ID   CDUB1_CHLTJ             Reviewed;         418 AA.
AC   C4PQR0;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 52.
DE   RecName: Full=Deubiquitinase and deneddylase Dub1;
DE            Short=ChlaDub1;
DE            EC=3.4.22.-;
GN   Name=cdu1; OrderedLocusNames=JALI_8791;
OS   Chlamydia trachomatis serovar B (strain Jali20/OT).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=580049;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Jali20/OT;
RX   PubMed=19460133; DOI=10.1186/1471-2164-10-239;
RA   Seth-Smith H.M.B., Harris S.R., Persson K., Marsh P., Barron A.,
RA   Bignell A., Bjartling C., Clark L., Cutcliffe L.T., Lambden P.R.,
RA   Lennard N., Lockey S.J., Quail M.A., Salim O., Skilton R.J., Wang Y.,
RA   Holland M.J., Parkhill J., Thomson N.R., Clarke I.N.;
RT   "Co-evolution of genomes and plasmids within Chlamydia trachomatis and the
RT   emergence in Sweden of a new variant strain.";
RL   BMC Genomics 10:239-239(2009).
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; FM872308; CAX11332.1; -; Genomic_DNA.
DR   RefSeq; WP_012728021.1; NC_012686.1.
DR   AlphaFoldDB; C4PQR0; -.
DR   SMR; C4PQR0; -.
DR   MEROPS; C48.032; -.
DR   KEGG; ctj:JALI_8791; -.
DR   HOGENOM; CLU_067510_0_0_0; -.
DR   OMA; YFHTLYP; -.
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..418
FT                   /note="Deubiquitinase and deneddylase Dub1"
FT                   /id="PRO_0000396491"
FT   TRANSMEM        40..60
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          72..144
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        84..142
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        288
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        305
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        358
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   418 AA;  46632 MW;  ED7C51811337611B CRC64;
     MLSPTNSISK TAPVPPQDSS KPVLISEEPQ NQLLQKVART ALAVLLVVVT LGLILLFYSF
     SDLQSFPWCC QTRPSTKEQP TISIPVPLPS PPLAVPRPST PPPPVISRPS TPPAPTPAIS
     PPSTPSAPKP STPPPLPPKA PKPVKTQEDL LPFVPEQVFV EMYEDMARRR IIEALVPAWD
     SDIIFKCLCY FHTLYPGLIP LETFPPATIF NFKQKIISIL EDKKAVLRGE PIKGSLPICC
     SEENYRRHLQ GTTLLPVFMW YHPTPKTLSD TMQTMKQLAI KGSVGASHWL LVIVDIQARR
     LVYFDSLYNY VMSPEDMKKD LQSFAQQLDQ VYPAYDSQIF SVKIAAKEVI QKGSGSSCGA
     WCCQFLHWYL RDPFTDALND LPVDSVERHE NLASFVQACE AAVQDLPELF WPEAKALF