINEAKAAMESGAITLKQYELLAVAINTGTNLPSVATPNGQAAFLFLLTSALAPLIRLSYGRMVWMALPYTLVLTLVGLLCVEFTLAPVTEWFMQMGWIA
23 -> 43 LALIIFLIVNPLIFLISPFVA UniProt: Helical.
52 -> 72 IFTLAMALKCYPLLPGGLLAI UniProt: Helical.
97 -> 117 LLLMFMVAGIYFMKQLLLFIF UniProt: Helical.
120 -> 140 LLLSIRSKMLLSLSFCVAAAF UniProt: Helical.

 
Classification:
Multifun Terms (GenProtEC)  
  4 - transport --> 4.2 - Electrochemical potential driven transporters --> 4.2.A - Porters (Uni-, Sym- and Antiporters)
  5 - cell processes --> 5.5 - adaptations --> 5.5.4 - pH
  6 - cell structure --> 6.1 - membrane
Gene Ontology Terms (GO)  
cellular_component GO:0016020 - membrane
GO:0005886 - plasma membrane
GO:0005887 - integral component of plasma membrane
GO:0016021 - integral component of membrane
molecular_function GO:0015297 - antiporter activity
GO:0015081 - sodium ion transmembrane transporter activity
GO:0015385 - sodium:proton antiporter activity
biological_process GO:0006811 - ion transport
GO:0006814 - sodium ion transport
GO:0055085 - transmembrane transport
GO:0010226 - response to lithium ion
GO:0035725 - sodium ion transmembrane transport
Note(s): Note(s): ...[more].
Reference(s): [1] Gerchman Y., et al., 1993
[2] Inoue H., et al., 1995
[3] Ishikawa T., et al., 1987
[4] Kayahara T., et al., 1992
[5] Lewinson O., et al., 2004
[6] Maurer LM., et al., 2005
[7] Ohyama T., et al., 1992
[8] Padan E., et al., 1999
[9] Padan E., et al., 1989
[10] Rimon A., et al., 1995
[11] Rimon A., et al., 2007
[12] Rowbury RJ., et al., 1994
[13] Rowbury RJ., et al., 1996
[14] Shijuku T., et al., 2001
[15] Shimamoto T., et al., 1994
[16] Verkhovskaya ML., et al., 1996
External database links:  
ALPHAFOLD:
 P0AFA7
ECOCYC:
 NHAB-MONOMER
ECOLIWIKI:
 b1186
INTERPRO:
 IPR004671
PANTHER:
 PTHR43302:SF1
PFAM:
 PF06450
PRIDE:
 P0AFA7
PRODB:
 PRO_000023380
REFSEQ:
 NP_415704
UNIPROT:
 P0AFA7


Operon      
Name: nhaB         
Operon arrangement:
Transcription unit        Promoter
nhaB


Elements in the selected gene context region unrelated to any object in RegulonDB      

  Type Name Post Left Post Right Strand Notes Evidence (Confirmed, Strong, Weak) References
  promoter dsbBp6 1233147 reverse nd [COMP-AINF] [17]
  promoter nhaBp7 1234767 reverse nd [COMP-AINF], [RS-EPT-CBR] [17], [18]


Evidence    

 [COMP-AINF] Inferred computationally without human oversight

 [RS-EPT-CBR] RNA-seq using two enrichment strategies for primary transcripts and consistent biological replicates


Reference(s)    

 [1] Gerchman Y., Olami Y., Rimon A., Taglicht D., Schuldiner S., Padan E., 1993, Histidine-226 is part of the pH sensor of NhaA, a Na+/H+ antiporter in Escherichia coli., Proc Natl Acad Sci U S A 90(4):1212-6

 [2] Inoue H., Noumi T., Tsuchiya T., Kanazawa H., 1995, Essential aspartic acid residues, Asp-133, Asp-163 and Asp-164, in the transmembrane helices of a Na+/H+ antiporter (NhaA) from Escherichia coli., FEBS Lett 363(3):264-8

 [3] Ishikawa T., Hama H., Tsuda M., Tsuchiya T., 1987, Isolation and properties of a mutant of Escherichia coli possessing defective Na+/H+ antiporter., J Biol Chem 262(16):7443-6

 [4] Kayahara T., Thelen P., Ogawa W., Inaba K., Tsuda M., Goldberg EB., Tsuchiya T., 1992, Properties of recombinant cells capable of growing on serine without NhaB Na+/H+ antiporter in Escherichia coli., J Bacteriol 174(22):7482-5

 [5] Lewinson O., Padan E., Bibi E., 2004, Alkalitolerance: a biological function for a multidrug transporter in pH homeostasis., Proc Natl Acad Sci U S A 101(39):14073-8

 [6] Maurer LM., Yohannes E., Bondurant SS., Radmacher M., Slonczewski JL., 2005, pH regulates genes for flagellar motility, catabolism, and oxidative stress in Escherichia coli K-12., J Bacteriol 187(1):304-19

 [7] Ohyama T., Imaizumi R., Igarashi K., Kobayashi H., 1992, Escherichia coli is able to grow with negligible sodium ion extrusion activity at alkaline pH., J Bacteriol 174(23):7743-9

 [8] Padan E., Gerchman Y., Rimon A., Rothman A., Dover N., Carmel-Harel O., 1999, The molecular mechanism of regulation of the NhaA Na+/H+ antiporter of Escherichia coli, a key transporter in the adaptation to Na+ and H+., Novartis Found Symp 221:183-96: discussion 196-9

 [9] Padan E., Maisler N., Taglicht D., Karpel R., Schuldiner S., 1989, Deletion of ant in Escherichia coli reveals its function in adaptation to high salinity and an alternative Na+/H+ antiporter system(s)., J Biol Chem 264(34):20297-302

 [10] Rimon A., Gerchman Y., Olami Y., Schuldiner S., Padan E., 1995, 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., J Biol Chem 270(45):26813-7

 [11] Rimon A., Tzubery T., Padan E., 2007, 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+., J Biol Chem 282(37):26810-21

 [12] Rowbury RJ., Goodson M., Humphrey TJ., 1994, Sodium chloride induces an NhaA/NhaR-independent acid sensitivity at neutral external pH in Escherichia coli., Appl Environ Microbiol 60(5):1630-4

 [13] Rowbury RJ., Hussain NH., 1996, Exposure of Escherichia coli to acid habituation conditions sensitizes it to alkaline stress., Lett Appl Microbiol 22(1):57-61

 [14] Shijuku T., Saito H., Kakegawa T., Kobayashi H., 2001, Expression of sodium/proton antiporter NhaA at various pH values in Escherichia coli., Biochim Biophys Acta 1506(3):212-7

 [15] Shimamoto T., Inaba K., Thelen P., Ishikawa T., Goldberg EB., Tsuda M., Tsuchiya T., 1994, The NhaB Na+/H+ antiporter is essential for intracellular pH regulation under alkaline conditions in Escherichia coli., J Biochem 116(2):285-90

 [16] Verkhovskaya ML., Verkhovsky MI., Wikstrom M., 1996, K+-dependent Na+ transport driven by respiration in Escherichia coli cells and membrane vesicles., Biochim Biophys Acta 1273(3):207-16

 [17] Huerta AM., Collado-Vides J., 2003, Sigma70 promoters in Escherichia coli: specific transcription in dense regions of overlapping promoter-like signals., J Mol Biol 333(2):261-78

 [18] Salgado H, Peralta-Gil M, Gama-Castro S, Santos-Zavaleta A, Muñiz-Rascado L, García-Sotelo JS, Weiss V, Solano-Lira H, Martínez-Flores I, Medina-Rivera A, Salgado-Osorio G, Alquicira-Hernández S, Alquicira-Hernández K, López-Fuentes A, Porrón-Sotelo L, Huerta AM, Bonavides-Martínez C, Balderas-Martínez YI, Pannier L, Olvera M, Labastida A, Jiménez-Jacinto V, Vega-Alvarado L, Del Moral-Chávez V, Hernández-Alvarez A, Morett E, Collado-Vides J., 2012, RegulonDB v8.0: omics data sets, evolutionary conservation, regulatory phrases, cross-validated gold standards and more., Nucleic Acids Res.

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