ID   CDUB1_CHLTR             Reviewed;         418 AA.
AC   O84876;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Deubiquitinase and deneddylase Dub1;
DE            Short=ChlaDub1;
DE            EC=3.4.22.-;
GN   Name=cdu1; OrderedLocusNames=CT_868;
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, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP   MUTAGENESIS OF CYS-358.
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; AAC68466.1; -; Genomic_DNA.
DR   PIR; D71460; D71460.
DR   RefSeq; NP_220390.1; NC_000117.1.
DR   RefSeq; WP_009872258.1; NC_000117.1.
DR   AlphaFoldDB; O84876; -.
DR   SMR; O84876; -.
DR   STRING; 813.O172_04855; -.
DR   MEROPS; C48.032; -.
DR   EnsemblBacteria; AAC68466; AAC68466; CT_868.
DR   GeneID; 884669; -.
DR   KEGG; ctr:CT_868; -.
DR   PATRIC; fig|272561.5.peg.959; -.
DR   HOGENOM; CLU_067510_0_0_0; -.
DR   InParanoid; O84876; -.
DR   OMA; YFHTLYP; -.
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.
DR   PROSITE; PS50600; ULP_PROTEASE; 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..418
FT                   /note="Deubiquitinase and deneddylase Dub1"
FT                   /id="PRO_0000396489"
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..143
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..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:0000305"
FT   MUTAGEN         358
FT                   /note="C->A: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:16824101"
SQ   SEQUENCE   418 AA;  46733 MW;  A73D23E32716BBE4 CRC64;
     MLSPTNSTSK KAPVPPQDSS KPVLISEEPQ NQLLQKVART ALAVLLVVVT LGLILLFYSF
     SDLQSFPWCC QTRPSTKEQP TISIPVPLPS PPLAVPRPST PPPPVISRPS TPPAPTPAIS
     PPSTPSAPKP STPPPLPPKA PKPVKTQEDL LPFVPEQVFV EMYEDMARRW IIEALVPAWD
     SDIIFKCLCY FHTLYQGLIP LETFPPATIF NFKQKIISIL EDKKAVLRGE PIKGSLPICC
     SEENYRRHLH GTTLLPVFMW YHPTPKTLSD TMQTMKQLAI KGSVGASHWL LVIVDIQARR
     LVYFDSLYNY VMSPEDMEKD LQSFAQQLDQ VYPAYDSQKF SVKIAAKEVI QKGSGSSCGA
     WCCQFLHWYL RDPFTDALND LPVDSVERHE NLASFVQACE AAVQDLPELF WPEAKALF