ID   EDIN_STAAU              Reviewed;         247 AA.
AC   P24121;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Epidermal cell differentiation inhibitor;
DE            Short=EDIN;
DE            EC=2.4.2.-;
DE   Flags: Precursor;
OS   Staphylococcus aureus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 36-58.
RC   STRAIN=E-1;
RX   PubMed=1993048; DOI=10.1016/0006-291x(91)91438-i;
RA   Inoue S., Sugai M., Murooka Y., Paik S.-Y., Hong Y.-M., Ohgai H.,
RA   Suginaka H.;
RT   "Molecular cloning and sequencing of the epidermal cell differentiation
RT   inhibitor gene from Staphylococcus aureus.";
RL   Biochem. Biophys. Res. Commun. 174:459-464(1991).
RN   [2]
RP   PROTEIN SEQUENCE OF 36-44.
RX   PubMed=2256941; DOI=10.1016/s0006-291x(05)81026-5;
RA   Sugai M., Enomoto T., Hashimoto K., Matsumoto K., Matsuo Y., Ohgai H.,
RA   Hong Y.M., Inoue S., Yoshikawa K., Suginaka H.;
RT   "A novel epidermal cell differentiation inhibitor (EDIN): purification and
RT   characterization from Staphylococcus aureus.";
RL   Biochem. Biophys. Res. Commun. 173:92-98(1990).
CC   -!- FUNCTION: Inhibits terminal differentiation of cultured mouse
CC       keratinocytes. In culture, inhibits also the differentiation of human
CC       keratinocytes. Probable ADP-ribosyltransferase.
CC   -!- SIMILARITY: To ADP-ribosyltransferase C3 of Clostridium. {ECO:0000305}.
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DR   EMBL; M63917; AAA26616.1; -; Genomic_DNA.
DR   PIR; JG0016; JG0016.
DR   RefSeq; WP_012211137.1; NZ_VCGL01000008.1.
DR   RefSeq; YP_001573884.1; NC_010077.1.
DR   RefSeq; YP_006937916.1; NC_013326.1.
DR   RefSeq; YP_006938649.1; NC_013348.1.
DR   RefSeq; YP_006939339.1; NC_018952.1.
DR   AlphaFoldDB; P24121; -.
DR   SMR; P24121; -.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0016763; F:pentosyltransferase activity; IEA:InterPro.
DR   GO; GO:0006471; P:protein ADP-ribosylation; IEA:InterPro.
DR   InterPro; IPR003540; ADP-ribosyltransferase.
DR   InterPro; IPR016678; Mono-ADP_RibTrfase_C3/Edin.
DR   Pfam; PF03496; ADPrib_exo_Tox; 1.
DR   PIRSF; PIRSF016951; MADP_ribosyltransf_Edin; 1.
DR   PROSITE; PS51996; TR_MART; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycosyltransferase; NAD; Signal; Transferase.
FT   SIGNAL          1..35
FT                   /evidence="ECO:0000269|PubMed:1993048,
FT                   ECO:0000269|PubMed:2256941"
FT   CHAIN           36..247
FT                   /note="Epidermal cell differentiation inhibitor"
FT                   /id="PRO_0000021149"
FT   DOMAIN          39..247
FT                   /note="TR mART core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT   ACT_SITE        120
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT   ACT_SITE        173
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT   ACT_SITE        215
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
SQ   SEQUENCE   247 AA;  27680 MW;  00AAD8BD4E4F0C9D CRC64;
     MKNKLLFKIF LSLSLALSVY SINDKIIEVS NTSLAADVKN FTDLDEATKW GNKLIKQAKY
     SSDDKIALYE YTKDSSKING PLRLAGGDIN KLDSTTQDKV RRLDSSISKS TTPESVYVYR
     LLNLDYLTSI VGFTNEDLYK LQQTNNGQYD ENLVRKLNNV MNSRIYREDG YSSTQLVSGA
     AVGGRPIELR LELPKGTKAA YLNSKDLTAY YGQQEVLLPR GTEYAVGSVE LSNDKKKIII
     TAIVFKK