NHAP2_VIBPA
ID NHAP2_VIBPA Reviewed; 581 AA.
AC Q87KV8;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 102.
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}; Synonyms=cvrA;
GN OrderedLocusNames=VP2867;
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 [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 [2]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, 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: K(+)/H(+) antiporter that extrudes potassium in exchange for
CC external protons and maintains the internal concentration of potassium
CC under toxic levels. {ECO:0000255|HAMAP-Rule:MF_01075,
CC ECO:0000269|PubMed:16390457}.
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:16390457};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29468;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01075,
CC ECO:0000269|PubMed:16390457};
CC -!- ACTIVITY REGULATION: May function more efficiently in K(+)
CC concentrations higher than 10 mM. {ECO:0000269|PubMed:16390457}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Active at alkaline pH. {ECO:0000269|PubMed:16390457};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01075, ECO:0000269|PubMed:16390457}; Multi-pass membrane
CC protein {ECO:0000255|HAMAP-Rule:MF_01075, ECO:0000269|PubMed:16390457}.
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; BA000031; BAC61130.1; -; Genomic_DNA.
DR RefSeq; NP_799246.1; NC_004603.1.
DR RefSeq; WP_005478599.1; NC_004603.1.
DR AlphaFoldDB; Q87KV8; -.
DR SMR; Q87KV8; -.
DR STRING; 223926.28807893; -.
DR TCDB; 2.A.36.6.3; the monovalent cation:proton antiporter-1 (cpa1) family.
DR EnsemblBacteria; BAC61130; BAC61130; BAC61130.
DR GeneID; 1190430; -.
DR KEGG; vpa:VP2867; -.
DR PATRIC; fig|223926.6.peg.2759; -.
DR eggNOG; COG3263; Bacteria.
DR HOGENOM; CLU_005912_9_2_6; -.
DR OMA; QIGMFVL; -.
DR Proteomes; UP000002493; Chromosome 1.
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; 3.30.465.10; -; 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; IPR016169; FAD-bd_PCMH_sub2.
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; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..581
FT /note="K(+)/H(+) antiporter NhaP2"
FT /id="PRO_0000052398"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01075"
FT TRANSMEM 34..54
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 95..115
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01075"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01075"
FT TRANSMEM 163..183
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01075"
FT TRANSMEM 185..205
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01075"
FT TRANSMEM 233..253
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01075"
FT TRANSMEM 281..301
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; 62639 MW; FD702247ED121455 CRC64;
MDADTINSFF LIGALLIALS VLLSPVSSKL GIPILLVFLA VGMLAGEDGL GGILFDNYSI
AYLVSNLALA IILLDGGMRT RVASFRVALW PSVSLATIGV AITTLLTGLM ATWLFDLDLL
QGILVGAIVG STDAAAVFSL LKGRSLNERV GSTLEIESGT NDPMAVFLTV TLIAILSSTG
TGLSAGFLAL SFVKQFGIGA LLGFAGGWVL WKVINRNQLP DGLYSILTVS GGLIIFALSN
SLGGSGILSI YLVGLLLGNR PTRSRHSILH VLDGMTWLAQ IGMFLVLGLL VTPSNLLSIA
VPGLALAFGM ILFARPISVW IGLLPFKSFT PREKWFVSWV GLRGAVPIIL AVFPMMAGLP
DAQLYFNLAF FVVMVSLIVQ GGTLTKAMSL AKVELPPKPE PISRTGVEIY PTSEWELFIY
RLKADKWCIG EPLRSLSMPE GTRIAAVFRN QELLHPSGST RLEEDDTLCV LAQEKDLAAL
SLLFSEAPEK ASLTRFFGDF FLDIEVKLAD VAMMYGLNLG YELQDKTLSN IVEEQLGSTP
VLGDQFEWQG LQWVIADVVD HQVTKVGLRL PNEEEEGEEE D
