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P13658

- MBEA_ECOLX

UniProt

P13658 - MBEA_ECOLX

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Protein

DNA relaxase MbeA

Gene
mbeA
Organism
Escherichia coli
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 cation Inferred
Metal bindingi104 – 1041Divalent metal cation Inferred
Metal bindingi106 – 1061Divalent metal cation Inferred

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
Complete GO annotation...

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.

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

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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: June 11, 2014
This is version 48 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

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