ID   CDUB1_CHLTB             Reviewed;         403 AA.
AC   B0BAX9;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Deubiquitinase and deneddylase Dub1;
DE            Short=ChlaDub1;
DE            EC=3.4.22.-;
GN   Name=cdu1; OrderedLocusNames=CTLon_0243;
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; CAP06641.1; -; Genomic_DNA.
DR   RefSeq; WP_012263576.1; NC_010280.2.
DR   AlphaFoldDB; B0BAX9; -.
DR   SMR; B0BAX9; -.
DR   MEROPS; C48.032; -.
DR   KEGG; ctl:CTLon_0243; -.
DR   HOGENOM; CLU_067510_0_0_0; -.
DR   OMA; YFHTLYP; -.
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..403
FT                   /note="Deubiquitinase and deneddylase Dub1"
FT                   /id="PRO_0000396494"
FT   TRANSMEM        40..60
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          77..132
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        84..130
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        277
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        294
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        347
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   403 AA;  45195 MW;  B676BE6952755C70 CRC64;
     MLSPTNSTSK TAPVPPRDSS KPVLISEEPR NQLLQKVART ALAVLLVVVT LGLILLFYSF
     SDLQSFPWCC QTHPSTKEQP TISIPVPLPS PPLAVPRPST PPAPTPAISR PSTPSAPKPS
     TPPPLLPKAP KPVKTQENLF PLVPEQVFVE MYEDMARRRI IEALVPAWDS DIIFKCLCYF
     HTLYPGLIPL ETFPPATIFN FKQKIISILE DKKAVLRGEP IKGSLPICCS KENYRRHLQG
     TTLLPMFMWY HPTPKTLADT MQTMKQLAIK GSVGASHWLL VIVDIQARRL VYFDSLYNYV
     MPPEDMKKDL QSLAQQLDQV YPARNGQKFS VKIAAKEVIQ KDSGFSCGAW CCQFLYWYLR
     DPFTDALNDL PVDSVERHEN LASFVQACEA AVQDLPELSW PEA