ID   MNHE1_STAAU             Reviewed;         159 AA.
AC   P60690; Q0Q2K3; Q9ZNG2;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   13-APR-2004, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Na(+)/H(+) antiporter subunit E1;
DE   AltName: Full=Mnh complex subunit E1;
DE   AltName: Full=Mrp complex subunit E1;
GN   Name=mnhE1; Synonyms=mrpE1;
OS   Staphylococcus aureus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION OF ANTIPORTER
RP   ACTIVITY.
RC   STRAIN=ATCC 21027 / 209-P;
RX   PubMed=9852009; DOI=10.1128/jb.180.24.6642-6648.1998;
RA   Hiramatsu T., Kodama K., Kuroda T., Mizushima T., Tsuchiya T.;
RT   "A putative multisubunit Na+/H+ antiporter from Staphylococcus aureus.";
RL   J. Bacteriol. 180:6642-6648(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION, AND PROBABLE
RP   ELECTROGENIC ANTIPORTER ACTIVITY.
RC   STRAIN=RF4220;
RX   PubMed=17293423; DOI=10.1128/jb.00021-07;
RA   Swartz T.H., Ito M., Ohira T., Natsui S., Hicks D.B., Krulwich T.A.;
RT   "Catalytic properties of Staphylococcus aureus and Bacillus members of the
RT   secondary cation/proton antiporter-3 (Mrp) family are revealed by an
RT   optimized assay in an Escherichia coli host.";
RL   J. Bacteriol. 189:3081-3090(2007).
CC   -!- FUNCTION: Mnh complex is a Na(+)Li(+)/H(+) antiporter involved in Na(+)
CC       and/or Li(+) excretion. Na(+)/H(+) antiport consumes a transmembrane
CC       electrical potential, and is thus inferred to be electrogenic. Does not
CC       transport K(+), Ca(2+) or Mg(2+).
CC   -!- ACTIVITY REGULATION: Na(+) extrusion is completely inhibited by the
CC       H(+) conductor carbonyl cyanide m-chlorophenylhydrazone (CCCP).
CC   -!- SUBUNIT: May form a heterooligomeric complex that consists of seven
CC       subunits: mnhA1, mnhB1, mnhC1, mnhD1, mnhE1, mnhF1 and mnhG1.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the CPA3 antiporters (TC 2.A.63) subunit E
CC       family. {ECO:0000305}.
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DR   EMBL; AB015981; BAA35099.1; -; Genomic_DNA.
DR   EMBL; DQ659238; ABG67114.1; -; Genomic_DNA.
DR   PIR; E89861; E89861.
DR   RefSeq; WP_000290674.1; NZ_WYDB01000003.1.
DR   AlphaFoldDB; P60690; -.
DR   SMR; P60690; -.
DR   TCDB; 2.A.63.1.3; the monovalent cation (k(+) or na(+)):proton antiporter-3 (cpa3) family.
DR   OMA; HAMDIED; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015297; F:antiporter activity; IEA:UniProtKB-KW.
DR   GO; GO:0008324; F:cation transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:1902600; P:proton transmembrane transport; IEA:InterPro.
DR   GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
DR   InterPro; IPR004847; Antiport_suE1.
DR   InterPro; IPR002758; Cation_antiport_E.
DR   PANTHER; PTHR34584; PTHR34584; 1.
DR   Pfam; PF01899; MNHE; 1.
DR   PIRSF; PIRSF019239; MrpE; 1.
DR   TIGRFAMs; TIGR00942; 2a6301s05; 1.
PE   1: Evidence at protein level;
KW   Antiport; Cell membrane; Hydrogen ion transport; Ion transport; Membrane;
KW   Sodium; Sodium transport; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..159
FT                   /note="Na(+)/H(+) antiporter subunit E1"
FT                   /id="PRO_0000217091"
FT   TRANSMEM        5..22
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        27..45
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        52..69
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        100..122
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   159 AA;  18319 MW;  95C11B67E678D3B7 CRC64;
     MAVQLVLNFI IAVFWLFVTN SYTTNNFVLG FIFGLVLVYL LHRVLPGRFY VITLYRIIKL
     VIIFLIELIK ANFDVLKIII KPSIKNEPGF FVYHTDLKKD WQIVLLSNLI TLTPGTVVLG
     VSDDRTKIYI HAIDFSTKEQ EVESIKTSLE KIVREVGEI