NHAP2_VIBC3
ID NHAP2_VIBC3 Reviewed; 581 AA.
AC A5F4U3;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=K(+)/H(+) antiporter NhaP2 {ECO:0000255|HAMAP-Rule:MF_01075};
DE AltName: Full=Potassium/proton antiporter NhaP2 {ECO:0000255|HAMAP-Rule:MF_01075};
GN Name=nhaP2 {ECO:0000255|HAMAP-Rule:MF_01075};
GN OrderedLocusNames=VC0395_A2276, VC395_2816;
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 [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 [2]
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 [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RX PubMed=20163190; DOI=10.1021/bi902173y;
RA Resch C.T., Winogrodzki J.L., Patterson C.T., Lind E.J., Quinn M.J.,
RA Dibrov P., Hase C.C.;
RT "The putative Na+/H+ antiporter of Vibrio cholerae, Vc-NhaP2, mediates the
RT specific K+/H+ exchange in vivo.";
RL Biochemistry 49:2520-2528(2010).
CC -!- FUNCTION: K(+)/H(+) antiporter that extrudes potassium in exchange for
CC external protons and maintains the internal concentration of potassium
CC under toxic levels (PubMed:20163190). In vitro, can also catalyze
CC Rb(+)/H(+), Na(+)/H(+) and, possibly, Li(+)/K(+) exchange, but not
CC Li(+)/H(+) exchange. Nonelectrogenic antiporter that exchanges one
CC cation per proton (PubMed:20163190). {ECO:0000269|PubMed:20163190}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(out) + K(+)(in) = H(+)(in) + K(+)(out);
CC Xref=Rhea:RHEA:29467, ChEBI:CHEBI:15378, ChEBI:CHEBI:29103;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01075,
CC ECO:0000269|PubMed:20163190};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29468;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01075,
CC ECO:0000269|PubMed:20163190};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.62 mM for potassium {ECO:0000269|PubMed:20163190};
CC KM=5.95 mM for potassium (in the presence of 20 mM NaCl)
CC {ECO:0000269|PubMed:20163190};
CC KM=9.0 mM for potassium (in the presence of 20 mM LiCl)
CC {ECO:0000269|PubMed:20163190};
CC KM=1.04 mM for sodium {ECO:0000269|PubMed:20163190};
CC pH dependence:
CC Optimum pH is 7.75. Inactive below pH 6.5.
CC {ECO:0000269|PubMed:20163190};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01075, ECO:0000269|PubMed:20163190}; Multi-pass membrane
CC protein {ECO:0000255|HAMAP-Rule:MF_01075, ECO:0000269|PubMed:20163190}.
CC -!- SIMILARITY: Belongs to the monovalent cation:proton antiporter 1 (CPA1)
CC transporter (TC 2.A.36) family. NhaP2 subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_01075}.
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DR EMBL; CP000627; ABQ21367.1; -; Genomic_DNA.
DR EMBL; CP001235; ACP10800.1; -; Genomic_DNA.
DR RefSeq; WP_000340296.1; NZ_JAACZH010000007.1.
DR AlphaFoldDB; A5F4U3; -.
DR SMR; A5F4U3; -.
DR STRING; 345073.VC395_2816; -.
DR EnsemblBacteria; ABQ21367; ABQ21367; VC0395_A2276.
DR KEGG; vco:VC0395_A2276; -.
DR KEGG; vcr:VC395_2816; -.
DR PATRIC; fig|345073.21.peg.2714; -.
DR eggNOG; COG3263; Bacteria.
DR HOGENOM; CLU_005912_9_2_6; -.
DR OMA; QIGMFVL; -.
DR Proteomes; UP000000249; Chromosome 2.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0015386; F:potassium:proton antiporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006884; P:cell volume homeostasis; IEA:InterPro.
DR Gene3D; 1.20.1530.20; -; 1.
DR Gene3D; 3.30.70.1450; -; 1.
DR HAMAP; MF_01075; NhaP2; 1.
DR InterPro; IPR006153; Cation/H_exchanger.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR038770; Na+/solute_symporter_sf.
DR InterPro; IPR030151; NhaP.
DR InterPro; IPR023729; NhaP2.
DR InterPro; IPR006037; RCK_C.
DR InterPro; IPR036721; RCK_C_sf.
DR InterPro; IPR005170; Transptr-assoc_dom.
DR PANTHER; PTHR32507:SF7; PTHR32507:SF7; 1.
DR Pfam; PF03471; CorC_HlyC; 1.
DR Pfam; PF00999; Na_H_Exchanger; 1.
DR Pfam; PF02080; TrkA_C; 1.
DR SMART; SM01091; CorC_HlyC; 1.
DR SUPFAM; SSF116726; SSF116726; 1.
DR SUPFAM; SSF56176; SSF56176; 1.
DR PROSITE; PS51202; RCK_C; 1.
PE 1: Evidence at protein level;
KW Antiport; Cell inner membrane; Cell membrane; Ion transport; Membrane;
KW Potassium; Potassium transport; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..581
FT /note="K(+)/H(+) antiporter NhaP2"
FT /id="PRO_0000423828"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01075"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01075"
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01075"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01075"
FT TRANSMEM 109..129
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01075"
FT TRANSMEM 195..215
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01075"
FT TRANSMEM 232..252
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01075"
FT TRANSMEM 271..291
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01075"
FT TRANSMEM 304..324
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01075"
FT TRANSMEM 335..355
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01075"
FT TRANSMEM 364..384
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01075"
FT DOMAIN 405..486
FT /note="RCK C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01075"
SQ SEQUENCE 581 AA; 62656 MW; D510E88F4981B679 CRC64;
MDAVTINSFF MIGALLIGIS VLLSPVSSKL GIPILLVFLA VGMLAGEDGI GQIAFDNYPV
AYLVSNLALA IILLDGGMRT RVASFRVAFW PSVSLATLGV AVTTLLTGLL AMWLFNLSLL
QGVLVGAIVG STDAAAVFSL LKGRSLNERV GATLEIESGT NDPMAVFLTV TLIAVLGSAE
TNLSAGFLLL SFAQQFGVGA LLGLAGGWIL WWLINRNQLP EGLYSILAVS GGLMIFALSN
ALGGSGILSI YLTGLLLGNR PTRSRHAILN VLDGMTWLAQ IGMFLVLGLL VTPSELMEIA
LPGLALAVGM ILFARPIAVW IGLAPFKSFT AREKWFVSWV GLRGAVPIIL AVFPMMAGLP
NAQLYFNLAF FVVMVSLVVQ GGTLTKAMSL AKVELPPKPE PISRTGVEIY PTSEWELFIY
KLKADKWCIG EPLRNLFMPE GTRIAAVFRD NQLLHPSGST ELCEGDTLCV MAQERDLESL
SRLFSEAPEK ASLARFFGDF FLDIEAKLQD VALLYGLDLG ELEADAKLKD LVLEHLGETP
VLGDYFEWHG LQWVVADVVD WKVTKIGLRL PPEEELQEGA E
