MRPA_BACSU
ID MRPA_BACSU Reviewed; 801 AA.
AC Q9K2S2;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 2.
DT 03-AUG-2022, entry version 124.
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; Synonyms=ntrA, shaA, yufT; OrderedLocusNames=BSU31600;
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.
RC STRAIN=168;
RX PubMed=9878723; DOI=10.1016/s0005-2728(98)00157-1;
RA Kosono S., Morotomi S., Kitada M., Kudo T.;
RT "Analyses of a Bacillus subtilis homologue of the Na+/H+ antiporter gene
RT which is important for pH homeostasis of alkaliphilic Bacillus sp. C-125.";
RL Biochim. Biophys. Acta 1409:171-175(1999).
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.
RC STRAIN=168;
RX PubMed=10648512; DOI=10.1128/jb.182.4.898-904.2000;
RA Kosono S., Ohashi Y., Kawamura F., Kitada M., Kudo T.;
RT "Function of a principal Na(+)/H(+) antiporter, ShaA, is required for
RT initiation of sporulation in Bacillus subtilis.";
RL J. Bacteriol. 182:898-904(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, AND SUBCELLULAR LOCATION.
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:10648512,
CC ECO:0000269|PubMed:17293423, ECO:0000269|PubMed:9878723}.
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:0000269|PubMed:17693497};
CC Multi-pass membrane protein {ECO:0000269|PubMed:17693497}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB07942.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; Z93937; CAB07942.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL009126; CAB15149.2; -; Genomic_DNA.
DR PIR; A70010; A70010.
DR RefSeq; NP_391038.2; NC_000964.3.
DR RefSeq; WP_003228821.1; NZ_JNCM01000033.1.
DR AlphaFoldDB; Q9K2S2; -.
DR SMR; Q9K2S2; -.
DR IntAct; Q9K2S2; 1.
DR STRING; 224308.BSU31600; -.
DR TCDB; 2.A.63.1.4; the monovalent cation (k(+) or na(+)):proton antiporter-3 (cpa3) family.
DR PaxDb; Q9K2S2; -.
DR PRIDE; Q9K2S2; -.
DR EnsemblBacteria; CAB15149; CAB15149; BSU_31600.
DR GeneID; 938828; -.
DR KEGG; bsu:BSU31600; -.
DR PATRIC; fig|224308.179.peg.3425; -.
DR eggNOG; COG1009; Bacteria.
DR eggNOG; COG2111; Bacteria.
DR InParanoid; Q9K2S2; -.
DR OMA; AFILQYM; -.
DR PhylomeDB; Q9K2S2; -.
DR BioCyc; BSUB:BSU31600-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; IMP:CACAO.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; 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; Sporulation; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..801
FT /note="Na(+)/H(+) antiporter subunit A"
FT /id="PRO_0000217074"
FT TRANSMEM 4..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 28..50
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 166..188
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 203..222
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 229..251
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 266..288
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 301..323
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 338..360
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 372..394
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 428..450
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 471..493
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 526..548
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 594..616
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 626..647
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 654..671
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 676..698
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 710..732
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 772..789
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 801 AA; 89531 MW; C6DE22B56DAA725D CRC64;
MQLLHLAILS PFLFAFIIPF LAKYAKRVHT GWFVLILPVL LFIYFLPMIR MTQSGETLRS
VLEWIPSLGI NFTVYIDGLG LLFALLITGI GSLVTLYSIF YLSKEKEQLG PFYVYLLMFM
GAMLGVVLVD NVMVLYMFWE LTSLSSFLLI GYWYKREKSR YGAAKSLLIT VSGGLCMLGG
FILLYLITDS FSIREMVHQV QLIAGHELFI PAMILILLGA FTKSAQFPFY IWLPDAMEAP
TPVSAYLHSA TMVKAGIYVI ARFSPIFAFS AQWFWIVSLV GLFTMVWGSF HAVKQTDLKS
ILAFSTVSQL GMIISMLGVS AAALHYGHTE YYTVAAMAAI FHLINHATFK GSLFMAVGII
DHETGTRDIR KLGGLMAIMP ITFTISLIGT FSMAGLPPFN GFLSKEMFFT SMLRVTHFDL
FNVQTWGVLF PLFAWIGSVF TFIYSMKLLF KTFRGNYQPE QLEKQAHEAP VGMLVPPVIL
VALAVSLFFF PNILSYSLIE PAMNSIYPTL LDGHEKFHVH ISQWHGVTTE LLMTAGIVVI
GTIGYLSLNK WKGIYKLFPS KLTLNRLYDK LLTMMEKGSY RVTKQYMTGF LRDYLLYIFA
GFIILIGGAF AIKGGFSFKT EGMAKIGVYE IILTLVMISA TVATVFARSR LTAIIALGVV
GYTLALFFVI FRAPDLALTQ LVIETISVAL FLLCFYHLPK LRLKTKTRTF RMTNFIISLG
VGVIVTLLGI ASSSQRTKDS IASFFVKHSH DLGGGDNVVN VILVDFRGFD TMFEITVLTI
AALGIYSMIK TKVKEEGKSG E
