CDUB1_CHLTS
ID CDUB1_CHLTS Reviewed; 418 AA.
AC D3UTF4;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 39.
DE RecName: Full=Deubiquitinase and deneddylase Dub1;
DE Short=ChlaDub1;
DE EC=3.4.22.-;
GN Name=cdu1; OrderedLocusNames=SW2_8841;
OS Chlamydia trachomatis serovar E (strain Sweden2).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=634464;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sweden2;
RX PubMed=20093289; DOI=10.1099/mic.0.036830-0;
RA Unemo M., Seth-Smith H.M., Cutcliffe L.T., Skilton R.J., Barlow D.,
RA Goulding D., Persson K., Harris S.R., Kelly A., Bjartling C., Fredlund H.,
RA Olcen P., Thomson N.R., Clarke I.N.;
RT "The Swedish new variant of Chlamydia trachomatis: Genome sequence,
RT morphology, cell tropism and phenotypic characterization.";
RL Microbiology 156:1394-1404(2010).
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; FN652779; CBJ15397.1; -; Genomic_DNA.
DR RefSeq; WP_014541837.1; NC_017441.1.
DR AlphaFoldDB; D3UTF4; -.
DR SMR; D3UTF4; -.
DR MEROPS; C48.032; -.
DR KEGG; csw:SW2_8841; -.
DR PATRIC; fig|634464.3.peg.964; -.
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_0000396495"
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..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; 46722 MW; F8C2D6D39DAAFCA4 CRC64;
MLSPTNSTSK TAPVPPQDSS KPVLISEEPQ NQLLQKVART ALVVLLVVVT LGLILLFYSF
SDLQSFPWCC QTRPSTKEQP TISIPVPLPS PPLAVPRPST PPPPVISRPS MPPAPTPAIS
PPSTPSAPKP STPPPLPPKA PKPVKTQEDL LPFVPEQVFV EMYEDMARRR TIEALVPAWD
SDIIFKCLCY FHTLYQGLIP LETFPPATIF NFKQKIISIL EDKKAVLRGE PIKGSLPICC
SEENYRRHLH GTTLLPVFMW YHPTPKTLSD TMQTMKQLAI KGSVGASHWL LVIVDIQARR
LVYFDSLYNY VMSPEDMEKD LQSFAQQLDQ VYPAYDSQKF SVKIAAKEVI QKGSGSSCGA
WCCQFLHWYL RDPFTDALND LPVDSVERHE NLASFVQACE AAVQDLPELF WPEAKALF
