CDUB1_CHLT2
ID CDUB1_CHLT2 Reviewed; 401 AA.
AC B0B9A0;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Deubiquitinase and deneddylase Dub1;
DE Short=ChlaDub1;
DE EC=3.4.22.-;
GN Name=cdu1; OrderedLocusNames=CTL0247;
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).
RN [2]
RP FUNCTION IN VIRULENCE, INTERACTION WITH HOST NFKBIA, SUBCELLULAR LOCATION,
RP AND INDUCTION.
RX PubMed=18503636; DOI=10.1111/j.1462-5822.2008.01178.x;
RA Le Negrate G., Krieg A., Faustin B., Loeffler M., Godzik A., Krajewski S.,
RA Reed J.C.;
RT "ChlaDub1 of Chlamydia trachomatis suppresses NF-kappaB activation and
RT inhibits IkappaBalpha ubiquitination and degradation.";
RL Cell. Microbiol. 10:1879-1892(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). Impairs
CC ubiquitination and degradation of NF-kappa-B inhibitor alpha (NFKBIA),
CC thereby preventing NF-kappa-B activation. {ECO:0000250,
CC ECO:0000269|PubMed:18503636}.
CC -!- SUBUNIT: Binds to host NFKBIA.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18503636}. Host cell
CC {ECO:0000269|PubMed:18503636}. Membrane {ECO:0000269|PubMed:18503636};
CC Single-pass membrane protein {ECO:0000269|PubMed:18503636}.
CC Note=Secreted, and delivered into the host cell. Located predominantly
CC on the plasma membrane and to a lesser extent on intracellular
CC membranes, especially the host cell nuclear envelope.
CC -!- INDUCTION: Expressed late in the infectious cycle.
CC {ECO:0000269|PubMed:18503636}.
CC -!- SIMILARITY: Belongs to the peptidase C48 family. {ECO:0000305}.
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DR EMBL; AM884176; CAP03687.1; -; Genomic_DNA.
DR RefSeq; WP_009873475.1; NC_010287.1.
DR RefSeq; YP_001654332.1; NC_010287.1.
DR PDB; 5B5Q; X-ray; 1.70 A; A=159-401, B=155-401.
DR PDB; 5HAG; X-ray; 2.10 A; A=130-401.
DR PDB; 6FDK; X-ray; 1.60 A; A=155-401.
DR PDB; 6FDQ; X-ray; 2.30 A; A/B=155-401.
DR PDB; 6FDU; X-ray; 2.30 A; A/B=155-401.
DR PDB; 6GZS; X-ray; 1.90 A; A=130-401.
DR PDB; 6GZT; X-ray; 2.10 A; A=130-401.
DR PDBsum; 5B5Q; -.
DR PDBsum; 5HAG; -.
DR PDBsum; 6FDK; -.
DR PDBsum; 6FDQ; -.
DR PDBsum; 6FDU; -.
DR PDBsum; 6GZS; -.
DR PDBsum; 6GZT; -.
DR AlphaFoldDB; B0B9A0; -.
DR SMR; B0B9A0; -.
DR MEROPS; C48.032; -.
DR EnsemblBacteria; CAP03687; CAP03687; CTL0247.
DR KEGG; ctb:CTL0247; -.
DR PATRIC; fig|471472.4.peg.264; -.
DR HOGENOM; CLU_067510_0_0_0; -.
DR OMA; YFHTLYP; -.
DR Proteomes; UP000000795; Chromosome.
DR GO; GO:0005576; C:extracellular region; IDA: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.
DR PROSITE; PS50600; ULP_PROTEASE; 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..401
FT /note="Deubiquitinase and deneddylase Dub1"
FT /id="PRO_0000396493"
FT TRANSMEM 40..60
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 77..130
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..128
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 275
FT /evidence="ECO:0000255"
FT ACT_SITE 292
FT /evidence="ECO:0000255"
FT ACT_SITE 345
FT /evidence="ECO:0000255"
FT HELIX 147..149
FT /evidence="ECO:0007829|PDB:5HAG"
FT HELIX 153..162
FT /evidence="ECO:0007829|PDB:6GZS"
FT HELIX 168..181
FT /evidence="ECO:0007829|PDB:6FDK"
FT TURN 196..198
FT /evidence="ECO:0007829|PDB:6FDK"
FT HELIX 199..214
FT /evidence="ECO:0007829|PDB:6FDK"
FT STRAND 225..227
FT /evidence="ECO:0007829|PDB:6FDK"
FT HELIX 229..238
FT /evidence="ECO:0007829|PDB:6FDK"
FT STRAND 241..248
FT /evidence="ECO:0007829|PDB:6FDK"
FT HELIX 255..268
FT /evidence="ECO:0007829|PDB:6FDK"
FT STRAND 275..282
FT /evidence="ECO:0007829|PDB:6FDK"
FT TURN 283..286
FT /evidence="ECO:0007829|PDB:6FDK"
FT STRAND 287..291
FT /evidence="ECO:0007829|PDB:6FDK"
FT STRAND 295..299
FT /evidence="ECO:0007829|PDB:6FDK"
FT HELIX 301..318
FT /evidence="ECO:0007829|PDB:6FDK"
FT STRAND 322..324
FT /evidence="ECO:0007829|PDB:6GZS"
FT STRAND 328..331
FT /evidence="ECO:0007829|PDB:6FDK"
FT HELIX 345..358
FT /evidence="ECO:0007829|PDB:6FDK"
FT STRAND 360..362
FT /evidence="ECO:0007829|PDB:5B5Q"
FT HELIX 364..366
FT /evidence="ECO:0007829|PDB:6FDK"
FT HELIX 372..390
FT /evidence="ECO:0007829|PDB:6FDK"
FT STRAND 391..393
FT /evidence="ECO:0007829|PDB:6FDU"
SQ SEQUENCE 401 AA; 44977 MW; 78F38689DC180B6A CRC64;
MLSPTNSTSK TAPVPPRDSS KPVLISEEPR NQLLQKVART ALAVLLVVVT LGLILLFYSF
SDLQSFPWCC QTHPSTKEQP TISIPVPLPS PPLAVPRPST PPPPVISRPS TPSAPKPSTP
PPLLPKAPKP VKTQEDLLPL VPEQVFVEMY EDMARRQTIE ALVPAWDSDI IFKCLCYFHT
LYPGLIPLET FPPATIFNFK QKIISILEDK KAVLRGEPIK GPLPICCSKE NYRRHLQRTT
LLPVFMWYHP TPKTLSDTMQ TMKQLAIKGS VGASHWLLVI VDIQARRLVY FDSLYNYVMP
PENMKKELQS FAQQLDQVYP AYDSKKFSVK IAAKEVIQRG SGSSCGAWCC QFLHWYLKDP
LTDALNDLPV DSVERHENLA SFVQACEAAV QDLPELSWPE A
