NHAB_VIBAL
ID NHAB_VIBAL Reviewed; 528 AA.
AC Q56577;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 69.
DE RecName: Full=Na(+)/H(+) antiporter NhaB {ECO:0000255|HAMAP-Rule:MF_01599, ECO:0000303|PubMed:8695633};
DE AltName: Full=Sodium/proton antiporter NhaB {ECO:0000255|HAMAP-Rule:MF_01599};
GN Name=nhaB {ECO:0000255|HAMAP-Rule:MF_01599, ECO:0000303|PubMed:8695633};
OS Vibrio alginolyticus.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=663;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=138-2;
RX PubMed=8695633; DOI=10.1016/0005-2728(96)00034-5;
RA Nakamura T., Enomoto H., Unemoto T.;
RT "Cloning and sequencing of nhaB gene encoding an Na+/H+ antiporter from
RT Vibrio alginolyticus.";
RL Biochim. Biophys. Acta 1275:157-160(1996).
RN [2]
RP SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=9518558; DOI=10.1016/s0005-2736(97)00245-9;
RA Enomoto H., Unemoto T., Nishibuchi M., Padan E., Nakamura T.;
RT "Topological study of Vibrio alginolyticus NhaB Na+/H+ antiporter using
RT gene fusions in Escherichia coli cells.";
RL Biochim. Biophys. Acta 1370:77-86(1998).
RN [3]
RP FUNCTION, AND MUTAGENESIS OF ASP-147.
RX PubMed=11544242; DOI=10.1128/jb.183.19.5762-5767.2001;
RA Nakamura T., Fujisaki Y., Enomoto H., Nakayama Y., Takabe T., Yamaguchi N.,
RA Uozumi N.;
RT "Residue aspartate-147 from the third transmembrane region of Na(+)/H(+)
RT antiporter NhaB of Vibrio alginolyticus plays a role in its activity.";
RL J. Bacteriol. 183:5762-5767(2001).
CC -!- FUNCTION: Na(+)/H(+) antiporter that extrudes sodium in exchange for
CC external protons. {ECO:0000255|HAMAP-Rule:MF_01599,
CC ECO:0000269|PubMed:11544242}.
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 PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29248;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01599};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:9518558};
CC Multi-pass membrane protein {ECO:0000269|PubMed:9518558}.
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; D83728; BAA12086.1; -; Genomic_DNA.
DR AlphaFoldDB; Q56577; -.
DR STRING; 663.BAU10_09505; -.
DR eggNOG; COG3067; Bacteria.
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:0015385; F:sodium:proton antiporter activity; IEA:InterPro.
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 Sodium; Sodium transport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..528
FT /note="Na(+)/H(+) antiporter NhaB"
FT /id="PRO_0000333144"
FT TOPO_DOM 1..23
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:9518558"
FT TRANSMEM 24..46
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 47..95
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:9518558"
FT TRANSMEM 96..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 119..129
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:9518558"
FT TRANSMEM 130..163
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 164..239
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:9518558"
FT TRANSMEM 240..262
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 263..297
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:9518558"
FT TRANSMEM 298..317
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 318..320
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:9518558"
FT TRANSMEM 321..340
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 341..352
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:9518558"
FT TRANSMEM 353..375
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 376..389
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:9518558"
FT TRANSMEM 390..412
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 413..477
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:9518558"
FT TRANSMEM 478..500
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 501..528
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:9518558"
FT SITE 147
FT /note="Important for antiport activity"
FT MUTAGEN 147
FT /note="D->E: Loss of antiport activity at pH 8.5. No change
FT in activity at pH 7.0."
FT /evidence="ECO:0000269|PubMed:11544242"
FT MUTAGEN 147
FT /note="D->G,M,T: Loss of antiport activity, both at pH 8.5
FT and at pH 7.0."
FT /evidence="ECO:0000269|PubMed:11544242"
SQ SEQUENCE 528 AA; 57215 MW; 469F007E38688C6E CRC64;
MPISLGNAFI KNFLGKAPDW YKVAIIAFLI INPIVFFLIN PFVAGWLLVA EFIFTLAMAL
KCYPLQPGGL LAIEAIAIGM TSPAQVKHEL VANIEVLLLL VFMVAGIYFM KHLLLFIFTK
ILLGIRSKTL LSLAFCFAAA FLSAFLDALT VIAVVISVAI GFYSIYHKVA SGNPIGDHDH
TQDDTITELT RDDLENYRAF LRSLLMHAGV GTALGGVTTM VGEPQNLIIA DQAGWLFGEF
LIRMSPVTLP VFFCGLITCA LVEKLKVFGY GAKLPNNVRQ ILVDFDNEER KTRTNQDVAK
LWVQGLIAVW LIVALALHLA AVGLIGLSVI ILATAFTGVI EEHSMGKAFE EALPFTALLA
VFFSIVAVII DQELFKPVID AVLAVEDKGT QLALFYVANG LLSMVSDNVF VGTVYINEVK
TALIEGLITR EQFDLLAVAI NTGTNLPSVA TPNGQAAFLF LLTSALAPLI RLSYGRMVIM
ALPYTIVLAI VGLMGIMFFL EPATASFYDA GWILPHSGDL TPVVSGGH
