ID NHAP2_ECO7I Reviewed; 578 AA.
AC B7NUV2;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 79.
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=ECIAI39_1522;
OS Escherichia coli O7:K1 (strain IAI39 / ExPEC).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IAI39 / ExPEC;
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
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 -!- 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 PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29468;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01075};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01075}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01075}.
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; CU928164; CAR17654.1; -; Genomic_DNA.
DR RefSeq; WP_000340206.1; NC_011750.1.
DR RefSeq; YP_002407522.1; NC_011750.1.
DR AlphaFoldDB; B7NUV2; -.
DR SMR; B7NUV2; -.
DR STRING; 585057.ECIAI39_1522; -.
DR GeneID; 75203304; -.
DR KEGG; ect:ECIAI39_1522; -.
DR PATRIC; fig|585057.6.peg.1591; -.
DR HOGENOM; CLU_005912_9_2_6; -.
DR Proteomes; UP000000749; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; Regulator of K+ conductance, C-terminal domain; 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; IPR023729; NhaP2.
DR InterPro; IPR006037; RCK_C.
DR InterPro; IPR036721; RCK_C_sf.
DR InterPro; IPR005170; Transptr-assoc_dom.
DR PANTHER; PTHR32507:SF7; K(+)_H(+) ANTIPORTER NHAP2; 1.
DR PANTHER; PTHR32507; NA(+)/H(+) ANTIPORTER 1; 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; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR SUPFAM; SSF116726; TrkA C-terminal domain-like; 1.
DR PROSITE; PS51202; RCK_C; 1.
PE 3: Inferred from homology;
KW Antiport; Cell inner membrane; Cell membrane; Ion transport; Membrane;
KW Potassium; Potassium transport; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..578
FT /note="K(+)/H(+) antiporter NhaP2"
FT /id="PRO_1000136701"
FT TRANSMEM 6..26
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 156..176
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 216..236
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01075"
FT TRANSMEM 237..257
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01075"
FT TRANSMEM 270..290
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01075"
FT TRANSMEM 293..313
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01075"
FT TRANSMEM 334..354
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01075"
FT TRANSMEM 363..383
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01075"
FT DOMAIN 403..485
FT /note="RCK C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01075"
SQ SEQUENCE 578 AA; 62205 MW; CB410D7750C59C59 CRC64;
MDATTIISLF ILGSILVTSS ILLSSFSSRL GIPILVIFLA IGMLAGVDGV GGIPFDNYPF
AYMVSNLALA IILLDGGMRT QASSFRVALG PALSLATLGV LITSGLTGMM AAWLFNLDLI
EGLLIGAIVG STDAAAVFSL LGGKGLNERV GSTLEIESGS NDPMAVFLTI TLIAMIQQHE
SSVSWMFVVD ILQQFGLGIV IGLGGGYLLL QMINRIALPA GLYPLLALSG GILIFALTTA
LEGSGILAVY LCGFLLGNRP IRNRYGILQN FDGLAWLAQI AMFLVLGLLV NPSDLLPIAI
PALILSAWMI FFARPLSVFA GLLPFRGFNL RERVFISWVG LRGAVPIILA VFPMMAGLEN
ARLFFNVAFF VVLVSLLLQG TSLSWAAKKA KVVVPPVGRP VSRVGLDIHP ENPWEQFVYQ
LSADKWCVGA ALRDLHMPKE TRIAALFRDN QLLHPTGSTR LREGDVLCVI GRERDLPALG
KLFSQSPPVA LDQRFFGDFI LEASAKYADV ALIYGLEDGR EYRDKQQTLG EIVQQLLGAA
PVVGDQVEFA GMIWTVAEKE DNEVLKIGVR VAEEEAES
//
