Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

ATPase RavA

Gene

ravA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Functions as an ATPase. May play a role in metal insertion (metal-chelatase) or as a chaperone.

Enzyme regulationi

The complex formed with CadA represents a possible means of regulating RavA activity in response to acid stress conditions. This interaction results in an increase in RavA ATPase activity.

Kineticsi

RavA also has GTPase activity.

  1. KM=790 µM for ATP (at pH 7.5)

    pH dependencei

    Optimum pH is 7.5.

    GO - Molecular functioni

    • ATPase activity Source: EcoCyc
    • ATP binding Source: UniProtKB-KW
    • hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances Source: InterPro
    • identical protein binding Source: IntAct
    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:EG11731-MONOMER.
    ECOL316407:JW3725-MONOMER.
    MetaCyc:EG11731-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    ATPase RavA (EC:3.6.3.-)
    Alternative name(s):
    Regulatory ATPase variant A
    Gene namesi
    Name:ravA
    Synonyms:yieN
    Ordered Locus Names:b3746, JW3725
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG11731. ravA.

    Subcellular locationi

    GO - Cellular componenti

    • cytoplasm Source: EcoCyc
    • cytosol Source: EcoCyc
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 498498ATPase RavAPRO_0000209370Add
    BLAST

    Proteomic databases

    PaxDbiP31473.
    PRIDEiP31473.

    Expressioni

    Inductioni

    Expression is sigma S-dependent.

    Interactioni

    Subunit structurei

    Hexameric oligomer. Interactions of five RavA oligomers with two CadA decamers. Possible formation of a ternary complex RavA-ViaA-CadA.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself4EBI-561223,EBI-561223
    cadAP0A9H37EBI-561223,EBI-545922

    GO - Molecular functioni

    • identical protein binding Source: IntAct

    Protein-protein interaction databases

    BioGridi4262601. 623 interactions.
    DIPiDIP-12469N.
    IntActiP31473. 21 interactions.
    MINTiMINT-1242859.
    STRINGi511145.b3746.

    Structurei

    Secondary structure

    1
    498
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi4 – 1916Combined sources
    Helixi26 – 3813Combined sources
    Beta strandi41 – 455Combined sources
    Beta strandi48 – 514Combined sources
    Helixi52 – 587Combined sources
    Helixi59 – 624Combined sources
    Beta strandi63 – 653Combined sources
    Beta strandi68 – 725Combined sources
    Helixi79 – 835Combined sources
    Helixi105 – 1073Combined sources
    Beta strandi109 – 1157Combined sources
    Helixi116 – 1183Combined sources
    Helixi121 – 13212Combined sources
    Beta strandi133 – 1375Combined sources
    Beta strandi139 – 1446Combined sources
    Beta strandi149 – 1568Combined sources
    Helixi165 – 1684Combined sources
    Beta strandi173 – 1764Combined sources
    Helixi183 – 1908Combined sources
    Turni203 – 2053Combined sources
    Helixi209 – 21911Combined sources
    Helixi226 – 24116Combined sources
    Beta strandi243 – 2453Combined sources
    Helixi250 – 26617Combined sources
    Helixi274 – 2829Combined sources
    Helixi288 – 30417Combined sources
    Turni305 – 3073Combined sources
    Helixi309 – 32921Combined sources
    Turni354 – 3563Combined sources
    Beta strandi360 – 37213Combined sources
    Beta strandi375 – 3839Combined sources
    Helixi384 – 39310Combined sources
    Beta strandi398 – 4014Combined sources
    Beta strandi405 – 4095Combined sources
    Beta strandi411 – 4144Combined sources
    Beta strandi420 – 4234Combined sources
    Beta strandi429 – 4335Combined sources
    Helixi444 – 46522Combined sources
    Helixi475 – 49521Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3NBXX-ray2.91X1-498[»]
    4UPBelectron microscopy11.00C/D/E1-498[»]
    4UPFelectron microscopy7.50D329-440[»]
    ProteinModelPortaliP31473.
    SMRiP31473. Positions 3-497.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP31473.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the RavA family.Curated

    Phylogenomic databases

    eggNOGiENOG4107R4Q. Bacteria.
    COG0714. LUCA.
    HOGENOMiHOG000272029.
    InParanoidiP31473.
    KOiK03924.
    OMAiRRFRNGN.
    OrthoDBiEOG6DG2RF.
    PhylomeDBiP31473.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    HAMAPiMF_01625. ATPase_RavA.
    InterProiIPR003593. AAA+_ATPase.
    IPR011704. ATPase_dyneun-rel_AAA.
    IPR023671. ATPase_RavA.
    IPR022547. ATPase_RavA_C.
    IPR027417. P-loop_NTPase.
    [Graphical view]
    PfamiPF07728. AAA_5. 1 hit.
    PF12592. DUF3763. 1 hit.
    [Graphical view]
    SMARTiSM00382. AAA. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P31473-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MAHPHLLAER ISRLSSSLEK GLYERSHAIR LCLLAALSGE SVFLLGPPGI
    60 70 80 90 100
    AKSLIARRLK FAFQNARAFE YLMTRFSTPE EVFGPLSIQA LKDEGRYERL
    110 120 130 140 150
    TSGYLPEAEI VFLDEIWKAG PAILNTLLTA INERQFRNGA HVEKIPMRLL
    160 170 180 190 200
    VAASNELPEA DSSLEALYDR MLIRLWLDKV QDKANFRSML TSQQDENDNP
    210 220 230 240 250
    VPDALQVTDE EYERWQKEIG EITLPDHVFE LIFMLRQQLD KLPDAPYVSD
    260 270 280 290 300
    RRWKKAIRLL QASAFFSGRS AVAPVDLILL KDCLWYDAQS LNLIQQQIDV
    310 320 330 340 350
    LMTGHAWQQQ GMLTRLGAIV QRHLQLQQQQ SDKTALTVIR LGGIFSRRQQ
    360 370 380 390 400
    YQLPVNVTAS TLTLLLQKPL KLHDMEVVHI SFERSALEQW LSKGGEIRGK
    410 420 430 440 450
    LNGIGFAQKL NLEVDSAQHL VVRDVSLQGS TLALPGSSAE GLPGEIKQQL
    460 470 480 490
    EELESDWRKQ HALFSEQQKC LFIPGDWLGR IEASLQDVGA QIRQAQQC
    Length:498
    Mass (Da):56,389
    Last modified:July 15, 1998 - v2
    Checksum:i3D2EDCAA17240BE9
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L10328 Genomic DNA. Translation: AAA62099.1. Frameshift.
    U00096 Genomic DNA. Translation: AAC76769.2.
    AP009048 Genomic DNA. Translation: BAE77542.1.
    PIRiC65178.
    RefSeqiNP_418202.4. NC_000913.3.
    WP_001299914.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76769; AAC76769; b3746.
    BAE77542; BAE77542; BAE77542.
    GeneIDi948256.
    KEGGiecj:JW3725.
    eco:b3746.
    PATRICi32122991. VBIEscCol129921_3871.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L10328 Genomic DNA. Translation: AAA62099.1. Frameshift.
    U00096 Genomic DNA. Translation: AAC76769.2.
    AP009048 Genomic DNA. Translation: BAE77542.1.
    PIRiC65178.
    RefSeqiNP_418202.4. NC_000913.3.
    WP_001299914.1. NZ_LN832404.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3NBXX-ray2.91X1-498[»]
    4UPBelectron microscopy11.00C/D/E1-498[»]
    4UPFelectron microscopy7.50D329-440[»]
    ProteinModelPortaliP31473.
    SMRiP31473. Positions 3-497.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4262601. 623 interactions.
    DIPiDIP-12469N.
    IntActiP31473. 21 interactions.
    MINTiMINT-1242859.
    STRINGi511145.b3746.

    Proteomic databases

    PaxDbiP31473.
    PRIDEiP31473.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC76769; AAC76769; b3746.
    BAE77542; BAE77542; BAE77542.
    GeneIDi948256.
    KEGGiecj:JW3725.
    eco:b3746.
    PATRICi32122991. VBIEscCol129921_3871.

    Organism-specific databases

    EchoBASEiEB1682.
    EcoGeneiEG11731. ravA.

    Phylogenomic databases

    eggNOGiENOG4107R4Q. Bacteria.
    COG0714. LUCA.
    HOGENOMiHOG000272029.
    InParanoidiP31473.
    KOiK03924.
    OMAiRRFRNGN.
    OrthoDBiEOG6DG2RF.
    PhylomeDBiP31473.

    Enzyme and pathway databases

    BioCyciEcoCyc:EG11731-MONOMER.
    ECOL316407:JW3725-MONOMER.
    MetaCyc:EG11731-MONOMER.

    Miscellaneous databases

    EvolutionaryTraceiP31473.
    PROiP31473.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    HAMAPiMF_01625. ATPase_RavA.
    InterProiIPR003593. AAA+_ATPase.
    IPR011704. ATPase_dyneun-rel_AAA.
    IPR023671. ATPase_RavA.
    IPR022547. ATPase_RavA_C.
    IPR027417. P-loop_NTPase.
    [Graphical view]
    PfamiPF07728. AAA_5. 1 hit.
    PF12592. DUF3763. 1 hit.
    [Graphical view]
    SMARTiSM00382. AAA. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome: organizational symmetry around the origin of replication."
      Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.
      Genomics 16:551-561(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], SEQUENCE REVISION.
      Strain: K12 / MG1655 / ATCC 47076.
    3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    4. "Formation of a distinctive complex between the inducible bacterial lysine decarboxylase and a novel AAA+ ATPase."
      Snider J., Gutsche I., Lin M., Baby S., Cox B., Butland G., Greenblatt J., Emili A., Houry W.A.
      J. Biol. Chem. 281:1532-1546(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION, SUBUNIT, INTERACTION WITH CADA AND VIAA.
      Strain: K12 / MG1655 / ATCC 47076.

    Entry informationi

    Entry nameiRAVA_ECOLI
    AccessioniPrimary (citable) accession number: P31473
    Secondary accession number(s): Q2M864
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: July 15, 1998
    Last modified: January 20, 2016
    This is version 134 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. 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.