NHAP2_SHESM
ID NHAP2_SHESM Reviewed; 574 AA.
AC Q0HFK8;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 25-MAY-2022, entry version 91.
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=Shewmr4_3088;
OS Shewanella sp. (strain MR-4).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=60480;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR-4;
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 Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Nealson K.,
RA Konstantinidis K., Klappenbach J., Tiedje J., Richardson P.;
RT "Complete sequence of Shewanella sp. MR-4.";
RL Submitted (AUG-2006) 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}.
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DR EMBL; CP000446; ABI40159.1; -; Genomic_DNA.
DR RefSeq; WP_011623832.1; NC_008321.1.
DR AlphaFoldDB; Q0HFK8; -.
DR SMR; Q0HFK8; -.
DR KEGG; she:Shewmr4_3088; -.
DR HOGENOM; CLU_005912_9_2_6; -.
DR OMA; QIGMFVL; -.
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; 3.30.70.1450; -; 1.
DR HAMAP; MF_01075; NhaP2; 1.
DR InterPro; IPR006153; Cation/H_exchanger.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; 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..574
FT /note="K(+)/H(+) antiporter NhaP2"
FT /id="PRO_0000278159"
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 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 173..193
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01075"
FT TRANSMEM 196..216
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01075"
FT TRANSMEM 219..239
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01075"
FT TRANSMEM 242..262
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01075"
FT TRANSMEM 271..291
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01075"
FT TRANSMEM 299..319
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01075"
FT TRANSMEM 335..355
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01075"
FT TRANSMEM 359..379
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01075"
FT DOMAIN 405..486
FT /note="RCK C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01075"
SQ SEQUENCE 574 AA; 61528 MW; B40CAF1AAE59E8BD CRC64;
MDADSINSFF LIGALLAAVS VLLSPVSSRL GIPILLIFLA VGILAGEDGP GGILFDDYST
AYLVSNLALA IILLDGGMRT RVASFRVALW PALSLATFGV AITTSITGVM AAWLFDLHWL
QGLLVGAIVG STDAAAVFSL LKGRSLNERV GATLEIESGS NDPMAVFLTV TLIAILGNVD
AELSASFMLI SFIKQFGLGI FLGLGGGWLL WKLVNLSKLA EGLYSILVLS GGLMIYAASN
KLGGSGILSI YLVGLFLGNK PTRGRHSILN VLDGMTWVSQ IGMFLVLGLL LTPSDLLDIW
LPGLALAFGM ILFARPLAVW LSLLPFKSFS SRDRWFISWV GLRGAVPIIL AVFPMMAGLP
GAQLYFNLAF FVVLVSLLVQ GASLTTAARL AKVELPPKPL PISRSGVEIY PSSEWEVFVY
RLSENKWCIG EPLKRLSMPD GTRIAAVFRH NTLLHPSGST CLEAGDILCV LGQEKSLEAL
SNLFSQAPET KEVPRFFGDF FIDTEVKLLD LAPIYGLELD EATGDMTVAD LVAAELGSHP
VLGDQFLWQS LHWVVAGLYE GKVTNVGIRL PAEA
