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P07112 (MOBA2_ECOLX) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mobilization protein A
Alternative name(s):
DNA strand transferase

Including the following 2 domains:

  1. DNA relaxase
    EC=5.99.1.2
    Alternative name(s):
    DNA nickase
  2. DNA primase
    EC=2.7.7.-
Gene names
Name:mobA
Synonyms:repB
Encoded onPlasmid IncQ RSF1010 Ref.1 Ref.2 Ref.3 Ref.4 Ref.5
Plasmid R1162 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11
OrganismEscherichia coli
Taxonomic identifier562 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length709 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Part of the relaxosome complex that is responsible for plasmid transfer during conjugation. Locally unwinds DNA and catalyzes the cleavage of one of the DNA strands at oriT. The cleaved strand is then transferred through the dedicated type IV secretion apparatus. MobA 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. The primase activity of MobA is essential for the synthesis of primers that will initiate the DNA replication events necessary to form the double-stranded plasmid in the recipient cell. Ref.5 Ref.7

Catalytic activity

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

Cofactor

Divalent metal cation. Can use Mg2+, and to a lesser extent, Mn2+, Ca2+ or Ba2+. Ref.4 Ref.5

Subunit structure

Interacts with MobB and MobC to form the relaxosome.

Subcellular location

Cytoplasm Probable.

Sequence similarities

Belongs to the MobA/MobL family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

rplVP611751EBI-554383,EBI-542255From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4
Chain2 – 709708Mobilization protein A
PRO_0000210849

Regions

Region2 – 186185DNA relaxase
Region315 – 709395DNA primase
Coiled coil567 – 59428 Potential

Sites

Active site251O-(5'-phospho-DNA)-tyrosine intermediate; for relaxase activity
Metal binding1121Divalent metal cation
Metal binding1201Divalent metal cation
Metal binding1221Divalent metal cation
Site701Involved in DNA binding Probable

Experimental info

Mutagenesis251Y → F: 99.5% decrease in conjugal transfer frequency. Ref.11
Mutagenesis321Y → F: No decrease in conjugal transfer frequency. Ref.11
Mutagenesis381E → A: No decrease in conjugal transfer frequency. Ref.11
Mutagenesis741E → A: 50% decrease in conjugal transfer frequency. 10-fold decrease in conjugal transfer frequency and great reduction in the rate of DNA cleavage; when associated with A-76. Ref.11
Mutagenesis741E → Q: 70% decrease in conjugal transfer frequency. Ref.11
Mutagenesis761E → A: No decrease in conjugal transfer frequency. 10-fold decrease in conjugal transfer frequency and great reduction in the rate of DNA cleavage; when associated with A-74. Ref.11
Sequence conflict2911P → Q in AAB22064. Ref.3

Secondary structure

....................... 709
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P07112 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: DDEACDC3CA53D3E1

FASTA70977,952
        10         20         30         40         50         60 
MAIYHLTAKT GSRSGGQSAR AKADYIQREG KYARDMDEVL HAESGHMPEF VERPADYWDA 

        70         80         90        100        110        120 
ADLYERANGR LFKEVEFALP VELTLDQQKA LASEFAQHLT GAERLPYTLA IHAGGGENPH 

       130        140        150        160        170        180 
CHLMISERIN DGIERPAAQW FKRYNGKTPE KGGAQKTEAL KPKAWLEQTR EAWADHANRA 

       190        200        210        220        230        240 
LERAGHDARI DHRTLEAQGI ERLPGVHLGP NVVEMEGRGI RTDRADVALN IDTANAQIID 

       250        260        270        280        290        300 
LQEYREAIDH ERNRQSEEIQ RHQRVSGADR TAGPEHGDTG RRSPAGHEPD PAGQRGAGGG 

       310        320        330        340        350        360 
VAESPAPDRG GMGGAGQRVA GGSRRGEQRR AERPERVAGV ALEAMANRDA GFHDAYGGAA 

       370        380        390        400        410        420 
DRIVALARPD ATDNRGRLDL AALGGPMKND RTLQAIGRQL KAMGCERFDI GVRDATTGQM 

       430        440        450        460        470        480 
MNREWSAAEV LQNTPWLKRM NAQGNDVYIR PAEQERHGLV LVDDLSEFDL DDMKAEGREP 

       490        500        510        520        530        540 
ALVVETSPKN YQAWVKVADA AGGELRGQIA RTLASEYDAD PASADSRHYG RLAGFTNRKD 

       550        560        570        580        590        600 
KHTTRAGYQP WVLLRESKGK TATAGPALVQ QAGQQIEQAQ RQQEKARRLA SLELPERQLS 

       610        620        630        640        650        660 
RHRRTALDEY RSEMAGLVKR FGDDLSKCDF IAAQKLASRG RSAEEIGKAM AEASPALAER 

       670        680        690        700 
KPGHEADYIE RTVSKVMGLP SVQLARAELA RAPAPRQRGM DRGGPDFSM 

« Hide

References

[1]"Complete nucleotide sequence and gene organization of the broad-host-range plasmid RSF1010."
Scholz P., Haring V., Wittmann-Liebold B., Ashman K., Bagdasarian M., Scherzinger E.
Gene 75:271-288(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Mobilization of the non-conjugative plasmid RSF1010: a genetic and DNA sequence analysis of the mobilization region."
Derbyshire K.M., Hatfull G., Willetts N.
Mol. Gen. Genet. 206:161-168(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-407.
[3]"Replication and copy number control of the broad-host-range plasmid RSF1010."
Frey J., Bagdasarian M.M., Bagdasarian M.
Gene 113:101-106(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-400.
[4]"Purification of the large mobilization protein of plasmid RSF1010 and characterization of its site-specific DNA-cleaving/DNA-joining activity."
Scherzinger E., Kruft V., Otto S.
Eur. J. Biochem. 217:929-938(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-15 AND 23-31, COFACTOR.
[5]"In vitro cleavage of double- and single-stranded DNA by plasmid RSF1010-encoded mobilization proteins."
Scherzinger E., Lurz R., Otto S., Dobrinski B.
Nucleic Acids Res. 20:41-48(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN DNA CLEAVAGE, COFACTOR.
[6]"Specific binding of MobA, a plasmid-encoded protein involved in the initiation and termination of conjugal DNA transfer, to single-stranded oriT DNA."
Bhattacharjee M.K., Meyer R.J.
Nucleic Acids Res. 21:4563-4568(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: BINDING TO SINGLE-STRANDED ORIT.
[7]"The primase of broad-host-range plasmid R1162 is active in conjugal transfer."
Henderson D., Meyer R.J.
J. Bacteriol. 178:6888-6894(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF PRIMASE DOMAIN IN CONJUGAL TRANSFER.
[8]"The MobA-linked primase is the only replication protein of R1162 required for conjugal mobilization."
Henderson D., Meyer R.
J. Bacteriol. 181:2973-2978(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: PRIMASE ACTIVITY.
[9]"MobA, the DNA strand transferase of plasmid R1162: the minimal domain required for DNA processing at the origin of transfer."
Becker E.C., Meyer R.J.
J. Biol. Chem. 277:14575-14580(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: TRANSFERASE ACTIVITY.
[10]"Relaxed specificity of the R1162 nickase: a model for evolution of a system for conjugative mobilization of plasmids."
Becker E.C., Meyer R.J.
J. Bacteriol. 185:3538-3546(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SPECIFICITY OF DNA SEQUENCE FOR CLEAVAGE.
[11]"The structure of the minimal relaxase domain of MobA at 2.1 A resolution."
Monzingo A.F., Ozburn A., Xia S., Meyer R.J., Robertus J.D.
J. Mol. Biol. 366:165-178(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 2-186 IN COMPLEX WITH MANGANESE, REACTION MECHANISM, MUTAGENESIS OF TYR-25; TYR-32; GLU-38; GLU-74 AND GLU-76.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M28829 Genomic DNA. Translation: AAA26445.1.
X04830 Genomic DNA. Translation: CAA28520.1.
S96966 Genomic DNA. Translation: AAB22064.1.
PIRJH0126.
RefSeqNP_044304.1. NC_001740.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2NS6X-ray2.10A2-186[»]
ProteinModelPortalP07112.
SMRP07112. Positions 2-186.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP07112. 1 interaction.

Chemistry

BindingDBP07112.
ChEMBLCHEMBL5420.

Proteomic databases

PRIDEP07112.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2716949.

Family and domain databases

InterProIPR005053. MobA_MobL.
[Graphical view]
PfamPF03389. MobA_MobL. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP07112.

Entry information

Entry nameMOBA2_ECOLX
AccessionPrimary (citable) accession number: P07112
Secondary accession number(s): Q60198
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: January 23, 2007
Last modified: May 14, 2014
This is version 76 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references