NHAB_ECOLI
ID NHAB_ECOLI Reviewed; 513 AA.
AC P0AFA7; P27377; P77533;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Na(+)/H(+) antiporter NhaB {ECO:0000255|HAMAP-Rule:MF_01599, ECO:0000303|PubMed:1317851};
DE AltName: Full=Sodium/proton antiporter NhaB {ECO:0000255|HAMAP-Rule:MF_01599, ECO:0000305};
GN Name=nhaB {ECO:0000255|HAMAP-Rule:MF_01599, ECO:0000303|PubMed:1317851};
GN OrderedLocusNames=b1186, JW1175;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=K12;
RX PubMed=1317851; DOI=10.1016/s0021-9258(19)49875-x;
RA Pinner E., Padan E., Schuldiner S.;
RT "Cloning, sequencing, and expression of the nhaB gene, encoding a Na+/H+
RT antiporter in Escherichia coli.";
RL J. Biol. Chem. 267:11064-11068(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [3]
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 [4]
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 [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=8093613; DOI=10.1016/s0021-9258(18)53913-2;
RA Pinner E., Kotler Y., Padan E., Schuldiner S.;
RT "Physiological role of nhaB, a specific Na+/H+ antiporter in Escherichia
RT coli.";
RL J. Biol. Chem. 268:1729-1734(1993).
RN [6]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12;
RX PubMed=8019504; DOI=10.1248/bpb.17.395;
RA Inaba K., Kuroda T., Shimamoto T., Kayahara T., Tsuda M., Tsuchiya T.;
RT "Lithium toxicity and Na+(Li+)/H+ antiporter in Escherichia coli.";
RL Biol. Pharm. Bull. 17:395-398(1994).
RN [7]
RP FUNCTION IN INTRACELLULAR PH REGULATION.
RC STRAIN=K12;
RX PubMed=7822245; DOI=10.1093/oxfordjournals.jbchem.a124521;
RA Shimamoto T., Inaba K., Thelen P., Ishikawa T., Goldberg E.B., Tsuda M.,
RA Tsuchiya T.;
RT "The NhaB Na+/H+ antiporter is essential for intracellular pH regulation
RT under alkaline conditions in Escherichia coli.";
RL J. Biochem. 116:285-290(1994).
RN [8]
RP FUNCTION, STOICHIOMETRY, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=K12;
RX PubMed=7929345; DOI=10.1016/s0021-9258(18)47190-6;
RA Pinner E., Padan E., Schuldiner S.;
RT "Kinetic properties of NhaB, a Na+/H+ antiporter from Escherichia coli.";
RL J. Biol. Chem. 269:26274-26279(1994).
RN [9]
RP 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).
CC -!- FUNCTION: Na(+)/H(+) antiporter that extrudes sodium in exchange for
CC external protons (PubMed:1317851, PubMed:8093613, PubMed:8019504,
CC PubMed:7929345). Catalyzes the exchange of 3 H(+) per 2 Na(+)
CC (PubMed:7929345). Can also transport lithium (PubMed:8019504).
CC Essential for regulation of intracellular pH under alkaline conditions
CC (PubMed:7822245). Is necessary for growth on Na(+)/symport substrates
CC such as glutamate and proline under conditions in which nhaA is not
CC expressed, such as acidic pH and low Na(+) concentration
CC (PubMed:8093613). {ECO:0000269|PubMed:1317851,
CC ECO:0000269|PubMed:7822245, ECO:0000269|PubMed:7929345,
CC ECO:0000269|PubMed:8019504, ECO:0000269|PubMed:8093613}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3 H(+)(out) + 2 Na(+)(in) = 3 H(+)(in) + 2 Na(+)(out);
CC Xref=Rhea:RHEA:29247, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01599,
CC ECO:0000269|PubMed:7929345};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29248;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01599,
CC ECO:0000269|PubMed:7929345};
CC -!- ACTIVITY REGULATION: Activity is weakly pH-dependent.
CC {ECO:0000269|PubMed:7929345}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=16.66 mM for Na(+) (at pH 7.2) {ECO:0000269|PubMed:7929345};
CC KM=3.44 mM for Na(+) (at pH 7.6) {ECO:0000269|PubMed:7929345};
CC KM=1.53 mM for Na(+) (at pH 8.5) {ECO:0000269|PubMed:7929345};
CC KM=0.73 mM for Na(+) {ECO:0000269|PubMed:8019504};
CC KM=0.63 mM for Li(+) {ECO:0000269|PubMed:8019504};
CC Vmax=107 umol/min/mg enzyme (at pH 7.2) {ECO:0000269|PubMed:7929345};
CC Vmax=67.5 umol/min/mg enzyme (at pH 7.6)
CC {ECO:0000269|PubMed:7929345};
CC Vmax=87.8 umol/min/mg enzyme (at pH 8.5)
CC {ECO:0000269|PubMed:7929345};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01599, ECO:0000269|PubMed:15919996}; Multi-pass membrane
CC protein {ECO:0000255|HAMAP-Rule:MF_01599}.
CC -!- DISRUPTION PHENOTYPE: At pH 6 and at low Na(+) concentrations, deletion
CC mutant grows slower than the wild type and its Na(+) dependent
CC transport of glutamate and proline is markedly inhibited. However, when
CC grown on these substrates at higher pH (7.5), mutant does not show any
CC specific phenotype. A mutant devoid of both nhaA and nhaB is extremely
CC sensitive to Na(+) and Li(+) at all pH values, and membranes prepared
CC from this strain show no Na(+)/H(+) antiporter activity
CC (PubMed:8093613). A mutant lacking this gene can grow in the presence
CC of 0.6 M LiCl, but a mutant lacking both nhaA and nhaB cannot grow in
CC the presence of 30 mM LiCl (PubMed:8019504).
CC {ECO:0000269|PubMed:8019504, ECO:0000269|PubMed:8093613}.
CC -!- MISCELLANEOUS: NhaB seems crucial when the level of NhaA activity is
CC growth limiting, when nhaA is not sufficiently induced, and/or when
CC NhaA is not activated. {ECO:0000269|PubMed:8093613}.
CC -!- SIMILARITY: Belongs to the NhaB Na(+)/H(+) (TC 2.A.34) antiporter
CC family. {ECO:0000255|HAMAP-Rule:MF_01599, ECO:0000305}.
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DR EMBL; M83655; AAA24218.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74270.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA36033.1; -; Genomic_DNA.
DR PIR; G64864; G64864.
DR RefSeq; NP_415704.1; NC_000913.3.
DR RefSeq; WP_000406391.1; NZ_STEB01000023.1.
DR AlphaFoldDB; P0AFA7; -.
DR SMR; P0AFA7; -.
DR BioGRID; 4260101; 18.
DR STRING; 511145.b1186; -.
DR TCDB; 2.A.34.1.1; the nhab na(+):h(+) antiporter (nhab) family.
DR jPOST; P0AFA7; -.
DR PaxDb; P0AFA7; -.
DR PRIDE; P0AFA7; -.
DR EnsemblBacteria; AAC74270; AAC74270; b1186.
DR EnsemblBacteria; BAA36033; BAA36033; BAA36033.
DR GeneID; 66674994; -.
DR GeneID; 944822; -.
DR KEGG; ecj:JW1175; -.
DR KEGG; eco:b1186; -.
DR PATRIC; fig|1411691.4.peg.1101; -.
DR EchoBASE; EB1365; -.
DR eggNOG; COG3067; Bacteria.
DR HOGENOM; CLU_041110_0_0_6; -.
DR InParanoid; P0AFA7; -.
DR OMA; QFEMLAV; -.
DR PhylomeDB; P0AFA7; -.
DR BioCyc; EcoCyc:NHAB-MON; -.
DR BioCyc; MetaCyc:NHAB-MON; -.
DR PRO; PR:P0AFA7; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; ISM:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoliWiki.
DR GO; GO:0015385; F:sodium:proton antiporter activity; IDA:EcoliWiki.
DR GO; GO:0010226; P:response to lithium ion; IGI:EcoliWiki.
DR HAMAP; MF_01599; NhaB; 1.
DR InterPro; IPR004671; Na+/H+_antiporter_NhaB.
DR PANTHER; PTHR43302:SF1; PTHR43302:SF1; 1.
DR Pfam; PF06450; NhaB; 1.
DR TIGRFAMs; TIGR00774; NhaB; 1.
PE 1: Evidence at protein level;
KW Antiport; Cell inner membrane; Cell membrane; Ion transport; Membrane;
KW Reference proteome; Sodium; Sodium transport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..513
FT /note="Na(+)/H(+) antiporter NhaB"
FT /id="PRO_0000052412"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01599"
FT TRANSMEM 52..72
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01599"
FT TRANSMEM 97..117
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01599"
FT TRANSMEM 120..140
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01599"
FT TRANSMEM 144..164
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01599"
FT TRANSMEM 202..222
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01599"
FT TRANSMEM 238..258
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01599"
FT TRANSMEM 303..323
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01599"
FT TRANSMEM 348..368
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01599"
FT TRANSMEM 391..411
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01599"
FT TRANSMEM 447..467
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01599"
FT TRANSMEM 475..495
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01599"
FT CONFLICT 1..11
FT /note="MEISWGRALWR -> MA (in Ref. 1; AAA24218)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 513 AA; 56728 MW; B5D85BD8E761E2BB CRC64;
MEISWGRALW RNFLGQSPDW YKLALIIFLI VNPLIFLISP FVAGWLLVAE FIFTLAMALK
CYPLLPGGLL AIEAVFIGMT SAEHVREEVA ANLEVLLLLM FMVAGIYFMK QLLLFIFTRL
LLSIRSKMLL SLSFCVAAAF LSAFLDALTV VAVVISVAVG FYGIYHRVAS SRTEDTDLQD
DSHIDKHYKV VLEQFRGFLR SLMMHAGVGT ALGGVMTMVG EPQNLIIAKA AGWHFGDFFL
RMSPVTVPVL ICGLLTCLLV EKLRWFGYGE TLPEKVREVL QQFDDQSRHQ RTRQDKIRLI
VQAIIGVWLV TALALHLAEV GLIGLSVIIL ATSLTGVTDE HAIGKAFTES LPFTALLTVF
FSVVAVIIDQ QLFSPIIQFV LQASEHAQLS LFYIFNGLLS SISDNVFVGT IYINEAKAAM
ESGAITLKQY ELLAVAINTG TNLPSVATPN GQAAFLFLLT SALAPLIRLS YGRMVWMALP
YTLVLTLVGL LCVEFTLAPV TEWFMQMGWI ATL
