ID   CDUB2_CHLTB             Reviewed;         339 AA.
AC   B0BAX8;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=Deubiquitinase and deneddylase Dub2;
DE            Short=ChlaDub2;
DE            EC=3.4.22.-;
GN   Name=cdu2; OrderedLocusNames=CTLon_0242;
OS   Chlamydia trachomatis serovar L2b (strain UCH-1/proctitis).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=471473;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCH-1/proctitis;
RX   PubMed=18032721; DOI=10.1101/gr.7020108;
RA   Thomson N.R., Holden M.T.G., Carder C., Lennard N., Lockey S.J., Marsh P.,
RA   Skipp P., O'Connor C.D., Goodhead I., Norbertzcak H., Harris B., Ormond D.,
RA   Rance R., Quail M.A., Parkhill J., Stephens R.S., Clarke I.N.;
RT   "Chlamydia trachomatis: genome sequence analysis of lymphogranuloma
RT   venereum isolates.";
RL   Genome Res. 18:161-171(2008).
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; AM884177; CAP06640.1; -; Genomic_DNA.
DR   RefSeq; WP_012263575.1; NC_010280.2.
DR   AlphaFoldDB; B0BAX8; -.
DR   SMR; B0BAX8; -.
DR   MEROPS; C48.033; -.
DR   KEGG; ctl:CTLon_0242; -.
DR   HOGENOM; CLU_067510_0_0_0; -.
DR   OMA; ECICNCL; -.
DR   Proteomes; UP000000794; Chromosome.
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_0000396501"
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;  38369 MW;  7202F1C46DAEE685 CRC64;
     MEPIHNPPPQ TCSYSRSSTT YTSFKDASCD TKVIRIIIAL FLIVISCGLI LCAYTFRDLL
     DADYLAQEGP QQATKLLQQL DDVLTGPPLP IWDNEHLFQF SCLMQNKHKR VLPIDICNPL
     TKFNFLECIC NCLMTKQSVN VNETDMCELF CPPTCTPENY RRLLCTSSVF PFVMWHDPSA
     DTQEAMLTKM DQTMSSGRVG NSHWVLVIVD IEYRCVTFFD SLCDYVASPQ QMREQLEGLA
     VSLGAIYPKE GGADSDQEEL LSPFQVRIGS TVKVQSPGEF TCGAWCCQFL AWYLENPDFD
     LEEKVPKNPS ERRALLADFI STTEQAMSRY SSLSWPTTD