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

DNA relaxase MbeA

Gene

mbeA

Organism
Escherichia coli
Status
Reviewed-Annotation score: 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

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei19O-(5'-phospho-DNA)-tyrosine intermediate1
Metal bindingi97Divalent metal cationCurated1
Metal bindingi104Divalent metal cationCurated1
Metal bindingi106Divalent metal cationCurated1

GO - Molecular functioni

GO - Biological processi

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi19Y → A: Loss of in vitro DNA-cleavage activity and in vivo functionality. 1 Publication1
Mutagenesisi97H → A: Loss of in vitro DNA-cleavage activity and in vivo functionality. No effect on DNA binding around the nic site. 1 Publication1
Mutagenesisi104E → A: Loss of in vitro DNA-cleavage activity and in vivo functionality. No effect on DNA binding around the nic site. 1 Publication1
Mutagenesisi104E → 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 Publication1
Mutagenesisi106N → 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 Publication1
Mutagenesisi106N → 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 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000684001 – 517DNA relaxase MbeAAdd BLAST517

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 interactor.
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

        10         20         30         40         50
MIVKFHARGK GGGSGPVDYL LGRERNREGA TVLQGNPEEV RELIDATPFA
60 70 80 90 100
KKYTSGVLSF AEKELPPGGR EKVMASFERV LMPGLEKNQY SILWVEHQDK
110 120 130 140 150
GRLELNFVIP NMELQTGKRL QPYYDRADRP RIDAWQTLVN HHYGLHDPNA
160 170 180 190 200
PENRRTLTLP DNLPETKQAL AEGVTRGIDA LYHAGEIKGR QDVIQALTEA
210 220 230 240 250
GLEVVRVTRT SISIADPNGG KNIRLKGAFY EQSFADGRGV REKAERESRI
260 270 280 290 300
YRENAEQRVQ EARRICKRGC DIKRDENQRR YSPVHSLDRG IAGKTPGRGE
310 320 330 340 350
RGDDAAQEGR VKAGREYGHD VTGDSLSPVY REWRDALVSW REDTGEPGRN
360 370 380 390 400
QEAGRDIAET EREDMGRGVC AGREQEIPCP SVREISGGDS LSGERVGTSE
410 420 430 440 450
GVTQSDRAGN TFAERLRAAA TGLYAAAERM GERLRGIAED VFAYATGQRD
460 470 480 490 500
AERAGHAVES AGAALERADR TLEPVIQREL EIREERLIQE REHVLSLERE
510
RQPEIQERTL DGPSLGW
Length:517
Mass (Da):57,808
Last modified:January 1, 1990 - v1
Checksum:i278E41B2D3B2A08A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15873 Genomic DNA. Translation: CAA33883.1.
PIRiJQ0390.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15873 Genomic DNA. Translation: CAA33883.1.
PIRiJQ0390.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP13658. 1 interactor.
MINTiMINT-8306165.

Proteomic databases

PRIDEiP13658.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

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

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: November 2, 2016
This is version 52 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

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.