ID MRPE_BACSU Reviewed; 158 AA.
AC Q7WY60;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 2.
DT 27-MAR-2024, entry version 109.
DE RecName: Full=Na(+)/H(+) antiporter subunit E;
DE AltName: Full=Mrp complex subunit E;
DE AltName: Full=Multiple resistance and pH homeostasis protein E;
GN Name=mrpE; OrderedLocusNames=BSU31640;
OS Bacillus subtilis (strain 168).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [2]
RP SEQUENCE REVISION TO 3; 14; 40; 50 AND 92.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [3]
RP FUNCTION.
RX PubMed=10198001; DOI=10.1128/jb.181.8.2394-2402.1999;
RA Ito M., Guffanti A.A., Oudega B., Krulwich T.A.;
RT "mrp, a multigene, multifunctional locus in Bacillus subtilis with roles in
RT resistance to cholate and to Na+ and in pH homeostasis.";
RL J. Bacteriol. 181:2394-2402(1999).
RN [4]
RP COUPLING ENERGIZATION MODE.
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 [5]
RP FUNCTION IN ANTIPORT OF LITHIUM.
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).
RN [6]
RP SUBUNIT.
RC STRAIN=168 / Marburg / UOT1285;
RX PubMed=17693497; DOI=10.1128/jb.00968-07;
RA Kajiyama Y., Otagiri M., Sekiguchi J., Kosono S., Kudo T.;
RT "Complex formation by the mrpABCDEFG gene products, which constitute a
RT principal Na+/H+ antiporter in Bacillus subtilis.";
RL J. Bacteriol. 189:7511-7514(2007).
CC -!- FUNCTION: Mrp complex is a Na(+)/H(+) antiporter that is considered to
CC be the major Na(+) excretion system in B.subtilis. Has a major role in
CC Na(+) resistance and a minor role in Na(+)- and K(+)-dependent pH
CC homeostasis as compared to TetB. MrpA may be the actual Na(+)/H(+)
CC antiporter, although the six other Mrp proteins are all required for
CC Na(+)/H(+) antiport activity and Na(+) resistance. MrpA is required for
CC initiation of sporulation when external Na(+) concentration increases.
CC Also transports Li(+) but not K(+), Ca(2+) or Mg(2+).
CC {ECO:0000269|PubMed:10198001, ECO:0000269|PubMed:17293423}.
CC -!- SUBUNIT: Forms a heterooligomeric complex that consists of seven
CC subunits: MrpA, MrpB, MrpC, MrpD, MrpE, MrpF and MrpG.
CC {ECO:0000269|PubMed:17693497}.
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 E
CC family. {ECO:0000305}.
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DR EMBL; AL009126; CAE01465.2; -; Genomic_DNA.
DR RefSeq; WP_003244015.1; NZ_JNCM01000033.1.
DR RefSeq; YP_054591.2; NC_000964.3.
DR AlphaFoldDB; Q7WY60; -.
DR SMR; Q7WY60; -.
DR STRING; 224308.BSU31640; -.
DR TCDB; 2.A.63.1.4; the monovalent cation (k(+) or na(+)):proton antiporter-3 (cpa3) family.
DR PaxDb; 224308-BSU31640; -.
DR EnsemblBacteria; CAE01465; CAE01465; BSU_31640.
DR GeneID; 2914191; -.
DR KEGG; bsu:BSU31640; -.
DR PATRIC; fig|224308.179.peg.3429; -.
DR eggNOG; COG1863; Bacteria.
DR InParanoid; Q7WY60; -.
DR OrthoDB; 9800498at2; -.
DR PhylomeDB; Q7WY60; -.
DR BioCyc; BSUB:BSU31640-MONOMER; -.
DR Proteomes; UP000001570; Chromosome.
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:monoatomic cation transmembrane transporter activity; IEA:InterPro.
DR GO; GO:1902600; P:proton transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
DR InterPro; IPR002758; Cation_antiport_E.
DR PANTHER; PTHR34584; NA(+)/H(+) ANTIPORTER SUBUNIT E1; 1.
DR PANTHER; PTHR34584:SF1; NA(+)_H(+) ANTIPORTER SUBUNIT E1; 1.
DR Pfam; PF01899; MNHE; 1.
DR PIRSF; PIRSF019239; MrpE; 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..158
FT /note="Na(+)/H(+) antiporter subunit E"
FT /id="PRO_0000217094"
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 51..71
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 158 AA; 18380 MW; 9CDA81C3156BDE7F CRC64;
MAFQILLNVF LAFCWMFLSN SPSAAGFITG YILGMLSLFF FRRFFTRQFY LWKLISIIKL
CFIFIKELYL ANVSVMKSVL SPKLNIRPGI FAFKTELTKD WEITMLSLLI TLTPGTLVMD
ISDDRTILYI HAMDIEDAEK AIFDIRESFE KAIQEVSR
//
