CDUB1_CHLTZ
ID CDUB1_CHLTZ Reviewed; 418 AA.
AC C4PLJ5;
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=CTB_8791;
OS Chlamydia trachomatis serovar B (strain TZ1A828/OT).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=672161;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TZ1A828/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; FM872307; CAX10439.1; -; Genomic_DNA.
DR RefSeq; WP_012728210.1; NC_012687.1.
DR AlphaFoldDB; C4PLJ5; -.
DR SMR; C4PLJ5; -.
DR MEROPS; C48.032; -.
DR KEGG; ctz:CTB_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_0000396492"
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; 46678 MW; D96E0C2FA4697AB9 CRC64;
MLSPTNSISK TAPVPPQDSS KPVLISEEPQ NQLLQKVART ALAVLLVVVT LGLILLFYSF
SDLQSFPWCC QTRPSTKEQP TISIPVPLPS PPLAVPRPST PPPPVISRPS TPPAPTPAIS
PPSTPSAPKP STPPPLPPKA PKPVKTQEDL LPFVPEQVFV EMYEDMARRR IIEALVPAWD
SDIIFKCLCY FHTLYQGLIP LETFPPATIF NFKQKIISIL EDKKAVLRGE PIKGSLPICC
SEENYRRHLQ GTTLLPVFMW YHPTPKTLSD TMQTMKQLAI KGSVGASHWL LVIVDIQARR
LVYFDSLYNY VMSPEDMKKD LQSFAQQLDQ VYPAYDSQKF SVKIAAKEVI QKGSGSSCGA
WCCQFLHWYL RDPFTDALND LPVDSVERHE NLASFVQACE AAVQDLPELF WPEAKALF
