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P07112

- MOBA2_ECOLX

UniProt

P07112 - MOBA2_ECOLX

Protein

Mobilization protein A

Gene

mobA

Organism
Escherichia coli
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 77 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    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.2 Publications

    Catalytic activityi

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

    Cofactori

    Divalent metal cation. Can use Mg2+, and to a lesser extent, Mn2+, Ca2+ or Ba2+.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei25 – 251O-(5'-phospho-DNA)-tyrosine intermediate; for relaxase activity
    Sitei70 – 701Involved in DNA bindingCurated
    Metal bindingi112 – 1121Divalent metal cation
    Metal bindingi120 – 1201Divalent metal cation
    Metal bindingi122 – 1221Divalent metal cation

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW
    2. DNA-directed RNA polymerase activity Source: UniProtKB-KW
    3. DNA topoisomerase type I activity Source: UniProtKB-EC
    4. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. unidirectional conjugation Source: InterPro

    Keywords - Molecular functioni

    Isomerase, Mobility protein, Topoisomerase, Transferase

    Keywords - Biological processi

    Conjugation, Transcription

    Keywords - Ligandi

    Calcium, DNA-binding, Magnesium, Manganese, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mobilization protein A
    Alternative name(s):
    DNA strand transferase
    Including the following 2 domains:
    DNA relaxase (EC:5.99.1.2)
    Alternative name(s):
    DNA nickase
    DNA primase (EC:2.7.7.-)
    Gene namesi
    Name:mobA
    Synonyms:repB
    Encoded oniPlasmid IncQ RSF10105 Publications
    Plasmid R11626 Publications
    OrganismiEscherichia coli
    Taxonomic identifieri562 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

    Subcellular locationi

    Cytoplasm Curated

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, DNA-directed RNA polymerase

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi25 – 251Y → F: 99.5% decrease in conjugal transfer frequency. 1 Publication
    Mutagenesisi32 – 321Y → F: No decrease in conjugal transfer frequency. 1 Publication
    Mutagenesisi38 – 381E → A: No decrease in conjugal transfer frequency. 1 Publication
    Mutagenesisi74 – 741E → 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. 1 Publication
    Mutagenesisi74 – 741E → Q: 70% decrease in conjugal transfer frequency. 1 Publication
    Mutagenesisi76 – 761E → 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. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 709708Mobilization protein APRO_0000210849Add
    BLAST

    Proteomic databases

    PRIDEiP07112.

    Interactioni

    Subunit structurei

    Interacts with MobB and MobC to form the relaxosome.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    rplVP611751EBI-554383,EBI-542255From a different organism.

    Protein-protein interaction databases

    IntActiP07112. 1 interaction.

    Structurei

    Secondary structure

    1
    709
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi6 – 94
    Helixi19 – 279
    Helixi32 – 343
    Beta strandi39 – 435
    Helixi54 – 6411
    Beta strandi73 – 786
    Helixi85 – 9915
    Beta strandi107 – 1126
    Beta strandi120 – 1256
    Helixi137 – 1404
    Helixi165 – 18218

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2NS6X-ray2.10A2-186[»]
    ProteinModelPortaliP07112.
    SMRiP07112. Positions 2-186.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP07112.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 186185DNA relaxaseAdd
    BLAST
    Regioni315 – 709395DNA primaseAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili567 – 59428Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the MobA/MobL family.Curated

    Keywords - Domaini

    Coiled coil

    Family and domain databases

    InterProiIPR005053. MobA_MobL.
    [Graphical view]
    PfamiPF03389. MobA_MobL. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P07112-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAIYHLTAKT GSRSGGQSAR AKADYIQREG KYARDMDEVL HAESGHMPEF    50
    VERPADYWDA ADLYERANGR LFKEVEFALP VELTLDQQKA LASEFAQHLT 100
    GAERLPYTLA IHAGGGENPH CHLMISERIN DGIERPAAQW FKRYNGKTPE 150
    KGGAQKTEAL KPKAWLEQTR EAWADHANRA LERAGHDARI DHRTLEAQGI 200
    ERLPGVHLGP NVVEMEGRGI RTDRADVALN IDTANAQIID LQEYREAIDH 250
    ERNRQSEEIQ RHQRVSGADR TAGPEHGDTG RRSPAGHEPD PAGQRGAGGG 300
    VAESPAPDRG GMGGAGQRVA GGSRRGEQRR AERPERVAGV ALEAMANRDA 350
    GFHDAYGGAA DRIVALARPD ATDNRGRLDL AALGGPMKND RTLQAIGRQL 400
    KAMGCERFDI GVRDATTGQM MNREWSAAEV LQNTPWLKRM NAQGNDVYIR 450
    PAEQERHGLV LVDDLSEFDL DDMKAEGREP ALVVETSPKN YQAWVKVADA 500
    AGGELRGQIA RTLASEYDAD PASADSRHYG RLAGFTNRKD KHTTRAGYQP 550
    WVLLRESKGK TATAGPALVQ QAGQQIEQAQ RQQEKARRLA SLELPERQLS 600
    RHRRTALDEY RSEMAGLVKR FGDDLSKCDF IAAQKLASRG RSAEEIGKAM 650
    AEASPALAER KPGHEADYIE RTVSKVMGLP SVQLARAELA RAPAPRQRGM 700
    DRGGPDFSM 709
    Length:709
    Mass (Da):77,952
    Last modified:January 23, 2007 - v4
    Checksum:iDDEACDC3CA53D3E1
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti291 – 2911P → Q in AAB22064. (PubMed:1563624)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M28829 Genomic DNA. Translation: AAA26445.1.
    X04830 Genomic DNA. Translation: CAA28520.1.
    S96966 Genomic DNA. Translation: AAB22064.1.
    PIRiJH0126.
    RefSeqiNP_044304.1. NC_001740.1.

    Genome annotation databases

    GeneIDi2716949.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M28829 Genomic DNA. Translation: AAA26445.1 .
    X04830 Genomic DNA. Translation: CAA28520.1 .
    S96966 Genomic DNA. Translation: AAB22064.1 .
    PIRi JH0126.
    RefSeqi NP_044304.1. NC_001740.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2NS6 X-ray 2.10 A 2-186 [» ]
    ProteinModelPortali P07112.
    SMRi P07112. Positions 2-186.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P07112. 1 interaction.

    Chemistry

    BindingDBi P07112.
    ChEMBLi CHEMBL5420.

    Proteomic databases

    PRIDEi P07112.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 2716949.

    Miscellaneous databases

    EvolutionaryTracei P07112.

    Family and domain databases

    InterProi IPR005053. MobA_MobL.
    [Graphical view ]
    Pfami PF03389. MobA_MobL. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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].
      Plasmid: IncQ RSF1010
    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.
      Plasmid: IncQ RSF1010
    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.
      Plasmid: IncQ RSF1010
    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.
      Plasmid: IncQ RSF1010
    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.
      Plasmid: IncQ RSF1010
    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.
      Plasmid: R1162
    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.
      Plasmid: R1162
    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.
      Plasmid: R1162
    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.
      Plasmid: R1162
    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.
      Plasmid: R1162
    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.
      Plasmid: R1162

    Entry informationi

    Entry nameiMOBA2_ECOLX
    AccessioniPrimary (citable) accession number: P07112
    Secondary accession number(s): Q60198
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1988
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 77 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing, Multifunctional enzyme, Plasmid

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3