Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P13658

- MBEA_ECOLX

UniProt

P13658 - MBEA_ECOLX

Protein

DNA relaxase MbeA

Gene

mbeA

Organism
Escherichia coli
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 49 (01 Oct 2014)
      Sequence version 1 (01 Jan 1990)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Relaxase involved in plasmid ColE1 conjugative mobilization and is thus essential to promote the specific transfer of the plasmid during conjugation. First catalyzes the specific cleavage of one of the DNA strands at oriT, forming a covalent 5'-phosphotyrosine intermediate. The nic site corresponds to 5'-(1469)CTGG/CTTA(1462)-3' in the cleaved strand. The cleaved strand is then transferred through the dedicated type IV secretion apparatus. MbeA remains covalently linked at the 5' end of the strand, and once in the recipient cell, it probably catalyzes the rejoining of the two ends of the strand, re-forming the circular plasmid DNA. Is functional in vitro without a requirement for the conjugative accessory proteins.1 Publication

    Catalytic activityi

    ATP-independent breakage of single-stranded DNA, followed by passage and rejoining.

    Cofactori

    Divalent metal cation. Can use Mg2+, Co2+ and Ni2+ with similar efficiencies, but is not active in the presence of Mn2+.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei19 – 191O-(5'-phospho-DNA)-tyrosine intermediate
    Metal bindingi97 – 971Divalent metal cationCurated
    Metal bindingi104 – 1041Divalent metal cationCurated
    Metal bindingi106 – 1061Divalent metal cationCurated

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW
    2. DNA topoisomerase type I activity Source: UniProtKB-EC
    3. metal ion binding Source: UniProtKB-KW
    4. protein binding Source: IntAct

    GO - Biological processi

    1. conjugation Source: UniProtKB-KW

    Keywords - Molecular functioni

    Isomerase, Mobility protein, Topoisomerase

    Keywords - Biological processi

    Conjugation

    Keywords - Ligandi

    Cobalt, DNA-binding, Magnesium, Metal-binding, Nickel

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DNA relaxase MbeA (EC:5.99.1.2)
    Alternative name(s):
    DNA nickase
    Mobilization protein MbeA
    Gene namesi
    Name:mbeA
    Encoded oniPlasmid ColE10 Publication
    OrganismiEscherichia coli
    Taxonomic identifieri562 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi19 – 191Y → A: Loss of in vitro DNA-cleavage activity and in vivo functionality. 1 Publication
    Mutagenesisi97 – 971H → A: Loss of in vitro DNA-cleavage activity and in vivo functionality. No effect on DNA binding around the nic site. 1 Publication
    Mutagenesisi104 – 1041E → A: Loss of in vitro DNA-cleavage activity and in vivo functionality. No effect on DNA binding around the nic site. 1 Publication
    Mutagenesisi104 – 1041E → H: Loss of the in vitro DNA-cleavage and strand-transfer activities but displays 1% of the in vivo wild-type activity; when associated with H-106. 1 Publication
    Mutagenesisi106 – 1061N → A: 4-fold and 3-fold reduction in the in vitro DNA-cleavage and strand-transfer activities, respectively, but no reduction in the in vivo functionality. 1 Publication
    Mutagenesisi106 – 1061N → H: Loss of the in vitro DNA-cleavage and strand-transfer activities but displays 1% of the in vivo wild-type activity; when associated with H-104. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 517517DNA relaxase MbeAPRO_0000068400Add
    BLAST

    Proteomic databases

    PRIDEiP13658.

    Interactioni

    Subunit structurei

    Interacts with MbeB and MbeC to form the relaxosome.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    mbeCP136572EBI-7798346,EBI-7798318

    Protein-protein interaction databases

    IntActiP13658. 1 interaction.
    MINTiMINT-8306165.

    Family & Domainsi

    Sequence similaritiesi

    To E.coli MbaA and MbkA.Curated

    Family and domain databases

    InterProiIPR005094. Endonuclease_MobA/VirD2.
    [Graphical view]
    PfamiPF03432. Relaxase. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P13658-1 [UniParc]FASTAAdd to Basket

    « Hide

    MIVKFHARGK GGGSGPVDYL LGRERNREGA TVLQGNPEEV RELIDATPFA    50
    KKYTSGVLSF AEKELPPGGR EKVMASFERV LMPGLEKNQY SILWVEHQDK 100
    GRLELNFVIP NMELQTGKRL QPYYDRADRP RIDAWQTLVN HHYGLHDPNA 150
    PENRRTLTLP DNLPETKQAL AEGVTRGIDA LYHAGEIKGR QDVIQALTEA 200
    GLEVVRVTRT SISIADPNGG KNIRLKGAFY EQSFADGRGV REKAERESRI 250
    YRENAEQRVQ EARRICKRGC DIKRDENQRR YSPVHSLDRG IAGKTPGRGE 300
    RGDDAAQEGR VKAGREYGHD VTGDSLSPVY REWRDALVSW REDTGEPGRN 350
    QEAGRDIAET EREDMGRGVC AGREQEIPCP SVREISGGDS LSGERVGTSE 400
    GVTQSDRAGN TFAERLRAAA TGLYAAAERM GERLRGIAED VFAYATGQRD 450
    AERAGHAVES AGAALERADR TLEPVIQREL EIREERLIQE REHVLSLERE 500
    RQPEIQERTL DGPSLGW 517
    Length:517
    Mass (Da):57,808
    Last modified:January 1, 1990 - v1
    Checksum:i278E41B2D3B2A08A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X15873 Genomic DNA. Translation: CAA33883.1.
    PIRiJQ0390.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X15873 Genomic DNA. Translation: CAA33883.1 .
    PIRi JQ0390.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P13658. 1 interaction.
    MINTi MINT-8306165.

    Proteomic databases

    PRIDEi P13658.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    InterProi IPR005094. Endonuclease_MobA/VirD2.
    [Graphical view ]
    Pfami PF03432. Relaxase. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of the ColE1 mobilization region and its protein products."
      Boyd A.C., Archer J.A.K., Sherratt D.J.
      Mol. Gen. Genet. 217:488-498(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Genetic and biochemical characterization of MbeA, the relaxase involved in plasmid ColE1 conjugative mobilization."
      Varsaki A., Lucas M., Afendra A.S., Drainas C., de la Cruz F.
      Mol. Microbiol. 48:481-493(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS A RELAXASE, COFACTOR, DETERMINATION OF THE NIC SITE, MUTAGENESIS OF TYR-19; HIS-97; GLU-104 AND ASN-106.

    Entry informationi

    Entry nameiMBEA_ECOLX
    AccessioniPrimary (citable) accession number: P13658
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: January 1, 1990
    Last modified: October 1, 2014
    This is version 49 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The 100 C-terminal amino acids are dispensable for activity.

    Keywords - Technical termi

    Plasmid

    External Data

    Dasty 3