CDUB2_CHLT2
ID CDUB2_CHLT2 Reviewed; 339 AA.
AC B0B999;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Deubiquitinase and deneddylase Dub2;
DE Short=ChlaDub2;
DE EC=3.4.22.-;
GN Name=cdu2; OrderedLocusNames=CTL0246;
OS Chlamydia trachomatis serovar L2 (strain 434/Bu / ATCC VR-902B).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=471472;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=434/Bu / ATCC VR-902B;
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; AM884176; CAP03686.1; -; Genomic_DNA.
DR RefSeq; WP_009873474.1; NC_010287.1.
DR RefSeq; YP_001654331.1; NC_010287.1.
DR PDB; 6MRN; X-ray; 2.29 A; A=93-339.
DR PDB; 6OAM; X-ray; 2.50 A; A/B=88-338.
DR PDBsum; 6MRN; -.
DR PDBsum; 6OAM; -.
DR AlphaFoldDB; B0B999; -.
DR SMR; B0B999; -.
DR MEROPS; C48.033; -.
DR EnsemblBacteria; CAP03686; CAP03686; CTL0246.
DR KEGG; ctb:CTL0246; -.
DR PATRIC; fig|471472.4.peg.263; -.
DR HOGENOM; CLU_067510_0_0_0; -.
DR OMA; ECICNCL; -.
DR Proteomes; UP000000795; 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 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Membrane; Protease; Secreted; Thiol protease;
KW Transmembrane; Transmembrane helix; Ubl conjugation pathway; Virulence.
FT CHAIN 1..339
FT /note="Deubiquitinase and deneddylase Dub2"
FT /id="PRO_0000396500"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 203
FT /evidence="ECO:0000255"
FT ACT_SITE 220
FT /evidence="ECO:0000255"
FT ACT_SITE 282
FT /evidence="ECO:0000255"
FT HELIX 94..108
FT /evidence="ECO:0007829|PDB:6MRN"
FT TURN 122..124
FT /evidence="ECO:0007829|PDB:6MRN"
FT HELIX 125..140
FT /evidence="ECO:0007829|PDB:6MRN"
FT HELIX 145..148
FT /evidence="ECO:0007829|PDB:6MRN"
FT HELIX 157..166
FT /evidence="ECO:0007829|PDB:6MRN"
FT STRAND 169..176
FT /evidence="ECO:0007829|PDB:6MRN"
FT HELIX 183..196
FT /evidence="ECO:0007829|PDB:6MRN"
FT STRAND 203..210
FT /evidence="ECO:0007829|PDB:6MRN"
FT TURN 211..214
FT /evidence="ECO:0007829|PDB:6MRN"
FT STRAND 215..219
FT /evidence="ECO:0007829|PDB:6MRN"
FT STRAND 223..227
FT /evidence="ECO:0007829|PDB:6MRN"
FT HELIX 229..246
FT /evidence="ECO:0007829|PDB:6MRN"
FT STRAND 265..268
FT /evidence="ECO:0007829|PDB:6MRN"
FT HELIX 282..295
FT /evidence="ECO:0007829|PDB:6MRN"
FT HELIX 301..304
FT /evidence="ECO:0007829|PDB:6MRN"
FT HELIX 309..328
FT /evidence="ECO:0007829|PDB:6MRN"
SQ SEQUENCE 339 AA; 38368 MW; 7C7AF92FC511EBCA CRC64;
MEPIHNPPPQ TCSYSRPSTT YTSFKDASCD TKVTRIIIAL FLIVISCGLI LCAYTFRDLL
DADYLAQEGP QQATKLLQQL DDVLTGPPLP IWDNEHLFQF SCLMQNKHRR VLPIDICNPL
TKFNFLECIC NCLMTKQSVN VNETDMCELF CPPTCTPENY RRLLCTSSVF PFVMWHDPSA
DTQEAMLTKM DQTMSSGRVG NSHWVLVIVD IEYRCVTFFD SLCDYVASPQ QMREQLEGLA
VSLGAIYPKE GGADSDQEEL LSPFQVRIGS TVKVQSPGEF TCGAWCCQFL AWYLENPDFD
LEEKVPTNPS ERRALLADFI STTEQAMSRY SSLSWPTTD
