ID   ESSD_STAAE              Reviewed;         617 AA.
AC   A0A0H3KDT7;
DT   05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT   16-SEP-2015, sequence version 1.
DT   25-MAY-2022, entry version 19.
DE   RecName: Full=Type VII secretion systems protein EssD {ECO:0000305};
DE   AltName: Full=Ess-associated gene D {ECO:0000303|PubMed:21278286};
DE   AltName: Full=Nuclease toxin EssD;
GN   Name=essD {ECO:0000303|PubMed:21278286}; Synonyms=esaD;
GN   OrderedLocusNames=NWMN_0228 {ECO:0000312|EMBL:BAF66500.1};
OS   Staphylococcus aureus (strain Newman).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=426430;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Newman;
RX   PubMed=17951380; DOI=10.1128/jb.01000-07;
RA   Baba T., Bae T., Schneewind O., Takeuchi F., Hiramatsu K.;
RT   "Genome sequence of Staphylococcus aureus strain Newman and comparative
RT   analysis of staphylococcal genomes: polymorphism and evolution of two major
RT   pathogenicity islands.";
RL   J. Bacteriol. 190:300-310(2008).
RN   [2]
RP   FUNCTION IN VIRULENCE, SUBCELLULAR LOCATION, INDUCTION, AND DISRUPTION
RP   PHENOTYPE.
RC   STRAIN=Newman;
RX   PubMed=21278286; DOI=10.1128/jb.01096-10;
RA   Anderson M., Chen Y.H., Butler E.K., Missiakas D.M.;
RT   "EsaD, a secretion factor for the Ess pathway in Staphylococcus aureus.";
RL   J. Bacteriol. 193:1583-1589(2011).
CC   -!- FUNCTION: Component of the type VII secretion system (Ess) (Probable).
CC       Plays a role in Ess secretion during infection. Required for the
CC       efficient secretion of EsxA. Required for abscess formation and
CC       staphylococcal persistence in host tissue (PubMed:21278286). Possesses
CC       a toxic DNase activity that is modulated by EssG by forming a nuclease
CC       toxin-antitoxin pair. This nuclease toxin targets competitor bacteria
CC       (By similarity). {ECO:0000250|UniProtKB:Q2G179,
CC       ECO:0000269|PubMed:21278286}.
CC   -!- SUBUNIT: Interacts (via C-terminal) with EssG; this interaction blocks
CC       EssD activity. Interacts with EssE. {ECO:0000250|UniProtKB:Q2G179}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q2G179}. Cell
CC       membrane {ECO:0000269|PubMed:21278286}. Note=Released from the cell in
CC       a form that is immediately active while EssG partner protein remains in
CC       the producing cell where it may potentially serve further protective
CC       functions. {ECO:0000250|UniProtKB:Q2G179}.
CC   -!- INDUCTION: Expression is activated by mutations in esaB and essB
CC       (newman). {ECO:0000269|PubMed:21278286}.
CC   -!- DISRUPTION PHENOTYPE: Deletions mutants generate fewer abscesses with a
CC       reduced bacterial load compared to wild-type strain.
CC       {ECO:0000269|PubMed:21278286}.
CC   -!- SIMILARITY: Belongs to the EssD family. {ECO:0000305}.
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DR   EMBL; AP009351; BAF66500.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0H3KDT7; -.
DR   EnsemblBacteria; BAF66500; BAF66500; NWMN_0228.
DR   KEGG; sae:NWMN_0228; -.
DR   HOGENOM; CLU_031044_1_0_9; -.
DR   OMA; NNYAQKT; -.
DR   Proteomes; UP000006386; 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; Secreted; Virulence.
FT   CHAIN           1..617
FT                   /note="Type VII secretion systems protein EssD"
FT                   /id="PRO_0000437418"
FT   REGION          420..448
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        428..442
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   617 AA;  68702 MW;  37F11566B7186FE1 CRC64;
     MHDMTKDIEY LTADYDNEKS SIQSVIDAIE GQDFLDVDTT MDDAVSDVSS LDEDGAISLT
     SSVVGPQGSK LMGYYQNELY DYASQLDSKM KEIIDTPFIE DIDKAFKGIT NVKLENILIK
     NGGGHGRDTY GASGKIAKGD AKKSDSDVYS IDEILKSDQE FVKVIDQHYK EMKKEDKKLS
     KSDFEKMMTQ GASCDYMTVA EAEELEEQKK KEEAIEIAAL AGMVVLSCIN PVAGAVAIGA
     YSAYSAANAA TGKNIVTGRK LSKEERIMEG LSLIPLPGMG FLKGAGKSLM KLGFKGGEKF
     AVKTGLQKTM QQAVSRISPK MGMMKNSVLN QSRNFAQNTH VGQMLSNMRG QATHTVQQSR
     NWIGQQAQNV KRIVNNGLDK EIAHPFKQQL APAGMGGIKF AETTTLRNMG QNIKRAVTPQ
     NHVTHGPKDS MVRSEGKHSI SSHEMNSSKY VESPNYTKVE FGEHYARLRP KKLKANIEYT
     TPTGHIYRTD HKGRIKEVYV DNLSLKDGDR NSHAQRTVGG EDRLPDDDGG HLIARMFGGS
     KDIDNLVAQS KFINRPFKEK GHWYNLEKEW QEFLNSGKEV KNIKMEVKYS GNSQRPTIFK
     VEYEINGERN IRRILNK