ID   NHAA_VIBCH              Reviewed;         382 AA.
AC   O85187; Q7DCU3;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   28-JAN-2026, entry version 118.
DE   RecName: Full=Na(+)/H(+) antiporter NhaA {ECO:0000303|PubMed:10781565};
DE   AltName: Full=Sodium/proton antiporter NhaA {ECO:0000255|HAMAP-Rule:MF_01844};
GN   Name=nhaA {ECO:0000303|PubMed:10781565}; OrderedLocusNames=VC_1627;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION AS ANTIPORTER, INDUCTION, AND
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=N18 / Serotype O1;
RX   PubMed=10781565; DOI=10.1128/jb.182.10.2937-2944.2000;
RA   Vimont S., Berche P.;
RT   "NhaA, an Na(+)/H(+) antiporter involved in environmental survival of
RT   Vibrio cholerae.";
RL   J. Bacteriol. 182:2937-2944(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
RN   [3]
RP   FUNCTION, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=N18 / Serotype O1;
RX   PubMed=12562793; DOI=10.1128/jb.185.4.1236-1244.2003;
RA   Herz K., Vimont S., Padan E., Berche P.;
RT   "Roles of NhaA, NhaB, and NhaD Na(+)/H(+) antiporters in survival of Vibrio
RT   cholerae in a saline environment.";
RL   J. Bacteriol. 185:1236-1244(2003).
CC   -!- FUNCTION: Na(+)/H(+) antiporter that extrudes sodium in exchange for
CC       external protons (PubMed:10781565, PubMed:12562793). Can also transport
CC       lithium (PubMed:12562793). Contributes to the survival of V.cholerae
CC       during the stationary and exponential growth phases in a saline
CC       environment (PubMed:12562793). {ECO:0000269|PubMed:10781565,
CC       ECO:0000269|PubMed:12562793}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Na(+)(in) + 2 H(+)(out) = Na(+)(out) + 2 H(+)(in);
CC         Xref=Rhea:RHEA:29251, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01844};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29252;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01844};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Li(+)(in) + 2 H(+)(out) = Li(+)(out) + 2 H(+)(in);
CC         Xref=Rhea:RHEA:70431, ChEBI:CHEBI:15378, ChEBI:CHEBI:49713;
CC         Evidence={ECO:0000305|PubMed:12562793};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70432;
CC         Evidence={ECO:0000305|PubMed:12562793};
CC   -!- ACTIVITY REGULATION: Activity is regulated by pH (PubMed:12562793).
CC       Active at alkaline pH (PubMed:12562793). {ECO:0000269|PubMed:12562793}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.65 mM for Na(+) {ECO:0000269|PubMed:12562793};
CC         KM=0.052 mM for Li(+) {ECO:0000269|PubMed:12562793};
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01844}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01844}.
CC   -!- INDUCTION: Induced by sodium, lithium and potassium.
CC       {ECO:0000269|PubMed:10781565}.
CC   -!- DISRUPTION PHENOTYPE: The growth of the inactivated mutant is not
CC       restricted at various pH and NaCl concentrations, although it is
CC       inhibited in the presence of LiCl at pH 8.5.
CC       {ECO:0000269|PubMed:10781565}.
CC   -!- SIMILARITY: Belongs to the NhaA Na(+)/H(+) (TC 2.A.33) antiporter
CC       family. {ECO:0000255|HAMAP-Rule:MF_01844, ECO:0000305}.
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DR   EMBL; AF051158; AAC33562.1; -; Genomic_DNA.
DR   EMBL; AE003852; AAF94778.1; -; Genomic_DNA.
DR   PIR; B82177; B82177.
DR   RefSeq; WP_001281946.1; NC_002505.1.
DR   AlphaFoldDB; O85187; -.
DR   SMR; O85187; -.
DR   STRING; 243277.VC_1627; -.
DR   DNASU; 2613882; -.
DR   EnsemblBacteria; AAF94778; AAF94778; VC_1627.
DR   KEGG; vch:VC_1627; -.
DR   PATRIC; fig|243277.26.peg.1555; -.
DR   eggNOG; COG3004; Bacteria.
DR   HOGENOM; CLU_015803_1_0_6; -.
DR   Proteomes; UP000000584; Chromosome I.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0015385; F:sodium:proton antiporter activity; IBA:GO_Central.
DR   GO; GO:0006885; P:regulation of pH; IEA:InterPro.
DR   Gene3D; 1.20.1530.10; Na+/H+ antiporter like domain; 1.
DR   HAMAP; MF_01844; NhaA; 1.
DR   InterPro; IPR023171; Na/H_antiporter_dom_sf.
DR   InterPro; IPR004670; NhaA.
DR   NCBIfam; TIGR00773; NhaA; 1.
DR   NCBIfam; NF007111; PRK09560.1; 1.
DR   NCBIfam; NF007112; PRK09561.1; 1.
DR   PANTHER; PTHR30341:SF0; NA(+)_H(+) ANTIPORTER NHAA; 1.
DR   PANTHER; PTHR30341; SODIUM ION/PROTON ANTIPORTER NHAA-RELATED; 1.
DR   Pfam; PF06965; Na_H_antiport_1; 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..382
FT                   /note="Na(+)/H(+) antiporter NhaA"
FT                   /id="PRO_0000334456"
FT   TRANSMEM        14..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01844"
FT   TRANSMEM        47..67
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01844"
FT   TRANSMEM        87..107
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01844"
FT   TRANSMEM        117..137
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01844"
FT   TRANSMEM        146..166
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01844"
FT   TRANSMEM        171..191
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01844"
FT   TRANSMEM        205..225
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01844"
FT   TRANSMEM        247..267
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01844"
FT   TRANSMEM        271..291
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01844"
FT   TRANSMEM        296..316
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01844"
FT   TRANSMEM        321..341
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01844"
FT   TRANSMEM        353..373
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01844"
SQ   SEQUENCE   382 AA;  40316 MW;  547A5E0586C525E4 CRC64;
     MSDMIRDFFK MESAGGILLV IAAAIAMVIA NSAMGEGYQA FLHTYVFGMS VSHWINDGLM
     AVFFLLIGLE VKRELLEGAL KSRETAIFPA IAAVGGMLAP ALIYVAFNFN DPAAIQGWAI
     PAATDIAFAL GIMALLGKRV PVSLKVFLLA LAIIDDLGVV VIIALFYSSD LSTIALTIGF
     IMTGVLFMLN AKHVTKLSIY LVAGLILWIA VLKSGVHATL AGVVIGFAIP LKGNKGEHSP
     LKHLEHALHP YVAFAILPVF AFANAGISLQ GVSLAGLTSM LPLGVALGLF LGKPLGIFSF
     SWAAVKLGVA KLPEGINFKH IFAVSVLCGI GFTMSIFISS LAFGQANEAY DTYARLGILM
     GSTTAALLGY SLLRLSLPLK KA
//