NHAA_VIBPA
ID NHAA_VIBPA Reviewed; 383 AA.
AC Q56725;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 114.
DE RecName: Full=Na(+)/H(+) antiporter NhaA {ECO:0000303|PubMed:7896730};
DE AltName: Full=Sodium/proton antiporter NhaA {ECO:0000255|HAMAP-Rule:MF_01844};
GN Name=nhaA {ECO:0000303|PubMed:7896730}; OrderedLocusNames=VP1228;
OS Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=223926;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, ACTIVITY REGULATION, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=AQ3334;
RX PubMed=7896730; DOI=10.1093/oxfordjournals.jbchem.a124624;
RA Kuroda T., Shimamoto T., Inaba K., Tsuda M., Tsuchiya T.;
RT "Properties and sequence of the NhaA Na+/H+ antiporter of Vibrio
RT parahaemolyticus.";
RL J. Biochem. 116:1030-1038(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIMD 2210633;
RX PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT distinct from that of V. cholerae.";
RL Lancet 361:743-749(2003).
RN [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=RIMD 2210633;
RX PubMed=16390457; DOI=10.1111/j.1365-2958.2005.04966.x;
RA Radchenko M.V., Waditee R., Oshimi S., Fukuhara M., Takabe T., Nakamura T.;
RT "Cloning, functional expression and primary characterization of Vibrio
RT parahaemolyticus K+/H+ antiporter genes in Escherichia coli.";
RL Mol. Microbiol. 59:651-663(2006).
CC -!- FUNCTION: Na(+)/H(+) antiporter that extrudes sodium in exchange for
CC external protons (PubMed:7896730, PubMed:16390457). Can also transport
CC lithium and potassium (PubMed:16390457, PubMed:7896730).
CC {ECO:0000269|PubMed:16390457, ECO:0000269|PubMed:7896730}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+)(out) + Na(+)(in) = 2 H(+)(in) + Na(+)(out);
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=2 H(+)(out) + Li(+)(in) = 2 H(+)(in) + Li(+)(out);
CC Xref=Rhea:RHEA:70431, ChEBI:CHEBI:15378, ChEBI:CHEBI:49713;
CC Evidence={ECO:0000305|PubMed:7896730};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70432;
CC Evidence={ECO:0000305|PubMed:7896730};
CC -!- ACTIVITY REGULATION: Activity is regulated by pH (PubMed:7896730).
CC Active at alkaline pH (PubMed:7896730). Amiloride strongly reduces
CC affinity for Na(+), but does not change the Vmax (PubMed:7896730).
CC {ECO:0000269|PubMed:7896730}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=36 mM for Na(+) {ECO:0000269|PubMed:7896730};
CC KM=24 mM for Li(+) {ECO:0000269|PubMed:7896730};
CC pH dependence:
CC Optimum pH is 8.5. Activity is null at pH 7.0 and increases as the pH
CC increases from 7.0 to 8.5. {ECO:0000269|PubMed:7896730};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:16390457}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_01844}.
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; D28504; BAA05864.1; -; Genomic_DNA.
DR EMBL; BA000031; BAC59491.1; -; Genomic_DNA.
DR PIR; JX0360; JX0360.
DR RefSeq; NP_797607.1; NC_004603.1.
DR RefSeq; WP_005462393.1; NC_004603.1.
DR AlphaFoldDB; Q56725; -.
DR SMR; Q56725; -.
DR STRING; 223926.28806216; -.
DR TCDB; 2.A.33.1.2; the nhaa na(+):h(+) antiporter (nhaa) family.
DR EnsemblBacteria; BAC59491; BAC59491; BAC59491.
DR GeneID; 1188733; -.
DR KEGG; vpa:VP1228; -.
DR PATRIC; fig|223926.6.peg.1168; -.
DR eggNOG; COG3004; Bacteria.
DR HOGENOM; CLU_015803_1_0_6; -.
DR OMA; MGLMLRC; -.
DR Proteomes; UP000002493; Chromosome 1.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015297; F:antiporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0015081; F:sodium ion transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006885; P:regulation of pH; IEA:InterPro.
DR Gene3D; 1.20.1530.10; -; 1.
DR HAMAP; MF_01844; NhaA; 1.
DR InterPro; IPR023171; Na/H_antiporter_dom_sf.
DR InterPro; IPR004670; NhaA.
DR PANTHER; PTHR30341; PTHR30341; 1.
DR Pfam; PF06965; Na_H_antiport_1; 1.
DR TIGRFAMs; TIGR00773; NhaA; 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..383
FT /note="Na(+)/H(+) antiporter NhaA"
FT /id="PRO_0000334460"
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 252..272
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01844"
FT TRANSMEM 280..300
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 356..376
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01844"
SQ SEQUENCE 383 AA; 40433 MW; 9EE53D008D2FD6A2 CRC64;
MNDVIRDFFK MESAGGILLV IAAAIAMTIA NSPLGETYQS LLHTYVFGMS VSHWINDGLM
AVFFLLIGLE VKRELLEGAL KSKETAIFPA IAAVGGMLAP ALIYVAFNAN DPEAISGWAI
PAATDIAFAL GIMALLGKRV PVSLKVFLLA LAIIDDLGVV VIIALFYTGD LSSMALLVGF
VMTGVLFMLN AKEVTKLTPY MIVGAILWFA VLKSGVHATL AGVVIGFAIP LKGKQGEHSP
LKHMEHALHP YVAFGILPLF AFANAGISLE GVSMSGLTSM LPLGIALGLL IGKPLGIFSF
SWAAVKLGVA KLPEGINFKH IFAVSVLCGI GFTMSIFISS LAFGNVSPEF DTYARLGILM
GSTTAAVLGY ALLHFSLPKK AQD
