MRPB_BACSU
ID MRPB_BACSU Reviewed; 143 AA.
AC O05259;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Na(+)/H(+) antiporter subunit B;
DE AltName: Full=Mrp complex subunit B;
DE AltName: Full=Multiple resistance and pH homeostasis protein B;
GN Name=mrpB; Synonyms=yufU; OrderedLocusNames=BSU31610;
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 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 B
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; Z93937; CAB07943.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15150.1; -; Genomic_DNA.
DR PIR; B70010; B70010.
DR RefSeq; NP_391039.1; NC_000964.3.
DR RefSeq; WP_003228819.1; NZ_JNCM01000033.1.
DR AlphaFoldDB; O05259; -.
DR SMR; O05259; -.
DR STRING; 224308.BSU31610; -.
DR TCDB; 2.A.63.1.4; the monovalent cation (k(+) or na(+)):proton antiporter-3 (cpa3) family.
DR PaxDb; O05259; -.
DR EnsemblBacteria; CAB15150; CAB15150; BSU_31610.
DR GeneID; 937177; -.
DR KEGG; bsu:BSU31610; -.
DR PATRIC; fig|224308.179.peg.3426; -.
DR eggNOG; COG2111; Bacteria.
DR InParanoid; O05259; -.
DR OMA; HPGFLMP; -.
DR PhylomeDB; O05259; -.
DR BioCyc; BSUB:BSU31610-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:0015297; F:antiporter activity; IEA:UniProtKB-KW.
DR GO; GO:0008324; F:cation transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
DR InterPro; IPR005281; CPA3_sub_B.
DR InterPro; IPR007182; MnhB.
DR Pfam; PF04039; MnhB; 1.
DR TIGRFAMs; TIGR00943; 2a6301s02; 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..143
FT /note="Na(+)/H(+) antiporter subunit B"
FT /id="PRO_0000088864"
FT TRANSMEM 9..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 36..58
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 71..93
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 117..139
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 143 AA; 15294 MW; 7170B6B649784F85 CRC64;
MNEQKTNDLI LQTATKLVSF IILLFSFYLF LSGHNAPGGG FVGGLITSSS IVLLLLAYDL
KTVRSLLPVN FIYVAGAGLL LAVLTGVGSF VFGAPFLTHT FGYFQLPILG KTELATATIF
DLGVYLVVVG ITMTIIQTIG EEE
