ID   MNHD1_STAAU             Reviewed;         498 AA.
AC   P60686; Q0Q2K4; Q9ZNG3;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   13-APR-2004, sequence version 1.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=Na(+)/H(+) antiporter subunit D1;
DE   AltName: Full=Mnh complex subunit D1;
DE   AltName: Full=Mrp complex subunit D1;
GN   Name=mnhD1; Synonyms=mrpD1;
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 D
CC       family. {ECO:0000305}.
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DR   EMBL; AB015981; BAA35098.1; -; Genomic_DNA.
DR   EMBL; DQ659238; ABG67113.1; -; Genomic_DNA.
DR   PIR; F89861; F89861.
DR   RefSeq; WP_000573077.1; NZ_WYDB01000003.1.
DR   AlphaFoldDB; P60686; -.
DR   SMR; P60686; -.
DR   TCDB; 2.A.63.1.3; the monovalent cation (k(+) or na(+)):proton antiporter-3 (cpa3) family.
DR   OMA; YVAHHIT; -.
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:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR   GO; GO:0015386; F:potassium:proton antiporter activity; IEA:InterPro.
DR   GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR   GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
DR   InterPro; IPR004775; MnhD1.
DR   InterPro; IPR003918; NADH_UbQ_OxRdtase.
DR   InterPro; IPR001750; ND/Mrp_mem.
DR   Pfam; PF00361; Proton_antipo_M; 1.
DR   PRINTS; PR01437; NUOXDRDTASE4.
DR   TIGRFAMs; TIGR00944; 2a6301s04; 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..498
FT                   /note="Na(+)/H(+) antiporter subunit D1"
FT                   /id="PRO_0000217081"
FT   TRANSMEM        6..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        32..54
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        74..96
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        109..126
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        131..153
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        165..187
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        211..233
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        238..260
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        275..297
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        304..323
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        328..350
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        371..393
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        408..430
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        451..470
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   498 AA;  54756 MW;  6B8A0D38B7B3A9A6 CRC64;
     MIESNMLVLT LVIPVITAIL LVFIGKRPII KRYVALGGTL LTLVAAIINL ANVVKHGPIR
     VELGSWKAPY SIVFVLDIFS ALLIITSIII TAIVILYSYQ TIGIERERYY YYFSVLFMLI
     GIIGAFTTGD IFNLFVFFEV FLMSSYFLLV IGSTKIQLQE TIKYVLVNVV SSSFFVMGVA
     ILYSVVGTLN LADISNKLAN LSAHDSGLVN IVFILFIFVF ATKAGVFPMF VWLPSAYYAP
     PIPIIAFFGA LLTKVGVYAI ARTLSLFFSD NVSFSHYVIL FLALLTIIFG CVGAVAYANI
     KKIILYNVMI AVGVILVGVA MMTESGMIGA IYYTLHDMLV KLALFLLIGI MIKITGTADL
     RQFGGLIKRY PVLGWSFFIA ALSLAGIPPL SGFYGKFFIV QSTFERGFYL SGVIVLLSSL
     VVLYSVIRIF LQGFFGQPKG YDLNNKVDVK YLTTIAIVAV VITVLYGLSA DYLYPMVKAG
     AETFYNPSTY VKAVLGGK