PRFA_LISMO
ID PRFA_LISMO Reviewed; 237 AA.
AC P22262;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Listeriolysin regulatory protein;
GN Name=prfA; OrderedLocusNames=lmo0200;
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=1662763; DOI=10.1111/j.1365-2958.1991.tb02158.x;
RA Mengaud J., Dramsi S., Gouin E., Vazquez-Boland J.A., Milon G., Cossart P.;
RT "Pleiotropic control of Listeria monocytogenes virulence factors by a gene
RT that is autoregulated.";
RL Mol. Microbiol. 5:2273-2283(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=EGD / Serovar 1/2a;
RX PubMed=2122460; DOI=10.1073/pnas.87.21.8336;
RA Leimeister-Waechter M., Haffner C., Domann E., Goebel W., Chakraborty T.;
RT "Identification of a gene that positively regulates expression of
RT listeriolysin, the major virulence factor of listeria monocytogenes.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:8336-8340(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=P14 / Serovar 4B;
RX PubMed=9045810; DOI=10.1128/jb.179.5.1533-1540.1997;
RA Ripio M.T., Dominguez-Bernal G., Lara M., Suarez M., Vazquez-Boland J.A.;
RT "A Gly145Ser substitution in the transcriptional activator PrfA causes
RT constitutive overexpression of virulence factors in Listeria
RT monocytogenes.";
RL J. Bacteriol. 179:1533-1540(1997).
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).
CC -!- FUNCTION: Positively regulates expression of listeriolysin, of 1-
CC phosphadidylinositol phosphodiesterase (PI-PLC) and other virulence
CC factors.
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DR EMBL; X61210; CAA43524.1; -; Genomic_DNA.
DR EMBL; M55160; AAA25291.1; -; Genomic_DNA.
DR EMBL; AJ002742; CAA05714.1; -; Genomic_DNA.
DR EMBL; AL591974; CAD00727.1; -; Genomic_DNA.
DR PIR; AI1099; AI1099.
DR PIR; S16890; S16890.
DR RefSeq; NP_463731.1; NC_003210.1.
DR RefSeq; WP_003722729.1; NZ_CP023861.1.
DR PDB; 1OMI; X-ray; 2.80 A; A/B=7-237.
DR PDB; 2BEO; X-ray; 2.70 A; A/B=2-237.
DR PDB; 2BGC; X-ray; 2.30 A; A/B/D/E/F/G/H/I=2-237.
DR PDB; 5F1R; X-ray; 2.25 A; A/B=1-237.
DR PDB; 5LEJ; X-ray; 2.70 A; A/B=1-237.
DR PDB; 5LEK; X-ray; 2.80 A; A/B=1-237.
DR PDB; 5LRR; X-ray; 2.17 A; A/B/C/D/E/F/G/H=1-237.
DR PDB; 5LRS; X-ray; 2.90 A; A/B=1-237.
DR PDB; 5X6D; X-ray; 2.94 A; A/B/G/H/M/N=1-237.
DR PDB; 5X6E; X-ray; 2.99 A; A/B/E/F/M/N=1-237.
DR PDB; 6EUT; X-ray; 1.90 A; A/B=1-237.
DR PDB; 6EUU; X-ray; 2.60 A; A/B=1-237.
DR PDB; 6EUZ; X-ray; 1.95 A; A/B=1-237.
DR PDB; 6EV0; X-ray; 2.30 A; A/B=1-237.
DR PDB; 6EXK; X-ray; 2.10 A; A/B=1-237.
DR PDB; 6EXL; X-ray; 1.90 A; A/B=1-237.
DR PDB; 6EXM; X-ray; 1.60 A; A/B=1-237.
DR PDB; 6HCK; X-ray; 2.70 A; A/B=1-237.
DR PDB; 6QVY; X-ray; 1.69 A; A/B=1-237.
DR PDB; 6QVZ; X-ray; 2.71 A; A/B=1-237.
DR PDB; 6QW1; X-ray; 1.84 A; A/B=1-237.
DR PDB; 6QW2; X-ray; 2.60 A; A/B=1-237.
DR PDB; 6QWF; X-ray; 2.70 A; A/B=1-237.
DR PDB; 6QWH; X-ray; 2.90 A; A/B=1-237.
DR PDB; 6QWK; X-ray; 2.90 A; A/B=1-237.
DR PDB; 6QWM; X-ray; 2.90 A; A/B=1-237.
DR PDBsum; 1OMI; -.
DR PDBsum; 2BEO; -.
DR PDBsum; 2BGC; -.
DR PDBsum; 5F1R; -.
DR PDBsum; 5LEJ; -.
DR PDBsum; 5LEK; -.
DR PDBsum; 5LRR; -.
DR PDBsum; 5LRS; -.
DR PDBsum; 5X6D; -.
DR PDBsum; 5X6E; -.
DR PDBsum; 6EUT; -.
DR PDBsum; 6EUU; -.
DR PDBsum; 6EUZ; -.
DR PDBsum; 6EV0; -.
DR PDBsum; 6EXK; -.
DR PDBsum; 6EXL; -.
DR PDBsum; 6EXM; -.
DR PDBsum; 6HCK; -.
DR PDBsum; 6QVY; -.
DR PDBsum; 6QVZ; -.
DR PDBsum; 6QW1; -.
DR PDBsum; 6QW2; -.
DR PDBsum; 6QWF; -.
DR PDBsum; 6QWH; -.
DR PDBsum; 6QWK; -.
DR PDBsum; 6QWM; -.
DR AlphaFoldDB; P22262; -.
DR SMR; P22262; -.
DR STRING; 169963.lmo0200; -.
DR BindingDB; P22262; -.
DR ChEMBL; CHEMBL4295575; -.
DR DrugBank; DB04447; 1,4-Dithiothreitol.
DR DrugBank; DB01692; Dithioerythritol.
DR DrugBank; DB03654; S,S-Propylthiocysteine.
DR PaxDb; P22262; -.
DR EnsemblBacteria; CAD00727; CAD00727; CAD00727.
DR GeneID; 987031; -.
DR KEGG; lmo:lmo0200; -.
DR PATRIC; fig|169963.11.peg.205; -.
DR eggNOG; COG0664; Bacteria.
DR HOGENOM; CLU_1173961_0_0_9; -.
DR OMA; AIAREDC; -.
DR PhylomeDB; P22262; -.
DR BioCyc; LMON169963:LMO0200-MON; -.
DR EvolutionaryTrace; P22262; -.
DR PHI-base; PHI:7470; -.
DR PHI-base; PHI:7898; -.
DR Proteomes; UP000000817; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 2.60.120.10; -; 1.
DR InterPro; IPR018490; cNMP-bd-like.
DR InterPro; IPR012318; HTH_CRP.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR018335; Tscrpt_reg_HTH_Crp-type_CS.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF13545; HTH_Crp_2; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF51206; SSF51206; 1.
DR PROSITE; PS00042; HTH_CRP_1; 1.
DR PROSITE; PS51063; HTH_CRP_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; DNA-binding; Reference proteome; Transcription;
KW Transcription regulation; Virulence.
FT CHAIN 1..237
FT /note="Listeriolysin regulatory protein"
FT /id="PRO_0000100188"
FT DOMAIN 137..212
FT /note="HTH crp-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00387"
FT VARIANT 145
FT /note="G -> S (in prfA* mutant which constitutively
FT overexpresses virulence genes. Presumably blocks prfA in a
FT cofactor-independent transcriptionally active
FT conformation)"
FT CONFLICT 234..236
FT /note="GKL -> E (in Ref. 2)"
FT /evidence="ECO:0000305"
FT HELIX 3..14
FT /evidence="ECO:0007829|PDB:6EXM"
FT STRAND 20..23
FT /evidence="ECO:0007829|PDB:6EXM"
FT STRAND 27..29
FT /evidence="ECO:0007829|PDB:6EXM"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:5LEJ"
FT STRAND 37..51
FT /evidence="ECO:0007829|PDB:6EXM"
FT TURN 53..55
FT /evidence="ECO:0007829|PDB:6EXK"
FT STRAND 57..72
FT /evidence="ECO:0007829|PDB:6EXM"
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:6EXM"
FT STRAND 79..82
FT /evidence="ECO:0007829|PDB:6EXM"
FT STRAND 84..87
FT /evidence="ECO:0007829|PDB:6EXM"
FT STRAND 89..98
FT /evidence="ECO:0007829|PDB:6EXM"
FT HELIX 99..106
FT /evidence="ECO:0007829|PDB:6EXM"
FT HELIX 110..154
FT /evidence="ECO:0007829|PDB:6EXM"
FT STRAND 155..158
FT /evidence="ECO:0007829|PDB:6EXM"
FT STRAND 161..164
FT /evidence="ECO:0007829|PDB:6EXM"
FT HELIX 168..175
FT /evidence="ECO:0007829|PDB:6EXM"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:6EXM"
FT HELIX 184..195
FT /evidence="ECO:0007829|PDB:6EXM"
FT STRAND 198..202
FT /evidence="ECO:0007829|PDB:6EXM"
FT STRAND 205..208
FT /evidence="ECO:0007829|PDB:6EXM"
FT HELIX 211..217
FT /evidence="ECO:0007829|PDB:6EXM"
FT HELIX 219..228
FT /evidence="ECO:0007829|PDB:6EXM"
FT HELIX 230..235
FT /evidence="ECO:0007829|PDB:6EXM"
SQ SEQUENCE 237 AA; 27301 MW; 697542B135158CFB CRC64;
MNAQAEEFKK YLETNGIKPK QFHKKELIFN QWDPQEYCIF LYDGITKLTS ISENGTIMNL
QYYKGAFVIM SGFIDTETSV GYYNLEVISE QATAYVIKIN ELKELLSKNL THFFYVFQTL
QKQVSYSLAK FNDFSINGKL GSICGQLLIL TYVYGKETPD GIKITLDNLT MQELGYSSGI
AHSSAVSRII SKLKQEKVIV YKNSCFYVQN LDYLKRYAPK LDEWFYLACP ATWGKLN
