ID   MNHD2_STAAU             Reviewed;         499 AA.
AC   Q0Q2J7;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   25-MAY-2022, entry version 40.
DE   RecName: Full=Putative antiporter subunit mnhD2;
DE   AltName: Full=Mrp complex subunit D2;
DE   AltName: Full=Putative NADH-ubiquinone oxidoreductase subunit mnhD2;
GN   Name=mnhD2; Synonyms=mrpD2;
OS   Staphylococcus aureus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND EXPRESSION IN E.COLI.
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: Expression of the mnh2 operon in E.coli is not able to
CC       catalyze Na(+)Li(+)/H(+) antiport. It does however confer higher growth
CC       rates than the control strain at up to pH 9.5. The operon may encode an
CC       NADH-ubiquinone oxidoreductase.
CC   -!- SUBUNIT: May form a heterooligomeric complex that consists of seven
CC       subunits: mnhA2, mnhB2, mnhC2, mnhD2, mnhE2, mnhF2 and mnhG2.
CC       {ECO:0000250}.
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; DQ659239; ABG67120.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q0Q2J7; -.
DR   SMR; Q0Q2J7; -.
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:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR   GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR   GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR   InterPro; IPR003918; NADH_UbQ_OxRdtase.
DR   InterPro; IPR001750; ND/Mrp_mem.
DR   Pfam; PF00361; Proton_antipo_M; 1.
DR   PRINTS; PR01437; NUOXDRDTASE4.
PE   3: Inferred from homology;
KW   Antiport; Cell membrane; Ion transport; Membrane; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..499
FT                   /note="Putative antiporter subunit mnhD2"
FT                   /id="PRO_0000372228"
FT   TRANSMEM        3..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        33..53
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        79..99
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        109..129
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        131..151
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        162..182
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        210..230
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        241..261
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        272..292
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        309..329
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        331..351
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        370..390
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        404..424
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        452..472
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   499 AA;  55284 MW;  9CD332F39932DEEB CRC64;
     MMLSNLLILP MLLPFLCALI LVFLKNNDRI SKYLYLGTMT ITTIISLMLL IYVQRHRPIT
     LDFGGWSAPF GIQFLGDSLS LIMVTTASFV ITLIMAYGFG RGEHKANRYH LPSFILFLSV
     GVIGSFLTSD LFNLYVMFEI MLLASFVLIT LGQSVEQLRA AIIYVVLNII GSWLFLLGIG
     LLYKTVGTLN FSHIAMRLND MGDNRTVTMI SLIFLVAFSA KAALVLFMWL PKAYAVLNTE
     LAALFAALMT KVGAYALIRF FTLLFDQHND LIHPLLATMA AITMVIGAIG VIAYKDIKKI
     AAYQVIISIG FIILGLGTNT FAGINGAIFY LVNDIVVKTL LFFIIGSLVY ITGYRQYQYL
     NGLAKKEPLF GVAFIIMIFA IGGVPPFSGF PGKVLIFQGA LQNGNYIGLA LMIITSLIAM
     YSLFRILFYM YFGDKDGEEV NFKKIPLYRK RILSILVVVV IAIGIAAPVV LNVTSDATEL
     NTSDQLYQKL VNPHLKGED