ID   CDUB1_CHLTA             Reviewed;         418 AA.
AC   Q3KKG8;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Deubiquitinase and deneddylase Dub1;
DE            Short=ChlaDub1;
DE            EC=3.4.22.-;
GN   Name=cdu1; OrderedLocusNames=CTA_0948;
OS   Chlamydia trachomatis serovar A (strain ATCC VR-571B / DSM 19440 / HAR-13).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=315277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-571B / DSM 19440 / HAR-13;
RX   PubMed=16177312; DOI=10.1128/iai.73.10.6407-6418.2005;
RA   Carlson J.H., Porcella S.F., McClarty G., Caldwell H.D.;
RT   "Comparative genomic analysis of Chlamydia trachomatis oculotropic and
RT   genitotropic strains.";
RL   Infect. Immun. 73:6407-6418(2005).
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; CP000051; AAX51154.1; -; Genomic_DNA.
DR   RefSeq; WP_011324911.1; NC_007429.1.
DR   AlphaFoldDB; Q3KKG8; -.
DR   SMR; Q3KKG8; -.
DR   MEROPS; C48.032; -.
DR   EnsemblBacteria; AAX51154; AAX51154; CTA_0948.
DR   KEGG; cta:CTA_0948; -.
DR   HOGENOM; CLU_067510_0_0_0; -.
DR   OMA; YFHTLYP; -.
DR   Proteomes; UP000002532; 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..418
FT                   /note="Deubiquitinase and deneddylase Dub1"
FT                   /id="PRO_0000396490"
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          75..145
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;  46657 MW;  F9A29202C498F34C CRC64;
     MLSPTNSISK TVPAPPQDSS KPVLISEEPQ NQLLQKVART ALAVLLVVVT LGLILLFYSF
     SDLQSFPWCC QTRPSTKEHP TISIPEPLPS PPLAVPRPST PPPPVISRPS TPPAPTPAIS
     PPSTPSAPKP STPPPLPPKA PKPVKTQEDL LPFVPEQVFV EMYEDMARRQ IIEALVPAWD
     SDIIFKCLCY FHTLYQGLIP LETFPPATIF NFKQKIISIL EDKKAVLRGE PIKGSLPICC
     SEENYRRHLQ GTTLLPVFMW YHPTPKTLSD TMQTMKQLAI KGSVGASHWL LVIVDIQARR
     LVYFDSLYNY VMSPEDMKKD LQSFAQQLDQ VYPACDSQKF SVKIAAKEVI QKGSGSSCGA
     WCCQFLHWYL RDPFTDALND LPVDSVERHE NLASFVRACE AAVQDLPELF WPEAKALF