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P07112

- MOBA2_ECOLX

UniProt

P07112 - MOBA2_ECOLX

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Protein

Mobilization protein A

Gene

mobA

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

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

Mg2+2 Publications, Mn2+2 Publications, Ca2+2 Publications, Ba2+2 PublicationsNote: Divalent metal cation. Can use Mg(2+), or to a lesser extent, Mn(2+), Ca(2+) or Ba(2+).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. conjugation Source: UniProtKB-KW
Complete GO annotation...

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-KW
Complete GO annotation...

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:
PDBei
RCSB PDBi
PDBji
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

        10         20         30         40         50
MAIYHLTAKT GSRSGGQSAR AKADYIQREG KYARDMDEVL HAESGHMPEF
60 70 80 90 100
VERPADYWDA ADLYERANGR LFKEVEFALP VELTLDQQKA LASEFAQHLT
110 120 130 140 150
GAERLPYTLA IHAGGGENPH CHLMISERIN DGIERPAAQW FKRYNGKTPE
160 170 180 190 200
KGGAQKTEAL KPKAWLEQTR EAWADHANRA LERAGHDARI DHRTLEAQGI
210 220 230 240 250
ERLPGVHLGP NVVEMEGRGI RTDRADVALN IDTANAQIID LQEYREAIDH
260 270 280 290 300
ERNRQSEEIQ RHQRVSGADR TAGPEHGDTG RRSPAGHEPD PAGQRGAGGG
310 320 330 340 350
VAESPAPDRG GMGGAGQRVA GGSRRGEQRR AERPERVAGV ALEAMANRDA
360 370 380 390 400
GFHDAYGGAA DRIVALARPD ATDNRGRLDL AALGGPMKND RTLQAIGRQL
410 420 430 440 450
KAMGCERFDI GVRDATTGQM MNREWSAAEV LQNTPWLKRM NAQGNDVYIR
460 470 480 490 500
PAEQERHGLV LVDDLSEFDL DDMKAEGREP ALVVETSPKN YQAWVKVADA
510 520 530 540 550
AGGELRGQIA RTLASEYDAD PASADSRHYG RLAGFTNRKD KHTTRAGYQP
560 570 580 590 600
WVLLRESKGK TATAGPALVQ QAGQQIEQAQ RQQEKARRLA SLELPERQLS
610 620 630 640 650
RHRRTALDEY RSEMAGLVKR FGDDLSKCDF IAAQKLASRG RSAEEIGKAM
660 670 680 690 700
AEASPALAER KPGHEADYIE RTVSKVMGLP SVQLARAELA RAPAPRQRGM

DRGGPDFSM
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 79 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