位置:首页 > 蛋白库 > ESSD_STAA8
ESSD_STAA8
ID   ESSD_STAA8              Reviewed;         614 AA.
AC   Q2G179;
DT   16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=Type VII secretion system protein EssD;
DE   AltName: Full=Nuclease toxin EssD {ECO:0000303|PubMed:27723728};
GN   Name=essD; Synonyms=esaD {ECO:0000303|PubMed:27723728};
GN   OrderedLocusNames=SAOUHSC_00268;
OS   Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 8325 / PS 47;
RA   Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT   "The Staphylococcus aureus NCTC 8325 genome.";
RL   (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL   Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL   D.C. (2006).
RN   [2]
RP   FUNCTION, MUTAGENESIS OF HIS-528, SUBCELLULAR LOCATION, AND INTERACTION
RP   WITH ESSG AND ESSE.
RC   STRAIN=NCTC 8325 / PS 47;
RX   PubMed=27723728; DOI=10.1038/nmicrobiol.2016.183;
RA   Cao Z., Casabona M.G., Kneuper H., Chalmers J.D., Palmer T.;
RT   "The type VII secretion system of Staphylococcus aureus secretes a nuclease
RT   toxin that targets competitor bacteria.";
RL   Nat. Microbiol. 2:16183-16183(2016).
CC   -!- FUNCTION: Component of the type VII secretion system (Ess). Plays a
CC       role in Ess secretion during infection. Required for the efficient
CC       secretion of EsxA. Required for abscess formation and staphylococcal
CC       persistence in host tissues (By similarity). Possesses a toxic DNase
CC       activity that is modulated by EssG by forming a nuclease toxin-
CC       antitoxin pair. This nuclease toxin targets competitor bacteria
CC       (PubMed:27723728). {ECO:0000250|UniProtKB:A0A0H2XIV9,
CC       ECO:0000269|PubMed:27723728}.
CC   -!- SUBUNIT: Interacts (via C-terminal) with EssG; this interaction blocks
CC       EssD activity (PubMed:27723728). Interacts with EssE (PubMed:27723728).
CC       {ECO:0000269|PubMed:27723728}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:27723728}. Cell
CC       membrane {ECO:0000250|UniProtKB:A0A0H2XIV9}. Note=Released from the
CC       cell in a form that is immediately active while EsaG partner protein
CC       remains in the producing cell where it may potentially serve further
CC       protective functions. {ECO:0000269|PubMed:27723728}.
CC   -!- SIMILARITY: Belongs to the EssD family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000253; ABD29441.1; -; Genomic_DNA.
DR   RefSeq; WP_000159025.1; NZ_LS483365.1.
DR   RefSeq; YP_498861.1; NC_007795.1.
DR   AlphaFoldDB; Q2G179; -.
DR   EnsemblBacteria; ABD29441; ABD29441; SAOUHSC_00268.
DR   GeneID; 3919209; -.
DR   KEGG; sao:SAOUHSC_00268; -.
DR   PATRIC; fig|93061.5.peg.246; -.
DR   HOGENOM; CLU_031044_1_0_9; -.
DR   OMA; NNYAQKT; -.
DR   Proteomes; UP000008816; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   Gene3D; 3.40.570.10; -; 1.
DR   InterPro; IPR044929; DNA/RNA_non-sp_Endonuclease_sf.
DR   InterPro; IPR044927; Endonuclea_NS_2.
DR   InterPro; IPR027797; PT-TG_dom.
DR   Pfam; PF13930; Endonuclea_NS_2; 1.
DR   Pfam; PF14449; PT-TG; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Membrane; Reference proteome; Secreted; Virulence.
FT   CHAIN           1..614
FT                   /note="Type VII secretion system protein EssD"
FT                   /id="PRO_0000448084"
FT   REGION          417..445
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        425..439
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        528
FT                   /evidence="ECO:0000305|PubMed:27723728"
FT   MUTAGEN         528
FT                   /note="H->A: Partial loss of DNase activity."
FT                   /evidence="ECO:0000269|PubMed:27723728"
SQ   SEQUENCE   614 AA;  68318 MW;  8C60D0FEEB1DC5AE CRC64;
     MTKDIEYLTA DYDNEKSSIQ SVIDAIEGQD FLDVDTTMDD AVSDVSSLDE DGAISLTSSV
     VGPQGSKLMG YYQNELYDYA SQLDSKMKEI IDTPFIEDID KAFKGITNVK LENILIKNGG
     GHGRDTYGAS GKIAKGDAKK SDSDVYSIDE ILKSDQEFVK VIDQHYKEMK KEDKKLSKSD
     FEKMMTQGAS CDYMTVAEAE ELEEQKKKEE AIEIAALAGM VVLSCINPVA GAVAIGAYSA
     YSAANAATGK NIVTGRKLSK EERIMEGLSL IPLPGMGFLK GAGKSLMKLG FKGGEKFAVK
     TGLQKTMQQA VSRISPKMGM MKNSVLNQSR NFAQNTHVGQ MLSNMRGQAT HTVQQSRNWI
     GQQAQNVKRI VNNGLDKEIA HPFKQQLAPA GMGGIKFAET TTLRNMGQNI KRAVTPQNHV
     THGPKDSMVR SEGKHSISSH EMNSSKYVES PNYTKVEFGE HYARLRPKKL KANIEYTTPT
     GHIYRTDHKG RIKEVYVDNL SLKDGDRNSH AQRTVGGEDR LPDDDGGHLI ARMFGGSKDI
     DNLVAQSKFI NRPFKEKGHW YNLEKEWQEF LNSGKEVKNI KMEVKYSGNS QRPTIFKVEY
     EINGERNIRR ILNK
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024