MRPD_ALKPO
ID MRPD_ALKPO Reviewed; 493 AA.
AC Q9RGZ2; D3FXH9;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Na(+)/H(+) antiporter subunit D;
DE AltName: Full=Mrp complex subunit D;
DE AltName: Full=Multiple resistance and pH homeostasis protein D;
GN Name=mrpD; OrderedLocusNames=BpOF4_13195;
OS Alkalihalophilus pseudofirmus (strain ATCC BAA-2126 / JCM 17055 / OF4)
OS (Bacillus pseudofirmus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalophilus.
OX NCBI_TaxID=398511;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RX PubMed=11356194; DOI=10.1016/s0014-5793(01)02417-6;
RA Ito M., Guffanti A.A., Krulwich T.A.;
RT "Mrp-dependent Na(+)/H(+) antiporters of Bacillus exhibit characteristics
RT that are unanticipated for completely secondary active transporters.";
RL FEBS Lett. 496:117-120(2001).
RN [2]
RP SEQUENCE REVISION TO 400.
RA Krulwich T.A.;
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-2126 / JCM 17055 / OF4;
RX PubMed=21951522; DOI=10.1111/j.1462-2920.2011.02591.x;
RA Janto B., Ahmed A., Ito M., Liu J., Hicks D.B., Pagni S., Fackelmayer O.J.,
RA Smith T.A., Earl J., Elbourne L.D., Hassan K., Paulsen I.T., Kolsto A.B.,
RA Tourasse N.J., Ehrlich G.D., Boissy R., Ivey D.M., Li G., Xue Y., Ma Y.,
RA Hu F.Z., Krulwich T.A.;
RT "Genome of alkaliphilic Bacillus pseudofirmus OF4 reveals adaptations that
RT support the ability to grow in an external pH range from 7.5 to 11.4.";
RL Environ. Microbiol. 13:3289-3309(2011).
RN [4]
RP CHARACTERIZATION, AND PROBABLE FUNCTION IN ELECTROGENIC ANTIPORTER
RP ACTIVITY.
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 and Na(+) resistance. Na(+)/H(+) antiport
CC consumes a transmembrane electrical potential, and is thus inferred to
CC be electrogenic. Does not transport K(+), Ca(2+) or Mg(2+).
CC -!- FUNCTION: Mrp complex is a Na(+)/H(+) antiporter involved in Na(+)
CC excretion and Na(+) resistance.
CC -!- SUBUNIT: Forms a heterooligomeric complex that consists of seven
CC subunits: MrpA, MrpB, MrpC, MrpD, MrpE, MrpF and MrpG. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- MISCELLANEOUS: Mrp-dependent antiport apparently occurs by a secondary,
CC proton motive force-dependent mechanism, but the similarity of several
CC Mrp proteins to membrane-embedded subunits of energy-coupled NADH
CC dehydrogenase complexes raises the possibility that there is a capacity
CC for electron transport that could provide a primary energy coupling
CC option for Mrp functions.
CC -!- SIMILARITY: Belongs to the CPA3 antiporters (TC 2.A.63) subunit D
CC family. {ECO:0000305}.
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DR EMBL; AF097740; AAF21815.2; -; Genomic_DNA.
DR EMBL; CP001878; ADC50690.1; -; Genomic_DNA.
DR RefSeq; WP_012958053.1; NC_013791.2.
DR AlphaFoldDB; Q9RGZ2; -.
DR SMR; Q9RGZ2; -.
DR STRING; 398511.BpOF4_13195; -.
DR EnsemblBacteria; ADC50690; ADC50690; BpOF4_13195.
DR KEGG; bpf:BpOF4_13195; -.
DR eggNOG; COG0651; Bacteria.
DR HOGENOM; CLU_007100_9_2_9; -.
DR OMA; YVAHHIT; -.
DR OrthoDB; 1887859at2; -.
DR Proteomes; UP000001544; Chromosome.
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:0006814; P:sodium 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 1: Evidence at protein level;
KW Antiport; Cell membrane; Hydrogen ion transport; Ion transport; Membrane;
KW Reference proteome; Sodium; Sodium transport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..493
FT /note="Na(+)/H(+) antiporter subunit D"
FT /id="PRO_0000217083"
FT TRANSMEM 4..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 30..52
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 72..94
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 107..126
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 130..149
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 162..184
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 204..226
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 233..255
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 270..292
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 299..321
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 325..347
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 368..390
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 405..427
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 448..470
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 493 AA; 54444 MW; C0093DCD9E142E27 CRC64;
MNNLVILPIL IPFIVGSFLI LFAKHHSLQR VISGFAVVGM LLVSIYLAVD VYQNGITVLE
LGNWQAPFGI VLVADLFATM MVILASIVGV VCLFFAFQTI SSEREKYYFY PFYFFLLAGV
NGAFLTGDLF NLFVFFEVML IASYILIVLG GTKYQLRESL KYVVINVFAS ILFIVGVAYI
YSITGTLNMA DLAVKVGELE QTGVLNVIAV IFLVVFAMKG GLFPLYFWLP RSYFGPPAAI
AALFGGLLTK VGIYAIMRTF TLIFNHDPGF THTLILILAG LTMFFGVLGA VSQFDFKRIL
SYHIISQVGY MVMGLGIYTQ LAIAGAIYYI AHHIIVKAAL FLFAGATQRI TGTTDLKKMG
GLLKTHPWLA WMFFISAISL AGIPPLSGFF SKFALILAAF LNENYIIAAV ALAVGLLTLF
SMMKIFIYAF WGEQKHTEEQ ANFKVGKLLL PIVPLVALTI ILGFAAEPIF QYSLQVADQI
LDPTIYIESV LKE
