NHAP2_PSEP1
ID NHAP2_PSEP1 Reviewed; 580 AA.
AC A5WA99;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 87.
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=Pput_4939;
OS Pseudomonas putida (strain ATCC 700007 / DSM 6899 / BCRC 17059 / F1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=351746;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700007 / DSM 6899 / BCRC 17059 / F1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Lykidis A., Parales R., Richardson P.;
RT "Complete sequence of Pseudomonas putida F1.";
RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000712; ABQ81059.1; -; Genomic_DNA.
DR RefSeq; WP_010955613.1; NC_009512.1.
DR AlphaFoldDB; A5WA99; -.
DR SMR; A5WA99; -.
DR STRING; 351746.Pput_4939; -.
DR PRIDE; A5WA99; -.
DR EnsemblBacteria; ABQ81059; ABQ81059; Pput_4939.
DR KEGG; ppf:Pput_4939; -.
DR eggNOG; COG3263; Bacteria.
DR HOGENOM; CLU_005912_9_2_6; -.
DR OMA; QIGMFVL; -.
DR OrthoDB; 1194802at2; -.
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 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..580
FT /note="K(+)/H(+) antiporter NhaP2"
FT /id="PRO_1000064670"
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 57..77
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01075"
FT TRANSMEM 86..106
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01075"
FT TRANSMEM 108..128
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01075"
FT TRANSMEM 162..182
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01075"
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01075"
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01075"
FT TRANSMEM 240..260
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01075"
FT TRANSMEM 269..289
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01075"
FT TRANSMEM 292..312
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 362..382
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01075"
FT DOMAIN 402..484
FT /note="RCK C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01075"
SQ SEQUENCE 580 AA; 61351 MW; 73DB9174F5F5BBD7 CRC64;
MDASTINSLF LIGALLVGAS ILVSSLSSRL GIPILVIILA VGMLAGVDGG GIIFNNYPTA
YLVGNLALAV ILLDGGLRTR VASFRVALWP ALSLATVGVM ITTALTGLIA AWLFNLSLIQ
GLLIGAIVGS TDAAAVFSLL GGKGLNERVS ATLEIESGSN DPMAVFLTVT LIDMIASGET
GLHWSLLGHL LREFGIGTLL GLGGGWLMLQ LVNRINLAGG LYPILVVAGG LVMFSLTNAL
HGSGFLAVYL CGLVLGNKPI RSRHGILHML DGMAWLAQIG MFLVLGLLVT PHDLLPIALP
ALGLALWMIL VARPLSVVAA LLPFKAFHGR EKGFISWVGL RGAVPIILAV FPLMAGLPDA
QLFFNLAFFI VLVSLLVQGT SLPWVAKLLK VTVPPDPAPI SRSALEVHIT SEWEMFVYRL
GAEKWCIGAA LRELKMPEGT RIAALFRGEQ LLHPSGSTVL EVGDMLCVIG HEHNLPALGK
LFSQAPQRGL DLRFFGDFVL EGDAELGAVA ALYGLKLDGL DAKMPLAQFI RQKVGGAPVV
GDQVEWHGTI WTVATMDGNK IQKVGVRFPE GTRPGPGLFL
