NHAD_VIBC3
ID NHAD_VIBC3 Reviewed; 477 AA.
AC A5F120; Q7DCN4; Q9EYG4; Q9KKT5;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 25-MAY-2022, entry version 66.
DE RecName: Full=Na(+)/H(+) antiporter NhaD;
DE AltName: Full=Sodium/proton antiporter NhaD;
GN Name=nhaD; OrderedLocusNames=VC0395_0225, VC395_A1039;
OS Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 /
OS O395).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=345073;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES,
RP AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RX PubMed=11936836; DOI=10.1023/a:1017932829927;
RA Dzioba J., Ostroumov E., Winogrodzki A., Dibrov P.;
RT "Cloning, functional expression in Escherichia coli and primary
RT characterization of a new Na+/H+ antiporter, NhaD, of Vibrio cholerae.";
RL Mol. Cell. Biochem. 229:119-124(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RA Heidelberg J.;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RX PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA Wang W., Wang J., Qian W., Li D., Wang L.;
RT "A recalibrated molecular clock and independent origins for the cholera
RT pandemic clones.";
RL PLoS ONE 3:E4053-E4053(2008).
RN [4]
RP PROTEIN SEQUENCE OF 1-13, FUNCTION, AND MUTAGENESIS OF GLU-100; GLU-251;
RP GLU-342; ASP-344; THR-345 AND ASP-393.
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RX PubMed=12101001; DOI=10.1016/s0005-2736(02)00407-8;
RA Ostroumov E., Dzioba J., Loewen P.C., Dibrov P.;
RT "Asp(344) and Thr(345) are critical for cation exchange mediated by NhaD,
RT Na(+)/H(+) antiporter of Vibrio cholerae.";
RL Biochim. Biophys. Acta 1564:99-106(2002).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, AND MUTAGENESIS OF HIS-93;
RP SER-150; ASP-154; ASN-155; THR-157; ASN-189; ASP-199; THR-201; THR-202;
RP HIS-210; HIS-274; HIS-278; SER-389; SER-390; ASN-394; SER-425; SER-428;
RP SER-431; HIS-450 AND HIS-468.
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RX PubMed=16186100; DOI=10.1074/jbc.m509328200;
RA Habibian R., Dzioba J., Barrett J., Galperin M.Y., Loewen P.C., Dibrov P.;
RT "Functional analysis of conserved polar residues in Vc-NhaD, Na+/H+
RT antiporter of Vibrio cholerae.";
RL J. Biol. Chem. 280:39637-39643(2005).
CC -!- FUNCTION: Na(+)/H(+) antiporter that extrudes sodium in exchange for
CC external protons. Can also transport lithium.
CC {ECO:0000269|PubMed:11936836, ECO:0000269|PubMed:12101001,
CC ECO:0000269|PubMed:16186100}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.0. Totally inactive at pH 9.0.
CC {ECO:0000269|PubMed:11936836};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:11936836,
CC ECO:0000269|PubMed:16186100}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:11936836, ECO:0000269|PubMed:16186100}.
CC -!- SIMILARITY: Belongs to the NhaD Na(+)/H(+) (TC 2.A.62) antiporter
CC family. {ECO:0000305}.
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DR EMBL; AF331042; AAG48354.2; -; Genomic_DNA.
DR EMBL; CP000626; ABQ19159.1; -; Genomic_DNA.
DR EMBL; CP001236; ACP11869.1; -; Genomic_DNA.
DR PIR; D82390; D82390.
DR RefSeq; WP_000147723.1; NZ_JAACZH010000003.1.
DR AlphaFoldDB; A5F120; -.
DR STRING; 345073.VC395_A1039; -.
DR TCDB; 2.A.62.1.6; the nhad na(+):h(+) antiporter (nhad) family.
DR DNASU; 2612475; -.
DR EnsemblBacteria; ABQ19159; ABQ19159; VC0395_0225.
DR GeneID; 57742369; -.
DR KEGG; vco:VC0395_0225; -.
DR KEGG; vcr:VC395_A1039; -.
DR PATRIC; fig|345073.21.peg.3762; -.
DR eggNOG; COG1055; Bacteria.
DR HOGENOM; CLU_029697_0_0_6; -.
DR OMA; DAHKGFS; -.
DR Proteomes; UP000000249; 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-KW.
DR GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
DR InterPro; IPR004680; Cit_transptr-like_dom.
DR InterPro; IPR045016; NhaD-like.
DR PANTHER; PTHR43269; PTHR43269; 1.
DR Pfam; PF03600; CitMHS; 1.
PE 1: Evidence at protein level;
KW Antiport; Cell inner membrane; Cell membrane; Direct protein sequencing;
KW Ion transport; Membrane; Sodium; Sodium transport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..477
FT /note="Na(+)/H(+) antiporter NhaD"
FT /id="PRO_0000423661"
FT TOPO_DOM 1..33
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 34..51
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 52..60
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 61..78
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 79..94
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 95..112
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 113..132
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 133..150
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 151..154
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 155..171
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 172..181
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 182..206
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 207..220
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 221..238
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 239..258
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 259..277
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 278..281
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 282..299
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 300..344
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 345..362
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 363..378
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 379..403
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 404..413
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 414..438
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 439..454
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 455..472
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 473..477
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MUTAGEN 93
FT /note="H->A: Shifts the pH optimum to more acidic pH."
FT /evidence="ECO:0000269|PubMed:16186100"
FT MUTAGEN 100
FT /note="E->A: No change in activity. Shifts the pH optimum
FT to more alkaline pH."
FT /evidence="ECO:0000269|PubMed:12101001"
FT MUTAGEN 150
FT /note="S->A: Lack of activity."
FT /evidence="ECO:0000269|PubMed:16186100"
FT MUTAGEN 154
FT /note="D->G: Lack of activity."
FT /evidence="ECO:0000269|PubMed:16186100"
FT MUTAGEN 155
FT /note="N->A: Lack of activity."
FT /evidence="ECO:0000269|PubMed:16186100"
FT MUTAGEN 157
FT /note="T->A: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:16186100"
FT MUTAGEN 189
FT /note="N->A: Lack of activity."
FT /evidence="ECO:0000269|PubMed:16186100"
FT MUTAGEN 199
FT /note="D->A: Lack of activity."
FT /evidence="ECO:0000269|PubMed:16186100"
FT MUTAGEN 201
FT /note="T->A: Lack of activity."
FT /evidence="ECO:0000269|PubMed:16186100"
FT MUTAGEN 202
FT /note="T->A: Lack of activity."
FT /evidence="ECO:0000269|PubMed:16186100"
FT MUTAGEN 210
FT /note="H->A: Shifts the pH optimum to more acidic pH."
FT /evidence="ECO:0000269|PubMed:16186100"
FT MUTAGEN 251
FT /note="E->A: No change in activity. Shifts the pH optimum
FT to more alkaline pH."
FT /evidence="ECO:0000269|PubMed:12101001"
FT MUTAGEN 274
FT /note="H->A: No change in activity."
FT /evidence="ECO:0000269|PubMed:16186100"
FT MUTAGEN 278
FT /note="H->A: No change in activity."
FT /evidence="ECO:0000269|PubMed:16186100"
FT MUTAGEN 342
FT /note="E->A: No change in activity. Shifts the pH optimum
FT to more alkaline pH."
FT /evidence="ECO:0000269|PubMed:12101001"
FT MUTAGEN 344
FT /note="D->A,N: Lack of activity."
FT /evidence="ECO:0000269|PubMed:12101001"
FT MUTAGEN 344
FT /note="D->E: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:12101001"
FT MUTAGEN 345
FT /note="T->A: Lack of activity."
FT /evidence="ECO:0000269|PubMed:12101001"
FT MUTAGEN 389
FT /note="S->A: Lack of activity."
FT /evidence="ECO:0000269|PubMed:16186100"
FT MUTAGEN 390
FT /note="S->A: No change in activity."
FT /evidence="ECO:0000269|PubMed:16186100"
FT MUTAGEN 393
FT /note="D->A: No change in activity. Shifts the pH optimum
FT to more alkaline pH."
FT /evidence="ECO:0000269|PubMed:12101001"
FT MUTAGEN 393
FT /note="D->E,N: Lack of activity."
FT /evidence="ECO:0000269|PubMed:12101001"
FT MUTAGEN 394
FT /note="N->G: Lack of activity."
FT /evidence="ECO:0000269|PubMed:16186100"
FT MUTAGEN 425
FT /note="S->A: Lack of activity."
FT /evidence="ECO:0000269|PubMed:16186100"
FT MUTAGEN 428
FT /note="S->A: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:16186100"
FT MUTAGEN 431
FT /note="S->A: Lack of activity."
FT /evidence="ECO:0000269|PubMed:16186100"
FT MUTAGEN 450
FT /note="H->A: No change in activity."
FT /evidence="ECO:0000269|PubMed:16186100"
FT MUTAGEN 468
FT /note="H->A: No change in activity."
FT /evidence="ECO:0000269|PubMed:16186100"
SQ SEQUENCE 477 AA; 52378 MW; 90644FAD3CCE1990 CRC64;
MTGRIALLSL TLFSPLSLAS TPDGQALDFT HSTIGYAALL IFAIAYTLVM LEEYLQLRKS
KPVLLAAGLI WAMIGYVYQQ TGSTEVARQA LEHNLLEYAE LLLFLLVAMT YISAMEERRL
FDALKAWMIN RGFNFHTLFW ITGWLAFFIS PIADNLTTAL LMCAVVMKVG GENPKFVSLA
CINIVIAANA GGAFSPFGDI TTLMVWQAGH VSFLEFMDLF LPSLANYLVP ALVMSLFVPH
QTPSSIQEVV ELKRGAKRIV VLFLFTILSA IGFHAFFHFP PVIGMMMGLA YLQFFGYFLR
KTLARSLAKK TAIAMAKNDE AALKRIGSVV PFDVFRSISH AEWDTLLFFY GVVMCVGGLS
LLGYLGLVSE ILYTEWNPIW ANVLVGLLSS VVDNIPVMFA VLSMQPEMSL GNWLLVTLTA
GVGGSLLSIG SAAGVALMGA AHGKYTFLSH LKWTPVILLG YVVSIVLHLL LNHQSFT
