ID LUBX_LEGPH Reviewed; 246 AA.
AC Q5ZRQ0;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 27-MAR-2024, entry version 86.
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; Synonyms=legU2; OrderedLocusNames=lpg2830;
OS Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC
OS 33152 / DSM 7513).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=272624;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513;
RX PubMed=15448271; DOI=10.1126/science.1099776;
RA Chien M., Morozova I., Shi S., Sheng H., Chen J., Gomez S.M., Asamani G.,
RA Hill K., Nuara J., Feder M., Rineer J., Greenberg J.J., Steshenko V.,
RA Park S.H., Zhao B., Teplitskaya E., Edwards J.R., Pampou S., Georghiou A.,
RA Chou I.-C., Iannuccilli W., Ulz M.E., Kim D.H., Geringer-Sameth A.,
RA Goldsberry C., Morozov P., Fischer S.G., Segal G., Qu X., Rzhetsky A.,
RA Zhang P., Cayanis E., De Jong P.J., Ju J., Kalachikov S., Shuman H.A.,
RA Russo J.J.;
RT "The genomic sequence of the accidental pathogen Legionella pneumophila.";
RL Science 305:1966-1968(2004).
RN [2]
RP FUNCTION, UBIQUITIN LIGASE ACTIVITY, UBIQUITINATION, INTERACTION WITH HOST
RP CLK1, SUBCELLULAR LOCATION, INDUCTION, DOMAIN, AND MUTAGENESIS OF ILE-45
RP AND ILE-140.
RC STRAIN=Lp01;
RX PubMed=18284575; DOI=10.1111/j.1365-2958.2008.06124.x;
RA Kubori T., Hyakutake A., Nagai H.;
RT "Legionella translocates an E3 ubiquitin ligase that has multiple U-boxes
RT with distinct functions.";
RL Mol. Microbiol. 67:1307-1319(2008).
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 Acts in conjunction with host E2 ubiquitin-conjugating enzymes UBE2D1
CC (UBCH5A) or UBE2D3 (UBCH5C), and mediates polyubiquitination of host
CC kinase CLK1. {ECO:0000269|PubMed:18284575}.
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 -!- SUBUNIT: Interacts with host CLK1. {ECO:0000269|PubMed:18284575}.
CC -!- INTERACTION:
CC Q5ZRQ0; P22518: Clk1; Xeno; NbExp=3; IntAct=EBI-6402540, EBI-6479117;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18284575}. Host cell
CC {ECO:0000269|PubMed:18284575}. Note=Secreted via type IV secretion
CC system (T4SS), and delivered into the host cell.
CC -!- INDUCTION: Induced upon infection. {ECO:0000269|PubMed:18284575}.
CC -!- DOMAIN: U-box 1 is critical to the ubiquitin ligase activity, and U-box
CC 2 mediates interaction with host CLK1. {ECO:0000269|PubMed:18284575}.
CC -!- DOMAIN: The 25 C-terminal region may carry the signal responsible for
CC translocation into the host cell. {ECO:0000269|PubMed:18284575}.
CC -!- PTM: Ubiquitinated in the presence of host E1 ubiquitin-activating
CC enzyme, E2 ubiquitin-conjugating enzyme (UBE2D1 or UBE2D3) and
CC ubiquitin. {ECO:0000269|PubMed:18284575}.
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DR EMBL; AE017354; AAU28878.1; -; Genomic_DNA.
DR RefSeq; WP_010948517.1; NC_002942.5.
DR RefSeq; YP_096825.1; NC_002942.5.
DR AlphaFoldDB; Q5ZRQ0; -.
DR SMR; Q5ZRQ0; -.
DR DIP; DIP-59158N; -.
DR IntAct; Q5ZRQ0; 3.
DR STRING; 272624.lpg2830; -.
DR PaxDb; 272624-lpg2830; -.
DR GeneID; 66492001; -.
DR KEGG; lpn:lpg2830; -.
DR PATRIC; fig|272624.6.peg.3015; -.
DR eggNOG; COG5113; Bacteria.
DR HOGENOM; CLU_1127976_0_0_6; -.
DR OrthoDB; 5637399at2; -.
DR Proteomes; UP000000609; Chromosome.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0043657; C:host cell; IDA:UniProtKB.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
DR CDD; cd16453; RING-Ubox; 1.
DR CDD; cd23149; RING-Ubox_LubX-like_rpt1; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR003613; Ubox_domain.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR46803; E3 UBIQUITIN-PROTEIN LIGASE CHIP; 1.
DR PANTHER; PTHR46803:SF2; E3 UBIQUITIN-PROTEIN LIGASE CHIP; 1.
DR Pfam; PF04564; U-box; 2.
DR SMART; SM00504; Ubox; 2.
DR SUPFAM; SSF57850; RING/U-box; 2.
DR PROSITE; PS51698; U_BOX; 2.
PE 1: Evidence at protein level;
KW Reference proteome; Repeat; Secreted; Transferase; Ubl conjugation;
KW Ubl conjugation pathway; Virulence.
FT CHAIN 1..246
FT /note="E3 ubiquitin-protein ligase LubX"
FT /id="PRO_0000395863"
FT DOMAIN 36..109
FT /note="U-box 1"
FT DOMAIN 131..204
FT /note="U-box 2"
FT MUTAGEN 45
FT /note="I->A: Loss of ubiquitin ligase activity."
FT /evidence="ECO:0000269|PubMed:18284575"
FT MUTAGEN 140
FT /note="I->A: No change in ubiquitin ligase activity."
FT /evidence="ECO:0000269|PubMed:18284575"
SQ SEQUENCE 246 AA; 28412 MW; 096EE12CF4F58824 CRC64;
MGYRIEMATR NPFDIDHKSK YLREAALEAN LSHPETTPTM LTCPIDSGFL KDPVITPEGF
VYNKSSILKW LETKKEDPQS RKPLTAKDLQ PFPELLIIVN RFVETQTNYE KLKNRLVQNA
RVAARQKEYT EIPDIFLCPI SKTLIKTPVI TAQGKVYDQE ALSNFLIATG NKDETGKKLS
IDDVVVFDEL YQQIKVYNFY RKREMQKNQI QPSVSSGFGF FSLNFLTSWL WGTEEKKEKT
SSDMTY
//
