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Protein

Na(+)/H(+) antiporter subunit A

Gene

mrpA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Mrp complex is a Na+/H+ antiporter that is considered to be the major Na+ excretion system in B.subtilis. Has a major role in Na+ resistance and a minor role in Na+- and K+-dependent pH homeostasis as compared to TetB. MrpA may be the actual Na+/H+ antiporter, although the six other Mrp proteins are all required for Na+/H+ antiport activity and Na+ resistance. MrpA is required for initiation of sporulation when external Na+ concentration increases. Also transports Li+ but not K+, Ca2+ or Mg2+.4 Publications

GO - Molecular functioni

  • NADH dehydrogenase (ubiquinone) activity Source: InterPro
  • sodium:proton antiporter activity Source: CACAO

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Antiport, Hydrogen ion transport, Ion transport, Sodium transport, Sporulation, Transport

Keywords - Ligandi

Sodium

Enzyme and pathway databases

BioCyciBSUB:BSU31600-MONOMER.

Protein family/group databases

TCDBi2.A.63.1.4. the monovalent cation (k(+) or na(+)):proton antiporter-3 (cpa3) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Na(+)/H(+) antiporter subunit A
Alternative name(s):
Mrp complex subunit A
Multiple resistance and pH homeostasis protein A
Gene namesi
Name:mrpA
Synonyms:ntrA, shaA, yufT
Ordered Locus Names:BSU31600
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei4 – 2118HelicalSequence analysisAdd
BLAST
Transmembranei28 – 5023HelicalSequence analysisAdd
BLAST
Transmembranei80 – 10223HelicalSequence analysisAdd
BLAST
Transmembranei109 – 12820HelicalSequence analysisAdd
BLAST
Transmembranei132 – 15423HelicalSequence analysisAdd
BLAST
Transmembranei166 – 18823HelicalSequence analysisAdd
BLAST
Transmembranei203 – 22220HelicalSequence analysisAdd
BLAST
Transmembranei229 – 25123HelicalSequence analysisAdd
BLAST
Transmembranei266 – 28823HelicalSequence analysisAdd
BLAST
Transmembranei301 – 32323HelicalSequence analysisAdd
BLAST
Transmembranei338 – 36023HelicalSequence analysisAdd
BLAST
Transmembranei372 – 39423HelicalSequence analysisAdd
BLAST
Transmembranei428 – 45023HelicalSequence analysisAdd
BLAST
Transmembranei471 – 49323HelicalSequence analysisAdd
BLAST
Transmembranei526 – 54823HelicalSequence analysisAdd
BLAST
Transmembranei594 – 61623HelicalSequence analysisAdd
BLAST
Transmembranei626 – 64722HelicalSequence analysisAdd
BLAST
Transmembranei654 – 67118HelicalSequence analysisAdd
BLAST
Transmembranei676 – 69823HelicalSequence analysisAdd
BLAST
Transmembranei710 – 73223HelicalSequence analysisAdd
BLAST
Transmembranei772 – 78918HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 801801Na(+)/H(+) antiporter subunit APRO_0000217074Add
BLAST

Proteomic databases

PaxDbiQ9K2S2.

Interactioni

Subunit structurei

Forms a heterooligomeric complex that consists of seven subunits: MrpA, MrpB, MrpC, MrpD, MrpE, MrpF and MrpG.1 Publication

Protein-protein interaction databases

IntActiQ9K2S2. 1 interaction.
STRINGi224308.Bsubs1_010100017171.

Structurei

3D structure databases

ProteinModelPortaliQ9K2S2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105D65. Bacteria.
COG1009. LUCA.
COG2111. LUCA.
HOGENOMiHOG000066204.
InParanoidiQ9K2S2.
KOiK05565.
OMAiAFILQYM.
OrthoDBiEOG6Z3KF1.
PhylomeDBiQ9K2S2.

Family and domain databases

InterProiIPR025383. DUF4040.
IPR005663. MrpA/MnhA1/PhaAB.
IPR018393. NADHpl_OxRdtase_5_subgr.
IPR001750. ND/Mrp_mem.
IPR001516. Proton_antipo_N.
[Graphical view]
PfamiPF13244. DUF4040. 1 hit.
PF00361. Proton_antipo_M. 1 hit.
PF00662. Proton_antipo_N. 1 hit.
[Graphical view]
PRINTSiPR01435. NPOXDRDTASE5.
TIGRFAMsiTIGR00940. 2a6301s01. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9K2S2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQLLHLAILS PFLFAFIIPF LAKYAKRVHT GWFVLILPVL LFIYFLPMIR
60 70 80 90 100
MTQSGETLRS VLEWIPSLGI NFTVYIDGLG LLFALLITGI GSLVTLYSIF
110 120 130 140 150
YLSKEKEQLG PFYVYLLMFM GAMLGVVLVD NVMVLYMFWE LTSLSSFLLI
160 170 180 190 200
GYWYKREKSR YGAAKSLLIT VSGGLCMLGG FILLYLITDS FSIREMVHQV
210 220 230 240 250
QLIAGHELFI PAMILILLGA FTKSAQFPFY IWLPDAMEAP TPVSAYLHSA
260 270 280 290 300
TMVKAGIYVI ARFSPIFAFS AQWFWIVSLV GLFTMVWGSF HAVKQTDLKS
310 320 330 340 350
ILAFSTVSQL GMIISMLGVS AAALHYGHTE YYTVAAMAAI FHLINHATFK
360 370 380 390 400
GSLFMAVGII DHETGTRDIR KLGGLMAIMP ITFTISLIGT FSMAGLPPFN
410 420 430 440 450
GFLSKEMFFT SMLRVTHFDL FNVQTWGVLF PLFAWIGSVF TFIYSMKLLF
460 470 480 490 500
KTFRGNYQPE QLEKQAHEAP VGMLVPPVIL VALAVSLFFF PNILSYSLIE
510 520 530 540 550
PAMNSIYPTL LDGHEKFHVH ISQWHGVTTE LLMTAGIVVI GTIGYLSLNK
560 570 580 590 600
WKGIYKLFPS KLTLNRLYDK LLTMMEKGSY RVTKQYMTGF LRDYLLYIFA
610 620 630 640 650
GFIILIGGAF AIKGGFSFKT EGMAKIGVYE IILTLVMISA TVATVFARSR
660 670 680 690 700
LTAIIALGVV GYTLALFFVI FRAPDLALTQ LVIETISVAL FLLCFYHLPK
710 720 730 740 750
LRLKTKTRTF RMTNFIISLG VGVIVTLLGI ASSSQRTKDS IASFFVKHSH
760 770 780 790 800
DLGGGDNVVN VILVDFRGFD TMFEITVLTI AALGIYSMIK TKVKEEGKSG

E
Length:801
Mass (Da):89,531
Last modified:April 13, 2004 - v2
Checksum:iC6DE22B56DAA725D
GO

Sequence cautioni

The sequence CAB07942.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z93937 Genomic DNA. Translation: CAB07942.1. Different initiation.
AL009126 Genomic DNA. Translation: CAB15149.2.
PIRiA70010.
RefSeqiNP_391038.2. NC_000964.3.
WP_003228821.1. NZ_JNCM01000033.1.

Genome annotation databases

EnsemblBacteriaiCAB15149; CAB15149; BSU31600.
GeneIDi938828.
KEGGibsu:BSU31600.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z93937 Genomic DNA. Translation: CAB07942.1. Different initiation.
AL009126 Genomic DNA. Translation: CAB15149.2.
PIRiA70010.
RefSeqiNP_391038.2. NC_000964.3.
WP_003228821.1. NZ_JNCM01000033.1.

3D structure databases

ProteinModelPortaliQ9K2S2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9K2S2. 1 interaction.
STRINGi224308.Bsubs1_010100017171.

Protein family/group databases

TCDBi2.A.63.1.4. the monovalent cation (k(+) or na(+)):proton antiporter-3 (cpa3) family.

Proteomic databases

PaxDbiQ9K2S2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB15149; CAB15149; BSU31600.
GeneIDi938828.
KEGGibsu:BSU31600.

Phylogenomic databases

eggNOGiENOG4105D65. Bacteria.
COG1009. LUCA.
COG2111. LUCA.
HOGENOMiHOG000066204.
InParanoidiQ9K2S2.
KOiK05565.
OMAiAFILQYM.
OrthoDBiEOG6Z3KF1.
PhylomeDBiQ9K2S2.

Enzyme and pathway databases

BioCyciBSUB:BSU31600-MONOMER.

Family and domain databases

InterProiIPR025383. DUF4040.
IPR005663. MrpA/MnhA1/PhaAB.
IPR018393. NADHpl_OxRdtase_5_subgr.
IPR001750. ND/Mrp_mem.
IPR001516. Proton_antipo_N.
[Graphical view]
PfamiPF13244. DUF4040. 1 hit.
PF00361. Proton_antipo_M. 1 hit.
PF00662. Proton_antipo_N. 1 hit.
[Graphical view]
PRINTSiPR01435. NPOXDRDTASE5.
TIGRFAMsiTIGR00940. 2a6301s01. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Analysis of the Bacillus subtilis genome: cloning and nucleotide sequence of a 62 kb region between 275 degrees (rrnB) and 284 degrees (pai)."
    Oudega B., Koningstein G., Rodrigues L., de Sales Ramon M., Hilbert H., Duesterhoeft A., Pohl T.M., Weitzenegger T.
    Microbiology 143:2769-2774(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 168.
  2. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
    Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
    , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
    Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.
  3. "Analyses of a Bacillus subtilis homologue of the Na+/H+ antiporter gene which is important for pH homeostasis of alkaliphilic Bacillus sp. C-125."
    Kosono S., Morotomi S., Kitada M., Kudo T.
    Biochim. Biophys. Acta 1409:171-175(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
    Strain: 168.
  4. "mrp, a multigene, multifunctional locus in Bacillus subtilis with roles in resistance to cholate and to Na+ and in pH homeostasis."
    Ito M., Guffanti A.A., Oudega B., Krulwich T.A.
    J. Bacteriol. 181:2394-2402(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. "Function of a principal Na(+)/H(+) antiporter, ShaA, is required for initiation of sporulation in Bacillus subtilis."
    Kosono S., Ohashi Y., Kawamura F., Kitada M., Kudo T.
    J. Bacteriol. 182:898-904(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
    Strain: 168.
  6. "Mrp-dependent Na(+)/H(+) antiporters of Bacillus exhibit characteristics that are unanticipated for completely secondary active transporters."
    Ito M., Guffanti A.A., Krulwich T.A.
    FEBS Lett. 496:117-120(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: COUPLING ENERGIZATION MODE.
  7. "Catalytic properties of Staphylococcus aureus and Bacillus members of the secondary cation/proton antiporter-3 (Mrp) family are revealed by an optimized assay in an Escherichia coli host."
    Swartz T.H., Ito M., Ohira T., Natsui S., Hicks D.B., Krulwich T.A.
    J. Bacteriol. 189:3081-3090(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ANTIPORT OF LITHIUM.
  8. "Complex formation by the mrpABCDEFG gene products, which constitute a principal Na+/H+ antiporter in Bacillus subtilis."
    Kajiyama Y., Otagiri M., Sekiguchi J., Kosono S., Kudo T.
    J. Bacteriol. 189:7511-7514(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, SUBCELLULAR LOCATION.
    Strain: 168 / Marburg / UOT1285.

Entry informationi

Entry nameiMRPA_BACSU
AccessioniPrimary (citable) accession number: Q9K2S2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: April 13, 2004
Last modified: July 6, 2016
This is version 102 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Mrp-dependent antiport apparently occurs by a secondary, proton motive force-dependent mechanism, but the similarity of several Mrp proteins to membrane-embedded subunits of energy-coupled NADH dehydrogenase complexes raises the possibility that there is a capacity for electron transport that could provide a primary energy coupling option for Mrp functions.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.