MRPF_BACSU
ID MRPF_BACSU Reviewed; 94 AA.
AC O05228;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Na(+)/H(+) antiporter subunit F;
DE AltName: Full=Mrp complex subunit F;
DE AltName: Full=Multiple resistance and pH homeostasis protein F;
DE AltName: Full=Sodium-cholate efflux protein MrpF;
GN Name=mrpF; Synonyms=yufC; OrderedLocusNames=BSU31650;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9274030; DOI=10.1099/00221287-143-8-2769;
RA Oudega B., Koningstein G., Rodrigues L., de Sales Ramon M., Hilbert H.,
RA Duesterhoeft A., Pohl T.M., Weitzenegger T.;
RT "Analysis of the Bacillus subtilis genome: cloning and nucleotide sequence
RT of a 62 kb region between 275 degrees (rrnB) and 284 degrees (pai).";
RL Microbiology 143:2769-2774(1997).
RN [2]
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 [3]
RP SEQUENCE REVISION TO 14.
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 [4]
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 [5]
RP FUNCTION.
RX PubMed=11004162; DOI=10.1128/jb.182.20.5663-5670.2000;
RA Ito M., Guffanti A.A., Wang W., Krulwich T.A.;
RT "Effects of nonpolar mutations in each of the seven Bacillus subtilis mrp
RT genes suggest complex interactions among the gene products in support of
RT Na(+) and alkali but not cholate resistance.";
RL J. Bacteriol. 182:5663-5670(2000).
RN [6]
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 [7]
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 [8]
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 -!- FUNCTION: Involved in cholate and Na(+) efflux activities, which may be
CC mechanistically coupled. Does not require other Mrp proteins for its
CC own function.
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 F
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z93932; CAB07907.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15153.2; -; Genomic_DNA.
DR PIR; F70008; F70008.
DR RefSeq; NP_391043.2; NC_000964.3.
DR RefSeq; WP_003228814.1; NZ_JNCM01000033.1.
DR AlphaFoldDB; O05228; -.
DR SMR; O05228; -.
DR STRING; 224308.BSU31650; -.
DR TCDB; 2.A.63.1.4; the monovalent cation (k(+) or na(+)):proton antiporter-3 (cpa3) family.
DR PaxDb; O05228; -.
DR EnsemblBacteria; CAB15153; CAB15153; BSU_31650.
DR GeneID; 938862; -.
DR KEGG; bsu:BSU31650; -.
DR PATRIC; fig|224308.179.peg.3430; -.
DR eggNOG; COG2212; Bacteria.
DR InParanoid; O05228; -.
DR OMA; VIAFARY; -.
DR PhylomeDB; O05228; -.
DR BioCyc; BSUB:BSU31650-MON; -.
DR Proteomes; UP000001570; 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:0015385; F:sodium:proton antiporter activity; IBA:GO_Central.
DR GO; GO:0036376; P:sodium ion export across plasma membrane; IMP:CACAO.
DR InterPro; IPR007208; MrpF/PhaF-like.
DR PANTHER; PTHR34702; PTHR34702; 1.
DR Pfam; PF04066; MrpF_PhaF; 1.
DR PIRSF; PIRSF028784; MrpF; 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..94
FT /note="Na(+)/H(+) antiporter subunit F"
FT /id="PRO_0000087742"
FT TRANSMEM 2..22
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 34..54
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 14
FT /note="A -> G (in Ref. 1; CAB07907)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 94 AA; 10244 MW; 0798D6ED6FB51DAB CRC64;
MFTLILQIAL GIMAVSTFLY VIRVIKGPTV PDRVVALDAI GINLIAITAL VSILLKTSAF
LDIILLLGIL SFIGTIAFSK FLEKGEIIEN DRNR
