ID A0A1H2VVZ8_9PSED Unreviewed; 581 AA.
AC A0A1H2VVZ8;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=K(+)/H(+) antiporter NhaP2 {ECO:0000256|HAMAP-Rule:MF_01075};
DE AltName: Full=Potassium/proton antiporter NhaP2 {ECO:0000256|HAMAP-Rule:MF_01075};
GN Name=nhaP2 {ECO:0000256|HAMAP-Rule:MF_01075};
GN ORFNames=SAMN05216287_1358 {ECO:0000313|EMBL:SDW72407.1};
OS Pseudomonas kuykendallii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1007099 {ECO:0000313|EMBL:SDW72407.1, ECO:0000313|Proteomes:UP000243778};
RN [1] {ECO:0000313|Proteomes:UP000243778}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL B-59562 {ECO:0000313|Proteomes:UP000243778};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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:0000256|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:0000256|HAMAP-Rule:MF_01075};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01075};
CC Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_01075}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the monovalent cation:proton antiporter 1 (CPA1)
CC transporter (TC 2.A.36) family. NhaP2 subfamily. {ECO:0000256|HAMAP-
CC Rule:MF_01075}.
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DR EMBL; FNNU01000002; SDW72407.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H2VVZ8; -.
DR STRING; 1007099.SAMN05216287_1358; -.
DR OrthoDB; 9810759at2; -.
DR Proteomes; UP000243778; Unassembled WGS sequence.
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 {ECO:0000256|ARBA:ARBA00022449, ECO:0000256|HAMAP-Rule:MF_01075};
KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_01075};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065, ECO:0000256|HAMAP-
KW Rule:MF_01075};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01075};
KW Potassium {ECO:0000256|HAMAP-Rule:MF_01075};
KW Potassium transport {ECO:0000256|ARBA:ARBA00022538, ECO:0000256|HAMAP-
KW Rule:MF_01075}; Reference proteome {ECO:0000313|Proteomes:UP000243778};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_01075};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_01075}; Transport {ECO:0000256|HAMAP-Rule:MF_01075}.
FT TRANSMEM 6..23
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01075"
FT TRANSMEM 30..47
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01075"
FT TRANSMEM 59..78
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01075"
FT TRANSMEM 90..114
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01075"
FT TRANSMEM 120..143
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01075"
FT TRANSMEM 187..210
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01075"
FT TRANSMEM 244..261
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01075"
FT TRANSMEM 273..292
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01075"
FT TRANSMEM 298..323
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01075"
FT TRANSMEM 335..355
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01075"
FT TRANSMEM 361..378
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01075"
FT DOMAIN 404..485
FT /note="RCK C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51202"
SQ SEQUENCE 581 AA; 61587 MW; 5B354CD4650F234C CRC64;
MDAITINSLF LIGALLVGAS ILVSSLSSRL GIPILVIILA VGMVAGIDGP GGIGFSNYPM
AYLVGNLALA IILLDGGLRT RVSSFRVALW PALSMATVGV LITTGLTGMA AAWLFDLNLI
QGLLIGAIVG STDAAAVFSL LGGKGLNERV NATLEIESGS NDPMAVFLTV TLIDMLAKGQ
TGVDIGFLGH LLSEFGIGAL LGLGGGWLLL QMINRIHLAH GLYPLLVISG GLMIFALTNT
LHGSGILAVY LCGLVLGNRP IRSRHSILHM LDGMAWLAQI GMFLVLGLLV TPHDLLPIAI
PALGLALWMI LIARPLSVLI GLWPFRAFHD REKAFIAWVG LRGAVPIILA VFPLMAGLPH
AQLYFNLAFF IVLVSLLVQG TSLPWAAKLL RVTVPPAPAP ISRAGLEVHP TSEWELFVYR
LGAEKWCIGA ALRELKMPED TRIAALFRGT DLLHPSGSTT LEAGDILCVI GHDRDLPALG
KLFSQAPKRG QDLRFFGDFV LEADAELGAI GALYGLQLDD LDGSQPLGRF IARQIGGEPI
VGDQVEWKGL TWTVASMDGN RIGKVGVRFP EGGRPGPGLF L
//
