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Protein

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

Gene

mrpD

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 3 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+.2 Publications

GO - Molecular functioni

  • NADH dehydrogenase (ubiquinone) activity Source: InterPro
  • potassium:proton antiporter 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, Transport

Keywords - Ligandi

Sodium

Enzyme and pathway databases

BioCyciBSUB:BSU31630-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 D
Alternative name(s):
Mrp complex subunit D
Multiple resistance and pH homeostasis protein D
Gene namesi
Name:mrpD
Synonyms:yufD
Ordered Locus Names:BSU31630
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei3 – 2321HelicalSequence analysisAdd
BLAST
Transmembranei31 – 5121HelicalSequence analysisAdd
BLAST
Transmembranei77 – 9721HelicalSequence analysisAdd
BLAST
Transmembranei107 – 12721HelicalSequence analysisAdd
BLAST
Transmembranei129 – 14921HelicalSequence analysisAdd
BLAST
Transmembranei163 – 18321HelicalSequence analysisAdd
BLAST
Transmembranei203 – 22321HelicalSequence analysisAdd
BLAST
Transmembranei227 – 24721HelicalSequence analysisAdd
BLAST
Transmembranei251 – 27121HelicalSequence analysisAdd
BLAST
Transmembranei274 – 29421HelicalSequence analysisAdd
BLAST
Transmembranei299 – 31921HelicalSequence analysisAdd
BLAST
Transmembranei330 – 35021HelicalSequence analysisAdd
BLAST
Transmembranei370 – 39021HelicalSequence analysisAdd
BLAST
Transmembranei407 – 42721HelicalSequence analysisAdd
BLAST
Transmembranei449 – 46921HelicalSequence 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 – 493493Na(+)/H(+) antiporter subunit DPRO_0000217084Add
BLAST

Proteomic databases

PaxDbiO05229.

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

STRINGi224308.Bsubs1_010100017186.

Structurei

3D structure databases

ProteinModelPortaliO05229.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4108JPZ. Bacteria.
COG0651. LUCA.
HOGENOMiHOG000066542.
InParanoidiO05229.
KOiK05568.
OMAiIFHPTFL.
PhylomeDBiO05229.

Family and domain databases

InterProiIPR004775. MnhD1.
IPR003918. NADH_UbQ_OxRdtase.
IPR001750. ND/Mrp_mem.
[Graphical view]
PfamiPF00361. Proton_antipo_M. 1 hit.
[Graphical view]
PRINTSiPR01437. NUOXDRDTASE4.
TIGRFAMsiTIGR00944. 2a6301s04. 1 hit.

Sequencei

Sequence statusi: Complete.

O05229-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNNFVILPIL IPLLSAILLI FMTKNLMLMR IFSTAASAIG IVISGILVQT
60 70 80 90 100
VFTKGIQTLS LGGWKAPYGI VLAADQFASL LVLTTAIIGL LVGLYSFRSV
110 120 130 140 150
GEKRERSFYY SGVQFLLAGV SGAFLTGDLF NMYVFFELLL IASYMLIVLG
160 170 180 190 200
GTKIQLRESL KYIVFNIVSS ALFVIGVGFL YAVTGTLNMA DLSVKISESG
210 220 230 240 250
QTGLITVIGV LLLLVFGMKG GIFPLYFWLP GSYYAPPAAI SALFGALLTK
260 270 280 290 300
VGLYAITRVF TLIFIHDTAF THQLMIWLAA LTVIFGVIGS LAYSNVMKIV
310 320 330 340 350
IYNIITAVGV ILFGVAVHTP ASIQGAIYYL IHDMLIKGAL FMLAGTLIAL
360 370 380 390 400
TGTASLHKMG GLIKRYPVLG WMFFISAISL AGIPPLSGFV GKFKIAEGGF
410 420 430 440 450
AEGEFTISML ILLSSLLVLY SVLRIFIHAF WGEEKETPKP NHRTAKGLLY
460 470 480 490
PAAIFLLLSL LFGLGTEWVS PYVDQAAETL LNPEKYIEAV LKE
Length:493
Mass (Da):53,477
Last modified:July 28, 2009 - v3
Checksum:i8A29662C5DF64BFB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti8 – 81P → A in CAB07908 (PubMed:9274030).Curated
Sequence conflicti13 – 131L → I in CAB07908 (PubMed:9274030).Curated
Sequence conflicti474 – 49320DQAAE…AVLKE → IKRPRRC in CAB07908 (PubMed:9274030).CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z93932 Genomic DNA. Translation: CAB07908.1.
AL009126 Genomic DNA. Translation: CAB15152.3.
PIRiG70008.
RefSeqiNP_391041.3. NC_000964.3.
WP_003244432.1. NZ_JNCM01000033.1.

Genome annotation databases

EnsemblBacteriaiCAB15152; CAB15152; BSU31630.
GeneIDi938858.
KEGGibsu:BSU31630.
PATRICi18978296. VBIBacSub10457_3311.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z93932 Genomic DNA. Translation: CAB07908.1.
AL009126 Genomic DNA. Translation: CAB15152.3.
PIRiG70008.
RefSeqiNP_391041.3. NC_000964.3.
WP_003244432.1. NZ_JNCM01000033.1.

3D structure databases

ProteinModelPortaliO05229.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100017186.

Protein family/group databases

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

Proteomic databases

PaxDbiO05229.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB15152; CAB15152; BSU31630.
GeneIDi938858.
KEGGibsu:BSU31630.
PATRICi18978296. VBIBacSub10457_3311.

Phylogenomic databases

eggNOGiENOG4108JPZ. Bacteria.
COG0651. LUCA.
HOGENOMiHOG000066542.
InParanoidiO05229.
KOiK05568.
OMAiIFHPTFL.
PhylomeDBiO05229.

Enzyme and pathway databases

BioCyciBSUB:BSU31630-MONOMER.

Family and domain databases

InterProiIPR004775. MnhD1.
IPR003918. NADH_UbQ_OxRdtase.
IPR001750. ND/Mrp_mem.
[Graphical view]
PfamiPF00361. Proton_antipo_M. 1 hit.
[Graphical view]
PRINTSiPR01437. NUOXDRDTASE4.
TIGRFAMsiTIGR00944. 2a6301s04. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiMRPD_BACSU
AccessioniPrimary (citable) accession number: O05229
Secondary accession number(s): O32088
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: July 28, 2009
Last modified: September 7, 2016
This is version 110 of the entry and version 3 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.