ID A0A2N5ETH5_9GAMM Unreviewed; 574 AA.
AC A0A2N5ETH5;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=CYR34_02150 {ECO:0000313|EMBL:PLR53412.1};
OS Chimaeribacter arupi.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Chimaeribacter.
OX NCBI_TaxID=2060066 {ECO:0000313|EMBL:PLR53412.1, ECO:0000313|Proteomes:UP000234626};
RN [1] {ECO:0000313|EMBL:PLR53412.1, ECO:0000313|Proteomes:UP000234626}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2016Iso1 {ECO:0000313|EMBL:PLR53412.1,
RC ECO:0000313|Proteomes:UP000234626};
RA Rossi A., Fisher M.;
RT "Characterization of six clinical isolates of Enterochimera gen. nov., a
RT novel genus of the Yersiniaciae family and the three species Enterochimera
RT arupensis sp. nov., Enterochimera coloradensis sp. nov, and Enterochimera
RT californica sp. nov.";
RL Submitted (DEC-2017) 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:PLR53412.1}.
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DR EMBL; PJZK01000001; PLR53412.1; -; Genomic_DNA.
DR RefSeq; WP_072925630.1; NZ_PJZK01000001.1.
DR AlphaFoldDB; A0A2N5ETH5; -.
DR OrthoDB; 9810759at2; -.
DR Proteomes; UP000234626; 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|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW 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:UP000234626};
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};
KW Transport {ECO:0000256|ARBA:ARBA00022448, 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..76
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01075"
FT TRANSMEM 88..113
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01075"
FT TRANSMEM 119..141
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01075"
FT TRANSMEM 185..209
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01075"
FT TRANSMEM 221..252
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..358
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01075"
FT TRANSMEM 364..386
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01075"
FT DOMAIN 403..485
FT /note="RCK C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51202"
SQ SEQUENCE 574 AA; 62003 MW; D1FD91FD29D15A47 CRC64;
MEASTINTLF VIGAVLVGAS ILLSSLSSRL GIPILVIFLA IGMLAGVDGL GGIEFDNYPL
AYMISNLALA VILLDGGMRT RASYFRVALW PALSLATVGV VLTAALTGLA AAWLFHVNLY
QGLLIGAIVG STDAAAVFSM IGGKGLNDRV SATLEIESGC NDPMAVFLTI TLIDMIGKGE
HGLSWMFIVD IIRQFGLGIA LGFAGGWLLQ QSINRIPLAP GLYPLLALSG GLLVFALTTL
LEGSGILAVY LCGLKLGNSP IRNRHGILQT FDGMAWLSQI GMFMVLGLLL TPSQLLPIAL
PALLLSVWMI VFVRPVAVFA SLLPFRSFTG RERVFLSWVG LRGAVPIILA VFPMMAGIPD
ARLFFNVAFF IVLVSLLVQG TSLAWAAQQA RVIVPPTPTP ESRIGLDIDP QNIWQHFTYK
LGAEKWYIGA AIRDLQLPPQ TRITALFRGQ EMLYPTRNTR LQEGDILCVI GRESDIPQLG
KLFSETPRTK VDERFFGDFI LDADARLGAV AEQYGLTLSA DIDPGQPLHH FMLQRLGGEP
VIGDHIDWND LIWTIAEMEG GNVTRIGVKI NNDA
//
