ID   CDUB2_CHLTS             Reviewed;         339 AA.
AC   D3UTF3;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   20-APR-2010, sequence version 1.
DT   03-AUG-2022, entry version 42.
DE   RecName: Full=Deubiquitinase and deneddylase Dub2;
DE            Short=ChlaDub2;
DE            EC=3.4.22.-;
GN   Name=cdu2; OrderedLocusNames=SW2_8831;
OS   Chlamydia trachomatis serovar E (strain Sweden2).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=634464;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sweden2;
RX   PubMed=20093289; DOI=10.1099/mic.0.036830-0;
RA   Unemo M., Seth-Smith H.M., Cutcliffe L.T., Skilton R.J., Barlow D.,
RA   Goulding D., Persson K., Harris S.R., Kelly A., Bjartling C., Fredlund H.,
RA   Olcen P., Thomson N.R., Clarke I.N.;
RT   "The Swedish new variant of Chlamydia trachomatis: Genome sequence,
RT   morphology, cell tropism and phenotypic characterization.";
RL   Microbiology 156:1394-1404(2010).
CC   -!- FUNCTION: Effector proteins function to alter host cell physiology and
CC       promote bacterial survival in host tissues. This protease possesses
CC       deubiquitinating and deneddylating activities (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Host cell {ECO:0000250}.
CC       Membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
CC       Note=Secreted, and delivered into the host cell. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase C48 family. {ECO:0000305}.
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DR   EMBL; FN652779; CBJ15396.1; -; Genomic_DNA.
DR   RefSeq; WP_009872257.1; NC_017441.1.
DR   AlphaFoldDB; D3UTF3; -.
DR   SMR; D3UTF3; -.
DR   KEGG; csw:SW2_8831; -.
DR   PATRIC; fig|634464.3.peg.963; -.
DR   HOGENOM; CLU_067510_0_0_0; -.
DR   OMA; ECICNCL; -.
DR   GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR   GO; GO:0043657; C:host cell; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; ISS:UniProtKB.
DR   GO; GO:0019784; F:deNEDDylase activity; ISS:UniProtKB.
DR   GO; GO:0000338; P:protein deneddylation; ISS:UniProtKB.
DR   GO; GO:0016579; P:protein deubiquitination; ISS:UniProtKB.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR003653; Peptidase_C48_C.
DR   Pfam; PF02902; Peptidase_C48; 1.
DR   SUPFAM; SSF54001; SSF54001; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Membrane; Protease; Secreted; Thiol protease; Transmembrane;
KW   Transmembrane helix; Ubl conjugation pathway; Virulence.
FT   CHAIN           1..339
FT                   /note="Deubiquitinase and deneddylase Dub2"
FT                   /id="PRO_0000396502"
FT   TRANSMEM        36..56
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        203
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        220
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        282
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   339 AA;  38411 MW;  CD15F0C33AA32188 CRC64;
     MEPIHNPPPQ TCSYSRPSTT YTSFKDASCG TKVTRIIIAL FLIVISCGLI LCAYTFRDLL
     DADYSAQEGP QQATKLLQQL DKVLTGPPLP IWDNEHLFQF SCLMQNKHRR VLPIDICNPL
     TKFNFLEYIC NCLMTKQSVN VNETDMCELF CPPTCTPENY RRLLCTSSVF PFVMWHDPSA
     DTQEAMLTKM DQTMSSGRVG NSHWVLVIVD IEHRCVTFFD SFYDYIASPQ QMREQLEGLA
     ASLGAIYPKE GGADSDQEEL LSPFQVRIGS TVKVQSPGEF TCGAWCCQFL AWYLENPDFD
     LEEKVPTNPS ERRALLADFI STTEQAMSRY SSLSWPTTD