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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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    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)DescriptionActionsGraphical viewLength
    ChainiPRO_00002093701 – 498ATPase RavAAdd BLAST498

    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 interactors.
    DIPiDIP-12469N.
    IntActiP31473. 21 interactors.
    MINTiMINT-1242859.
    STRINGi511145.b3746.

    Structurei

    Secondary structure

    1498
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi4 – 19Combined sources16
    Helixi26 – 38Combined sources13
    Beta strandi41 – 45Combined sources5
    Beta strandi48 – 51Combined sources4
    Helixi52 – 58Combined sources7
    Helixi59 – 62Combined sources4
    Beta strandi63 – 65Combined sources3
    Beta strandi68 – 72Combined sources5
    Helixi79 – 83Combined sources5
    Helixi105 – 107Combined sources3
    Beta strandi109 – 115Combined sources7
    Helixi116 – 118Combined sources3
    Helixi121 – 132Combined sources12
    Beta strandi133 – 137Combined sources5
    Beta strandi139 – 144Combined sources6
    Beta strandi149 – 156Combined sources8
    Helixi165 – 168Combined sources4
    Beta strandi173 – 176Combined sources4
    Helixi183 – 190Combined sources8
    Turni203 – 205Combined sources3
    Helixi209 – 219Combined sources11
    Helixi226 – 241Combined sources16
    Beta strandi243 – 245Combined sources3
    Helixi250 – 266Combined sources17
    Helixi274 – 282Combined sources9
    Helixi288 – 304Combined sources17
    Turni305 – 307Combined sources3
    Helixi309 – 329Combined sources21
    Turni354 – 356Combined sources3
    Beta strandi360 – 372Combined sources13
    Beta strandi375 – 383Combined sources9
    Helixi384 – 393Combined sources10
    Beta strandi398 – 401Combined sources4
    Beta strandi405 – 409Combined sources5
    Beta strandi411 – 414Combined sources4
    Beta strandi420 – 423Combined sources4
    Beta strandi429 – 433Combined sources5
    Helixi444 – 465Combined sources22
    Helixi475 – 495Combined sources21

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3NBXX-ray2.91X1-498[»]
    4UPBelectron microscopy11.00C/D/E1-498[»]
    4UPFelectron microscopy7.50D329-440[»]
    5FL2electron microscopy6.20K332-437[»]
    ProteinModelPortaliP31473.
    SMRiP31473.
    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.
    PhylomeDBiP31473.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    HAMAPiMF_01625. ATPase_RavA. 1 hit.
    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
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3NBXX-ray2.91X1-498[»]
    4UPBelectron microscopy11.00C/D/E1-498[»]
    4UPFelectron microscopy7.50D329-440[»]
    5FL2electron microscopy6.20K332-437[»]
    ProteinModelPortaliP31473.
    SMRiP31473.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4262601. 623 interactors.
    DIPiDIP-12469N.
    IntActiP31473. 21 interactors.
    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.
    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. 1 hit.
    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...

    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: November 2, 2016
    This is version 137 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.