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P0A3U1 (LTRA_LACLM) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 33. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Group II intron-encoded protein ltrA

Including the following 3 domains:

  1. Reverse-transcriptase
    EC=2.7.7.49
  2. RNA maturase
    EC=3.1.-.-
  3. DNA endonuclease
    EC=3.1.-.-
Gene names
Name:ltrA
Synonyms:matR
Ordered Locus Names:llmg_1371
OrganismLactococcus lactis subsp. cremoris (strain MG1363) [Complete proteome] [HAMAP]
Taxonomic identifier416870 [NCBI]
Taxonomic lineageBacteriaFirmicutesLactobacillalesStreptococcaceaeLactococcus

Protein attributes

Sequence length599 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Multifunctional protein that promotes group II intron splicing and mobility by acting both on RNA and DNA. It has three activities: reverse transcriptase (RT) for intron duplication, maturase to promote splicing, and DNA endonuclease for site-specific cleavage of recipient alleles. The intron-encoded protein promotes splicing by facilitating the formation of the catalytically active structure of the intron RNA. After splicing, the protein remains bound to the excised intron lariat RNA, forming ribonucleoprotein particles, and cleaving the antisense strand of the recipient DNA in the 3' exon. After DNA cleavage, retrohoming occurs by a target DNA-primed reverse transcription of the intron RNA that had reverse spliced into the sense strand of the recipient DNA. It also contributes to the recognition of the DNA target site and acts as a repressor of its own translation.

Catalytic activity

Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).

Cofactor

Magnesium.

Subunit structure

Homodimer Probable.

Biotechnological use

Mobile group II introns can be retargeted and used for highly specific chromosomal gene disruption in bacteria. Could be useful for genetic engineering and functional genomics in a wide variety of bacteria.

Miscellaneous

The correct folding of ltrA seems to be facilitated by binding to the unspliced precursor or intron RNA. RNA would serve in part as a chaperone that promotes folding of the protein into an active conformation. Purified protein lacks endonuclease activity unless complexed with intron lariat RNA. It may preferentially function in cis by binding to the intron RNA from which it was translated.

Sequence similarities

Contains 1 reverse transcriptase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 599599Group II intron-encoded protein ltrA
PRO_0000084513

Regions

Domain70 – 361292Reverse transcriptase
Region381 – 549169Intron maturase type-2

Sequences

Sequence LengthMass (Da)Tools
P0A3U1 [UniParc].

Last modified March 15, 2005. Version 1.
Checksum: 52A286BD5F504589

FASTA59970,163
        10         20         30         40         50         60 
MKPTMAILER ISKNSQENID EVFTRLYRYL LRPDIYYVAY QNLYSNKGAS TKGILDDTAD 

        70         80         90        100        110        120 
GFSEEKIKKI IQSLKDGTYY PQPVRRMYIA KKNSKKMRPL GIPTFTDKLI QEAVRIILES 

       130        140        150        160        170        180 
IYEPVFEDVS HGFRPQRSCH TALKTIKREF GGARWFVEGD IKGCFDNIDH VTLIGLINLK 

       190        200        210        220        230        240 
IKDMKMSQLI YKFLKAGYLE NWQYHKTYSG TPQGGILSPL LANIYLHELD KFVLQLKMKF 

       250        260        270        280        290        300 
DRESPERITP EYRELHNEIK RISHRLKKLE GEEKAKVLLE YQEKRKRLPT LPCTSQTNKV 

       310        320        330        340        350        360 
LKYVRYADDF IISVKGSKED CQWIKEQLKL FIHNKLKMEL SEEKTLITHS SQPARFLGYD 

       370        380        390        400        410        420 
IRVRRSGTIK RSGKVKKRTL NGSVELLIPL QDKIRQFIFD KKIAIQKKDS SWFPVHRKYL 

       430        440        450        460        470        480 
IRSTDLEIIT IYNSELRGIC NYYGLASNFN QLNYFAYLME YSCLKTIASK HKGTLSKTIS 

       490        500        510        520        530        540 
MFKDGSGSWG IPYEIKQGKQ RRYFANFSEC KSPYQFTDEI SQAPVLYGYA RNTLENRLKA 

       550        560        570        580        590 
KCCELCGTSD ENTSYEIHHV NKVKNLKGKE KWEMAMIAKQ RKTLVVCFHC HRHVIHKHK 

« Hide

References

« Hide 'large scale' references
[1]"Splicing of a group II intron in a functional transfer gene of Lactococcus lactis."
Shearman C., Godon J.-J., Gasson M.
Mol. Microbiol. 21:45-53(1996) [PubMed: 8843433] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The complete genome sequence of the lactic acid bacterial paradigm Lactococcus lactis subsp. cremoris MG1363."
Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C., Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P., van Sinderen D., Kok J.
J. Bacteriol. 189:3256-3270(2007) [PubMed: 17307855] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MG1363.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X89922 Genomic DNA. Translation: CAA61996.1.
AM406671 Genomic DNA. Translation: CAL97959.1.
PIRS77648.
RefSeqYP_001032672.1. NC_009004.1.

3D structure databases

ModBaseSearch...

Protein family/group databases

REBASE3057. I-LlaI.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4797413.
GenomeReviewsGene locus llmg_1371 in contig AM406671_GR.
KEGGllm:llmg_1371.
PATRIC22283919. VBILacLac4574_1415.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG3344.
HOGENOMHBG343449.
OMAYLMEYSC.
ProtClustDBCLSK862318.

Family and domain databases

InterProIPR003615. HNH_nuc.
IPR000477. RVT.
[Graphical view]
PfamPF00078. RVT_1. 1 hit.
[Graphical view]
SMARTSM00507. HNHc. 1 hit.
[Graphical view]
PROSITEPS50878. RT_POL. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLTRA_LACLM
AccessionPrimary (citable) accession number: P0A3U1
Secondary accession number(s): A2RKZ3, Q57005, Q9FB65
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: March 15, 2005
Last modified: January 25, 2012
This is version 33 of the entry and version 1 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