MRPA_ALKPO
ID MRPA_ALKPO Reviewed; 805 AA.
AC Q9RGZ5; D3FXI2;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Na(+)/H(+) antiporter subunit A;
DE AltName: Full=Mrp complex subunit A;
DE AltName: Full=Multiple resistance and pH homeostasis protein A;
GN Name=mrpA; OrderedLocusNames=BpOF4_13210;
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 15 AND 331.
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 -!- 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:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
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 A
CC family. {ECO:0000305}.
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DR EMBL; AF097740; AAF21812.2; -; Genomic_DNA.
DR EMBL; CP001878; ADC50693.1; -; Genomic_DNA.
DR RefSeq; WP_012958056.1; NC_013791.2.
DR AlphaFoldDB; Q9RGZ5; -.
DR SMR; Q9RGZ5; -.
DR STRING; 398511.BpOF4_13210; -.
DR EnsemblBacteria; ADC50693; ADC50693; BpOF4_13210.
DR KEGG; bpf:BpOF4_13210; -.
DR eggNOG; COG1009; Bacteria.
DR eggNOG; COG2111; Bacteria.
DR HOGENOM; CLU_007100_2_1_9; -.
DR OMA; AFILQYM; -.
DR OrthoDB; 1274678at2; -.
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:0005451; F:monovalent cation:proton antiporter activity; IEA:InterPro.
DR GO; GO:0098662; P:inorganic cation transmembrane transport; IEA:InterPro.
DR GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
DR InterPro; IPR025383; MbhD-like_TM.
DR InterPro; IPR005663; MrpA/MnhA1/PhaAB.
DR InterPro; IPR001750; ND/Mrp_mem.
DR InterPro; IPR001516; Proton_antipo_N.
DR Pfam; PF13244; DUF4040; 1.
DR Pfam; PF00361; Proton_antipo_M; 1.
DR Pfam; PF00662; Proton_antipo_N; 1.
DR TIGRFAMs; TIGR00940; 2a6301s01; 1.
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..805
FT /note="Na(+)/H(+) antiporter subunit A"
FT /id="PRO_0000217073"
FT TRANSMEM 4..22
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 29..51
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 80..102
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 109..128
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 132..154
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 167..189
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 209..231
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 244..266
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 271..293
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 300..322
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 332..354
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 375..397
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 431..453
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 474..496
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 529..551
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 597..614
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 629..651
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 656..674
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 679..701
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 714..736
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 778..795
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 805 AA; 89397 MW; 1F93C781C52940F0 CRC64;
MTVLHWATIS PFLLAILIPF LYKYARRIHT GWFVLVLPLV LFIYFIQYLS ITSTGGVVEH
TIPWVPSLGI NFTVFVDGLS LLFALLITGI GTLVILYSIF YLSKKTESLN NFYVYLLMFM
GAMLGVVLSD NLIVLYVFWE LTSLASSLLI SYWFHREKST YGAQKSMLIT VFGGFAMLGG
FSLLYVMTGT FSIRGIIENV DLVTSSELFL PAMILVLLGA FTKSAQFPFH IWLPDAMEAP
TPVSAYLHSA TMVKAGIYLV ARLTPVFAGS AEWFWLLTGF GVVTLLWGST SAVRQKDLKG
ILAFSTVSQL GLIMTLLGLG SAAIYFGESV DPAFYSFAIM AAIFHLINHA TFKGSLFMTA
GIIDHETGTR DIRKLGGLMA IMPVTFTVSL IGLASMAGLP PFNGFLSKEM FFTALLRATE
MNAFNMETFG IIIVVLAWIA SVFTFLYCLI MFFKTFTGKF KPENYDVKVH EAPIGMLISP
VILGSLVIVF GFFPNILAYT IIEPAMQAVL PTVLADGELF HVNIYMWHGF NAELFMTMGV
VAAGIILFLM MKNWAKAAFY MKERDPLNWF YDSSLSGVIT GSQFVTRIQM TGLLRDYFAY
MIVFMILLLG YTMFRYDAFA IDTTNVTEIA PYIWVITIVF IVATLSIPFI NKRITAVVVV
GVIGFLLALL FVVFRAPDLA LTQLLIETVT VLLLMLAFYH LPELRKEEFK PRFNVLNLII
SIGVGFFITA IALSSLALGN EAGIEPISQF FIENSKELAG GYNMVNVILV DFRGLDTMLE
VLVLGIAALG VIALIKLRMT GREDV
