ID A0A0A1I492_9PSED Unreviewed; 580 AA.
AC A0A0A1I492;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 52.
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=BN844_4864 {ECO:0000313|EMBL:CDF97089.1};
OS Pseudomonas sp. SHC52.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=984195 {ECO:0000313|EMBL:CDF97089.1, ECO:0000313|Proteomes:UP000031550};
RN [1] {ECO:0000313|EMBL:CDF97089.1, ECO:0000313|Proteomes:UP000031550}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SHC52 {ECO:0000313|EMBL:CDF97089.1,
RC ECO:0000313|Proteomes:UP000031550};
RA Van der Voort M., Mendes R., Raaijmakers J.M.;
RT "Genome mining of the rhizosphere bacterium Pseudomonas sp. SH-C52.";
RL Submitted (MAY-2013) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CDF97089.1}.
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DR EMBL; CBLV010000361; CDF97089.1; -; Genomic_DNA.
DR RefSeq; WP_041024591.1; NZ_CBLV010000361.1.
DR AlphaFoldDB; A0A0A1I492; -.
DR OrthoDB; 9810759at2; -.
DR Proteomes; UP000031550; 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};
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..54
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01075"
FT TRANSMEM 60..77
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01075"
FT TRANSMEM 89..112
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01075"
FT TRANSMEM 118..140
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01075"
FT TRANSMEM 161..178
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01075"
FT TRANSMEM 190..209
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01075"
FT TRANSMEM 221..237
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01075"
FT TRANSMEM 272..291
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01075"
FT TRANSMEM 297..322
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01075"
FT TRANSMEM 334..354
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01075"
FT TRANSMEM 360..377
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01075"
FT DOMAIN 402..484
FT /note="RCK C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51202"
SQ SEQUENCE 580 AA; 61345 MW; 80F55CAC00DCC2E8 CRC64;
MTATTINSLF LIGALLVGAS ILVSSLSSRL GIPILVIILA VGMVAGVDGA GILFDNYATA
YLVGNLALAV ILLDGGLRTR VSSFRVALWP ALSLATIGVL ITTGLTGLAA AWLFNLNLIQ
GLLIGAIVGS TDAAAVFSLL GGKGLNERVS ASLEIESGSN DPMAVFLTVT LIGMLASGQT
DLEWNLVGHL VREFGIGAVL GLGGGWLMLQ LVNRINLANG LYPILVISGG LAVFALTNAL
HGSGFLAVYL CGLVIGNRPV RSRHGILHML DGMAWLAQIG MFLVLGLLVT PHDLLPIALP
ALGLALWMIL FARPLSVIVG LLPFKAFHGR EKAFISWVGL RGAVPIILAV FPLMAGLPHA
QLYFNLAFFI VLVSLLVQGT SLPWVAKLLH VTVPPEPLPI SRAALEVHVT SEWELFIYRL
GAEKWCIGSP LRDLKMPEGT RIAALFRGQQ LLHPSGSTVL ETDDLLCVIG HEHDLPALGK
LFSQAPQRGL DLRFFGDFVL EGDAQLAAVA ALYGLQLDGI DPDMSLGRFI AQKVGGAPVV
GDQVDWNNTL WTVAAMDGNK IGKVGVRFPE GSRPGPGLFL
//
