ID   CDUB2_CHLTR             Reviewed;         339 AA.
AC   O84875;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Deubiquitinase and deneddylase Dub2;
DE            Short=ChlaDub2;
DE            EC=3.4.22.-;
GN   Name=cdu2; OrderedLocusNames=CT_867;
OS   Chlamydia trachomatis (strain D/UW-3/Cx).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=272561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D/UW-3/Cx;
RX   PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA   Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA   Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT   "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT   trachomatis.";
RL   Science 282:754-759(1998).
RN   [2]
RP   FUNCTION AS A PROTEASE.
RC   STRAIN=L2;
RX   PubMed=16824101; DOI=10.1111/j.1365-2958.2006.05199.x;
RA   Misaghi S., Balsara Z.R., Catic A., Spooner E., Ploegh H.L.,
RA   Starnbach M.N.;
RT   "Chlamydia trachomatis-derived deubiquitinating enzymes in mammalian cells
RT   during infection.";
RL   Mol. Microbiol. 61:142-150(2006).
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.
CC       {ECO:0000269|PubMed:16824101}.
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; AE001273; AAC68465.1; -; Genomic_DNA.
DR   PIR; B71462; B71462.
DR   RefSeq; NP_220389.1; NC_000117.1.
DR   RefSeq; WP_009872257.1; NC_000117.1.
DR   AlphaFoldDB; O84875; -.
DR   SMR; O84875; -.
DR   STRING; 813.O172_04850; -.
DR   MEROPS; C48.033; -.
DR   EnsemblBacteria; AAC68465; AAC68465; CT_867.
DR   GeneID; 884676; -.
DR   KEGG; ctr:CT_867; -.
DR   PATRIC; fig|272561.5.peg.958; -.
DR   HOGENOM; CLU_067510_0_0_0; -.
DR   InParanoid; O84875; -.
DR   OMA; ECICNCL; -.
DR   Proteomes; UP000000431; 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; IDA:UniProtKB.
DR   GO; GO:0019784; F:deNEDDylase activity; IDA:UniProtKB.
DR   GO; GO:0000338; P:protein deneddylation; IDA:UniProtKB.
DR   GO; GO:0016579; P:protein deubiquitination; IDA: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   1: Evidence at protein level;
KW   Hydrolase; Membrane; Protease; Reference proteome; Secreted;
KW   Thiol protease; Transmembrane; Transmembrane helix;
KW   Ubl conjugation pathway; Virulence.
FT   CHAIN           1..339
FT                   /note="Deubiquitinase and deneddylase Dub2"
FT                   /id="PRO_0000396496"
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