LUBX_LEGPA
ID LUBX_LEGPA Reviewed; 240 AA.
AC Q5X159;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=E3 ubiquitin-protein ligase LubX;
DE EC=2.3.2.27;
DE AltName: Full=Legionella U-box protein;
DE AltName: Full=RING-type E3 ubiquitin transferase LubX {ECO:0000305};
GN Name=lubX; OrderedLocusNames=lpp2887;
OS Legionella pneumophila (strain Paris).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=297246;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Paris;
RX PubMed=15467720; DOI=10.1038/ng1447;
RA Cazalet C., Rusniok C., Brueggemann H., Zidane N., Magnier A., Ma L.,
RA Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J.,
RA Glaser P., Buchrieser C.;
RT "Evidence in the Legionella pneumophila genome for exploitation of host
RT cell functions and high genome plasticity.";
RL Nat. Genet. 36:1165-1173(2004).
CC -!- FUNCTION: Effector proteins function to alter host cell physiology and
CC promote bacterial survival in host tissues. This protein is an E3
CC ubiquitin ligase that interferes with host's ubiquitination pathway.
CC {ECO:0000250|UniProtKB:Q5ZRQ0}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Host cell {ECO:0000250}.
CC Note=Secreted via type IV secretion system (T4SS), and delivered into
CC the host cell. {ECO:0000250}.
CC -!- DOMAIN: U-box 1 is critical to the ubiquitin ligase activity, and U-box
CC 2 mediates interaction with host target. {ECO:0000250}.
CC -!- DOMAIN: The 25 C-terminal region may carry the signal responsible for
CC translocation into the host cell. {ECO:0000250}.
CC -!- PTM: Ubiquitinated in the presence of host E1 ubiquitin-activating
CC enzyme, E2 ubiquitin-conjugating enzyme and ubiquitin. {ECO:0000250}.
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DR EMBL; CR628336; CAH14040.1; -; Genomic_DNA.
DR PDB; 4WZ0; X-ray; 1.95 A; A=17-117.
DR PDB; 4WZ2; X-ray; 3.41 A; A/B/C=102-202.
DR PDB; 4WZ3; X-ray; 2.70 A; B=1-215.
DR PDB; 4XI1; X-ray; 2.98 A; A/B/C=102-202.
DR PDBsum; 4WZ0; -.
DR PDBsum; 4WZ2; -.
DR PDBsum; 4WZ3; -.
DR PDBsum; 4XI1; -.
DR AlphaFoldDB; Q5X159; -.
DR SMR; Q5X159; -.
DR DIP; DIP-61711N; -.
DR IntAct; Q5X159; 1.
DR KEGG; lpp:lpp2887; -.
DR LegioList; lpp2887; -.
DR HOGENOM; CLU_1127976_0_0_6; -.
DR OMA; YTEIPDI; -.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0043657; C:host cell; ISS:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR CDD; cd16654; RING-Ubox_CHIP; 1.
DR Gene3D; 3.30.40.10; -; 2.
DR InterPro; IPR045200; CHIP/LubX.
DR InterPro; IPR045202; CHIP/LubX_RING-Ubox.
DR InterPro; IPR003613; Ubox_domain.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR46803; PTHR46803; 2.
DR Pfam; PF04564; U-box; 2.
DR SMART; SM00504; Ubox; 2.
DR PROSITE; PS51698; U_BOX; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Repeat; Secreted; Transferase; Ubl conjugation;
KW Ubl conjugation pathway; Virulence.
FT CHAIN 1..240
FT /note="E3 ubiquitin-protein ligase LubX"
FT /id="PRO_0000395864"
FT DOMAIN 30..103
FT /note="U-box 1"
FT DOMAIN 125..198
FT /note="U-box 2"
FT HELIX 17..25
FT /evidence="ECO:0007829|PDB:4WZ0"
FT HELIX 33..35
FT /evidence="ECO:0007829|PDB:4WZ0"
FT TURN 38..40
FT /evidence="ECO:0007829|PDB:4WZ0"
FT STRAND 45..49
FT /evidence="ECO:0007829|PDB:4WZ0"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:4WZ0"
FT HELIX 58..67
FT /evidence="ECO:0007829|PDB:4WZ0"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:4WZ0"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:4WZ0"
FT HELIX 89..116
FT /evidence="ECO:0007829|PDB:4WZ0"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:4WZ3"
FT TURN 133..135
FT /evidence="ECO:0007829|PDB:4WZ3"
FT STRAND 140..144
FT /evidence="ECO:0007829|PDB:4WZ3"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:4WZ3"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:4WZ3"
FT HELIX 153..162
FT /evidence="ECO:0007829|PDB:4WZ3"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:4WZ3"
FT TURN 168..170
FT /evidence="ECO:0007829|PDB:4WZ3"
FT HELIX 175..177
FT /evidence="ECO:0007829|PDB:4XI1"
FT HELIX 182..184
FT /evidence="ECO:0007829|PDB:4WZ3"
SQ SEQUENCE 240 AA; 27657 MW; 84CB1FFF15A0F25C CRC64;
MATRNPFDID HKSKYLREAA LEANLSHPET TPTMLTCPID SGFLKDPVIT PEGFVYNKSS
ILKWLETKKE DPQSRKPLTA KDLQPFPELL IIVNRFVETQ TNYEKLKNRL VQNARVAARQ
KEYTEIPDIF LCPISKTLIK TPVITAQGKV YDQEALSNFL IATGNKDETG KKLSIDDVVV
FDELYQQIKV YNFYRKREVQ KNQIQPSVSN GFGFFSLNFL TSWLWGTEEK KEKTSSDMTY
