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P33379 (ACTA_LISMO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 83. Feed History...

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

Names and origin

Protein namesRecommended name:
Actin assembly-inducing protein
Gene names
Name:actA
Synonyms:prtB
Ordered Locus Names:lmo0204
OrganismListeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e) [Reference proteome] [HAMAP]
Taxonomic identifier169963 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesListeriaceaeListeria

Protein attributes

Sequence length639 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Virulence factor required for host cell microfilament interaction. It induces actin assembly around the bacteria to allow it to move within the cytoplasm. It is involved in the actin polymerization process. It seems to act as a nucleator that induces the reorganization of the actin cytoskeleton.

Subcellular location

Cell membrane; Single-pass membrane protein.

Ontologies

Keywords
   Biological processVirulence
   Cellular componentCell membrane
Membrane
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processpathogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentintegral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2929 Ref.3
Chain30 – 639610Actin assembly-inducing protein
PRO_0000020625

Regions

Transmembrane613 – 63321Helical; Potential
Repeat264 – 298351
Repeat299 – 333352
Repeat334 – 378453; approximate
Repeat379 – 417394; approximate
Repeat418 – 42255; truncated
Region264 – 333705 X approximate tandem repeats, Pro-rich
Motif360 – 3623Cell attachment site Potential
Compositional bias266 – 33974Pro-rich

Experimental info

Sequence conflict465 – 4662AP → DR in CAA42407. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P33379 [UniParc].

Last modified February 1, 1994. Version 1.
Checksum: 5A06CF78BC5F3C91

FASTA63970,349
        10         20         30         40         50         60 
MGLNRFMRAM MVVFITANCI TINPDIIFAA TDSEDSSLNT DEWEEEKTEE QPSEVNTGPR 

        70         80         90        100        110        120 
YETAREVSSR DIKELEKSNK VRNTNKADLI AMLKEKAEKG PNINNNNSEQ TENAAINEEA 

       130        140        150        160        170        180 
SGADRPAIQV ERRHPGLPSD SAAEIKKRRK AIASSDSELE SLTYPDKPTK VNKKKVAKES 

       190        200        210        220        230        240 
VADASESDLD SSMQSADESS PQPLKANQQP FFPKVFKKIK DAGKWVRDKI DENPEVKKAI 

       250        260        270        280        290        300 
VDKSAGLIDQ LLTKKKSEEV NASDFPPPPT DEELRLALPE TPMLLGFNAP ATSEPSSFEF 

       310        320        330        340        350        360 
PPPPTDEELR LALPETPMLL GFNAPATSEP SSFEFPPPPT EDELEIIRET ASSLDSSFTR 

       370        380        390        400        410        420 
GDLASLRNAI NRHSQNFSDF PPIPTEEELN GRGGRPTSEE FSSLNSGDFT DDENSETTEE 

       430        440        450        460        470        480 
EIDRLADLRD RGTGKHSRNA GFLPLNPFAS SPVPSLSPKV SKISAPALIS DITKKTPFKN 

       490        500        510        520        530        540 
PSQPLNVFNK KTTTKTVTKK PTPVKTAPKL AELPATKPQE TVLRENKTPF IEKQAETNKQ 

       550        560        570        580        590        600 
SINMPSLPVI QKEATESDKE EMKPQTEEKM VEESESANNA NGKNRSAGIE EGKLIAKSAE 

       610        620        630 
DEKAKEEPGN HTTLILAMLA IGVFSLGAFI KIIQLRKNN 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of the lecithinase operon of Listeria monocytogenes and possible role of lecithinase in cell-to-cell spread."
Vazquez-Boland J.-A., Kocks C., Dramsi S., Ohayon H., Geoffroy C., Mengaud J., Cossart P.
Infect. Immun. 60:219-230(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: LO28 / Serovar 1/2c.
[2]"L. monocytogenes-induced actin assembly requires the actA gene product, a surface protein."
Kocks C., Gouin E., Tabouret M., Berche P., Ohayon H., Cossart P.
Cell 68:521-531(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"A novel bacterial virulence gene in Listeria monocytogenes required for host cell microfilament interaction with homology to the proline-rich region of vinculin."
Domann E., Wehland J., Rohde M., Pistor S., Hartl M., Goebel W., Leimeister-Waechter M., Wuensher M., Chakraborty T.
EMBO J. 11:1981-1990(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 30-59.
Strain: EGD / Serovar 1/2a.
[4]"Comparative genomics of Listeria species."
Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F., Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A., Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E., Dominguez-Bernal G., Duchaud E. expand/collapse author list , Durant L., Dussurget O., Entian K.-D., Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W., Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U., Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A., Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B., Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N., Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.
Science 294:849-852(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-679 / EGD-e.
[5]"The ActA protein of Listeria monocytogenes acts as a nucleator inducing reorganization of the actin cytoskeleton."
Pistor S., Chakraborty T., Niebuhr K., Domann E., Wehland J.
EMBO J. 13:758-763(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M82881 Genomic DNA. Translation: AAA25269.1.
X59723 Genomic DNA. Translation: CAA42407.1.
AL591974 Genomic DNA. Translation: CAD00731.1.
PIRAE1100.
S20887.
RefSeqNP_463735.1. NC_003210.1.

3D structure databases

ProteinModelPortalP33379.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING169963.lmo0204.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAD00731; CAD00731; CAD00731.
GeneID987035.
KEGGlmo:lmo0204.
PATRIC20309415. VBILisMon69206_0209.

Organism-specific databases

GenoListLMO0204.

Phylogenomic databases

HOGENOMHOG000033794.
KOK16644.
OMASFEFPPP.
OrthoDBEOG6VMTG2.

Enzyme and pathway databases

BioCycLMON169963:LMO0204-MONOMER.

Family and domain databases

InterProIPR007752. Virulence_actor_ActA.
[Graphical view]
PfamPF05058. ActA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameACTA_LISMO
AccessionPrimary (citable) accession number: P33379
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: May 14, 2014
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program