ID   E10_VACCW               Reviewed;          95 AA.
AC   P23373; Q76ZV5;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   23-FEB-2022, entry version 78.
DE   RecName: Full=Probable FAD-linked sulfhydryl oxidase E10;
DE            EC=1.8.3.2;
GN   OrderedLocusNames=VACWR066; ORFNames=E10R;
OS   Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain
OS   WR)).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX   NCBI_TaxID=10254;
OH   NCBI_TaxID=9913; Bos taurus (Bovine).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2398897; DOI=10.1128/mcb.10.10.5433-5441.1990;
RA   Ahn B.-Y., Gershon P.D., Jones E.V., Moss B.;
RT   "Identification of rpo30, a vaccinia virus RNA polymerase gene with
RT   structural similarity to a eucaryotic transcription elongation factor.";
RL   Mol. Cell. Biol. 10:5433-5441(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Esposito J.J., Frace A.M., Sammons S.A., Olsen-Rasmussen M., Osborne J.,
RA   Wohlhueter R.;
RT   "Sequencing of the coding region of Vaccinia-WR to an average 9-fold
RT   redundancy and an error rate of 0.16/10kb.";
RL   Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   SUBCELLULAR LOCATION, AND INDUCTION.
RX   PubMed=11112499; DOI=10.1006/viro.2000.0656;
RA   Senkevich T.G., Weisberg A.S., Moss B.;
RT   "Vaccinia virus E10R protein is associated with the membranes of
RT   intracellular mature virions and has a role in morphogenesis.";
RL   Virology 278:244-252(2000).
RN   [4]
RP   FUNCTION, AND INTERACTION WITH A2.5.
RX   PubMed=11983854; DOI=10.1073/pnas.062163799;
RA   Senkevich T.G., White C.L., Koonin E.V., Moss B.;
RT   "Complete pathway for protein disulfide bond formation encoded by
RT   poxviruses.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:6667-6672(2002).
CC   -!- FUNCTION: FAD-dependent sulfhydryl oxidase that catalyzes disulfide
CC       bond formation. The complete pathway for formation of disulfide bonds
CC       in intracellular virion membrane proteins sequentially involves thiol-
CC       disulfide transfer between E10, A2.5 and G4. {ECO:0000255|PROSITE-
CC       ProRule:PRU00654, ECO:0000269|PubMed:11983854}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=O2 + 2 R'C(R)SH = H2O2 + R'C(R)S-S(R)CR';
CC         Xref=Rhea:RHEA:17357, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:16520, ChEBI:CHEBI:17412; EC=1.8.3.2;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00654};
CC   -!- SUBUNIT: Interacts with A2.5; this interaction involves formation of a
CC       transient disulfide-bonded intermediate, allowing disulfide bond
CC       transfer. {ECO:0000269|PubMed:11983854}.
CC   -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000305|PubMed:11112499}.
CC       Note=Associated with crescent membranes, immature virions (IV) and
CC       mature virions (MV). {ECO:0000305}.
CC   -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC       {ECO:0000269|PubMed:11112499}.
CC   -!- SIMILARITY: Belongs to the poxviridae E10 family. {ECO:0000305}.
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DR   EMBL; M36339; AAB59830.1; -; Genomic_DNA.
DR   EMBL; AY243312; AAO89345.1; -; Genomic_DNA.
DR   PIR; T30803; T30803.
DR   RefSeq; YP_232948.1; NC_006998.1.
DR   SMR; P23373; -.
DR   DNASU; 3707599; -.
DR   GeneID; 3707599; -.
DR   KEGG; vg:3707599; -.
DR   Proteomes; UP000000344; Genome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
DR   GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016972; F:thiol oxidase activity; IEA:UniProtKB-EC.
DR   Gene3D; 1.20.120.310; -; 1.
DR   InterPro; IPR036774; ERV/ALR_sulphydryl_oxid_sf.
DR   InterPro; IPR017905; ERV/ALR_sulphydryl_oxidase.
DR   InterPro; IPR006890; Sulphydryl_Oase_FAD-link_ERV1.
DR   Pfam; PF04805; Pox_E10; 1.
DR   PIRSF; PIRSF015696; VAC_E10R; 1.
DR   SUPFAM; SSF69000; SSF69000; 1.
DR   PROSITE; PS51324; ERV_ALR; 1.
PE   1: Evidence at protein level;
KW   Disulfide bond; FAD; Flavoprotein; Late protein; Membrane; Oxidoreductase;
KW   Redox-active center; Reference proteome; Transmembrane;
KW   Transmembrane helix; Viral envelope protein; Virion.
FT   CHAIN           1..95
FT                   /note="Probable FAD-linked sulfhydryl oxidase E10"
FT                   /id="PRO_0000099465"
FT   TOPO_DOM        1..8
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        9..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        26..95
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          1..95
FT                   /note="ERV/ALR sulfhydryl oxidase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00654"
FT   DISULFID        43..46
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00654"
SQ   SEQUENCE   95 AA;  10851 MW;  F4A2FAB4159DFA50 CRC64;
     MNPKHWGRAV WTIIFIVLSQ AGLDGNIEAC KRKLYTIVST LPCPACRRHA TIAIEDNNVM
     SSDDLNYIYY FFIRLFNNLA SDPKYAIDVT KVNPL