ACTA_LISMO
ID ACTA_LISMO Reviewed; 639 AA.
AC P33379;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Actin assembly-inducing protein;
DE Flags: Precursor;
GN Name=actA; Synonyms=prtB; OrderedLocusNames=lmo0204;
OS Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=169963;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LO28 / Serovar 1/2c;
RX PubMed=1309513; DOI=10.1128/iai.60.1.219-230.1992;
RA Vazquez-Boland J.-A., Kocks C., Dramsi S., Ohayon H., Geoffroy C.,
RA Mengaud J., Cossart P.;
RT "Nucleotide sequence of the lecithinase operon of Listeria monocytogenes
RT and possible role of lecithinase in cell-to-cell spread.";
RL Infect. Immun. 60:219-230(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1739966; DOI=10.1016/0092-8674(92)90188-i;
RA Kocks C., Gouin E., Tabouret M., Berche P., Ohayon H., Cossart P.;
RT "L. monocytogenes-induced actin assembly requires the actA gene product, a
RT surface protein.";
RL Cell 68:521-531(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 30-59.
RC STRAIN=EGD / Serovar 1/2a;
RX PubMed=1582425; DOI=10.1002/j.1460-2075.1992.tb05252.x;
RA Domann E., Wehland J., Rohde M., Pistor S., Hartl M., Goebel W.,
RA Leimeister-Waechter M., Wuensher M., Chakraborty T.;
RT "A novel bacterial virulence gene in Listeria monocytogenes required for
RT host cell microfilament interaction with homology to the proline-rich
RT region of vinculin.";
RL EMBO J. 11:1981-1990(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).
RN [5]
RP CHARACTERIZATION.
RX PubMed=8112291; DOI=10.1002/j.1460-2075.1994.tb06318.x;
RA Pistor S., Chakraborty T., Niebuhr K., Domann E., Wehland J.;
RT "The ActA protein of Listeria monocytogenes acts as a nucleator inducing
RT reorganization of the actin cytoskeleton.";
RL EMBO J. 13:758-763(1994).
CC -!- FUNCTION: Virulence factor required for host cell microfilament
CC interaction. It induces actin assembly around the bacteria to allow it
CC to move within the cytoplasm. It is involved in the actin
CC polymerization process. It seems to act as a nucleator that induces the
CC reorganization of the actin cytoskeleton.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein.
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DR EMBL; M82881; AAA25269.1; -; Genomic_DNA.
DR EMBL; X59723; CAA42407.1; -; Genomic_DNA.
DR EMBL; AL591974; CAD00731.1; -; Genomic_DNA.
DR PIR; AE1100; AE1100.
DR PIR; S20887; S20887.
DR RefSeq; NP_463735.1; NC_003210.1.
DR RefSeq; WP_010989374.1; NZ_CP023861.1.
DR PDB; 5NC2; X-ray; 1.58 A; I/J=336-344.
DR PDB; 5NC7; X-ray; 2.70 A; I/J/K/L/W/X/Y/Z=335-344.
DR PDBsum; 5NC2; -.
DR PDBsum; 5NC7; -.
DR AlphaFoldDB; P33379; -.
DR SMR; P33379; -.
DR ELM; P33379; -.
DR STRING; 169963.lmo0204; -.
DR PaxDb; P33379; -.
DR PRIDE; P33379; -.
DR EnsemblBacteria; CAD00731; CAD00731; CAD00731.
DR GeneID; 987035; -.
DR KEGG; lmo:lmo0204; -.
DR PATRIC; fig|169963.11.peg.209; -.
DR eggNOG; ENOG503083A; Bacteria.
DR HOGENOM; CLU_451854_0_0_9; -.
DR OMA; KEEPGNH; -.
DR BioCyc; LMON169963:LMO0204-MON; -.
DR Proteomes; UP000000817; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR InterPro; IPR007752; Virulence_actor_ActA.
DR Pfam; PF05058; ActA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Direct protein sequencing; Membrane;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix;
KW Virulence.
FT SIGNAL 1..29
FT /evidence="ECO:0000269|PubMed:1582425"
FT CHAIN 30..639
FT /note="Actin assembly-inducing protein"
FT /id="PRO_0000020625"
FT TRANSMEM 613..633
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 264..298
FT /note="1"
FT REPEAT 299..333
FT /note="2"
FT REPEAT 334..378
FT /note="3; approximate"
FT REPEAT 379..417
FT /note="4; approximate"
FT REPEAT 418..422
FT /note="5; truncated"
FT REGION 36..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 132..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 264..333
FT /note="5 X approximate tandem repeats, Pro-rich"
FT REGION 285..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 320..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 372..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 474..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 360..362
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT COMPBIAS 132..155
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..185
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..411
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..436
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..501
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 533..550
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 553..574
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..609
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 465..466
FT /note="AP -> DR (in Ref. 3; CAA42407)"
FT /evidence="ECO:0000305"
FT TURN 341..343
FT /evidence="ECO:0007829|PDB:5NC7"
SQ SEQUENCE 639 AA; 70349 MW; 5A06CF78BC5F3C91 CRC64;
MGLNRFMRAM MVVFITANCI TINPDIIFAA TDSEDSSLNT DEWEEEKTEE QPSEVNTGPR
YETAREVSSR DIKELEKSNK VRNTNKADLI AMLKEKAEKG PNINNNNSEQ TENAAINEEA
SGADRPAIQV ERRHPGLPSD SAAEIKKRRK AIASSDSELE SLTYPDKPTK VNKKKVAKES
VADASESDLD SSMQSADESS PQPLKANQQP FFPKVFKKIK DAGKWVRDKI DENPEVKKAI
VDKSAGLIDQ LLTKKKSEEV NASDFPPPPT DEELRLALPE TPMLLGFNAP ATSEPSSFEF
PPPPTDEELR LALPETPMLL GFNAPATSEP SSFEFPPPPT EDELEIIRET ASSLDSSFTR
GDLASLRNAI NRHSQNFSDF PPIPTEEELN GRGGRPTSEE FSSLNSGDFT DDENSETTEE
EIDRLADLRD RGTGKHSRNA GFLPLNPFAS SPVPSLSPKV SKISAPALIS DITKKTPFKN
PSQPLNVFNK KTTTKTVTKK PTPVKTAPKL AELPATKPQE TVLRENKTPF IEKQAETNKQ
SINMPSLPVI QKEATESDKE EMKPQTEEKM VEESESANNA NGKNRSAGIE EGKLIAKSAE
DEKAKEEPGN HTTLILAMLA IGVFSLGAFI KIIQLRKNN
