NHAP2_ECOLI
ID NHAP2_ECOLI Reviewed; 578 AA.
AC P76007; O07654;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 2.
DT 03-AUG-2022, entry version 152.
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=cvrA; Synonyms=nhaP2, ycgO; OrderedLocusNames=b1191, JW5184;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP FUNCTION IN CELL VOLUME REGULATION.
RC STRAIN=GR70N;
RX PubMed=11700351; DOI=10.1099/00221287-147-11-3005;
RA Verkhovskaya M.L., Barquera B., Wikstroem M.;
RT "Deletion of one of two Escherichia coli genes encoding putative Na+/H+
RT exchangers (ycgO) perturbs cytoplasmic alkali cation balance at low
RT osmolarity.";
RL Microbiology 147:3005-3013(2001).
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 (By similarity). Participates in control of cell
CC volume in low-osmolarity conditions. {ECO:0000255|HAMAP-Rule:MF_01075,
CC ECO:0000269|PubMed:11700351}.
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; U00096; AAC74275.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA36046.2; -; Genomic_DNA.
DR PIR; D64865; D64865.
DR RefSeq; NP_415709.2; NC_000913.3.
DR RefSeq; WP_000340194.1; NZ_LN832404.1.
DR AlphaFoldDB; P76007; -.
DR SMR; P76007; -.
DR BioGRID; 4261367; 17.
DR BioGRID; 850122; 1.
DR IntAct; P76007; 1.
DR STRING; 511145.b1191; -.
DR TCDB; 2.A.36.6.11; the monovalent cation:proton antiporter-1 (cpa1) family.
DR PaxDb; P76007; -.
DR PRIDE; P76007; -.
DR EnsemblBacteria; AAC74275; AAC74275; b1191.
DR EnsemblBacteria; BAA36046; BAA36046; BAA36046.
DR GeneID; 945755; -.
DR KEGG; ecj:JW5184; -.
DR KEGG; eco:b1191; -.
DR PATRIC; fig|1411691.4.peg.1095; -.
DR EchoBASE; EB3655; -.
DR eggNOG; COG3263; Bacteria.
DR HOGENOM; CLU_005912_9_2_6; -.
DR InParanoid; P76007; -.
DR OMA; QIGMFVL; -.
DR PhylomeDB; P76007; -.
DR BioCyc; EcoCyc:YCGO-MON; -.
DR PRO; PR:P76007; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; ISM:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
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; IMP:EcoCyc.
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..578
FT /note="K(+)/H(+) antiporter NhaP2"
FT /id="PRO_0000052381"
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 183..203
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; 62285 MW; 4637F874E527334A CRC64;
MDATTIISLF ILGSILVTSS ILLSSFSSRL GIPILVIFLA IGMLAGVDGV GGIPFDNYPF
AYMVSNLALA IILLDGGMRT QASSFRVALG PALSLATLGV LITSGLTGMM AAWLFNLDLI
EGLLIGAIVG STDAAAVFSL LGGKGLNERV GSTLEIESGS NDPMAVFLTI TLIAMIQHHE
SNISWMFIVD ILQQFGLGIV IGLGGGYLLL QMINRIALPA GLYPLLALSG GILIFSLTTA
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
