ICMW_LEGPH
ID ICMW_LEGPH Reviewed; 151 AA.
AC Q5ZS31;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Type 4 adapter protein IcmW {ECO:0000305};
DE AltName: Full=Intracellular multiplication protein W {ECO:0000305};
DE AltName: Full=Secretion adapter protein IcmW {ECO:0000303|PubMed:22694730};
GN Name=icmW {ECO:0000303|PubMed:10361301};
GN OrderedLocusNames=lpg2688 {ECO:0000312|EMBL:AAU28746.1};
OS Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC
OS 33152 / DSM 7513).
OC Bacteria; Proteobacteria; 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, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=Philadelphia 1 / Lp01;
RX PubMed=10361301; DOI=10.1046/j.1365-2958.1999.01410.x;
RA Zuckman D.M., Hung J.B., Roy C.R.;
RT "Pore-forming activity is not sufficient for Legionella pneumophila
RT phagosome trafficking and intracellular growth.";
RL Mol. Microbiol. 32:990-1001(1999).
RN [3]
RP FUNCTION, INTERACTION WITH ICMS, AND DISRUPTION PHENOTYPE.
RC STRAIN=Philadelphia 1 / Lp01;
RX PubMed=11115108; DOI=10.1046/j.1365-2958.2000.02176.x;
RA Coers J., Kagan J.C., Matthews M., Nagai H., Zuckman D.M., Roy C.R.;
RT "Identification of Icm protein complexes that play distinct roles in the
RT biogenesis of an organelle permissive for Legionella pneumophila
RT intracellular growth.";
RL Mol. Microbiol. 38:719-736(2000).
RN [4]
RP FUNCTION, INTERACTION WITH ICMS AND EFFECTOR PROTEINS, SUBCELLULAR
RP LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=Philadelphia 1 / Lp01;
RX PubMed=15661013; DOI=10.1111/j.1365-2958.2004.04435.x;
RA Ninio S., Zuckman-Cholon D.M., Cambronne E.D., Roy C.R.;
RT "The Legionella IcmS-IcmW protein complex is important for Dot/Icm-mediated
RT protein translocation.";
RL Mol. Microbiol. 55:912-926(2005).
RN [5]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=Philadelphia 1 / Lp02;
RX PubMed=17040490; DOI=10.1111/j.1365-2958.2006.05446.x;
RA Vincent C.D., Friedman J.R., Jeong K.C., Buford E.C., Miller J.L.,
RA Vogel J.P.;
RT "Identification of the core transmembrane complex of the Legionella Dot/Icm
RT type IV secretion system.";
RL Mol. Microbiol. 62:1278-1291(2006).
RN [6]
RP FUNCTION, INTERACTION WITH EFFECTOR PROTEINS, AND DISRUPTION PHENOTYPE.
RC STRAIN=Philadelphia 1 / Lp01;
RX PubMed=18069892; DOI=10.1371/journal.ppat.0030188;
RA Cambronne E.D., Roy C.R.;
RT "The Legionella pneumophila IcmSW complex interacts with multiple Dot/Icm
RT effectors to facilitate type IV translocation.";
RL PLoS Pathog. 3:e188-e188(2007).
RN [7]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=Philadelphia 1 / Lp02;
RX PubMed=22694730; DOI=10.1111/j.1365-2958.2012.08118.x;
RA Vincent C.D., Friedman J.R., Jeong K.C., Sutherland M.C., Vogel J.P.;
RT "Identification of the DotL coupling protein subcomplex of the Legionella
RT Dot/Icm type IV secretion system.";
RL Mol. Microbiol. 85:378-391(2012).
RN [8]
RP FUNCTION, ACTIVITY REGULATION, INTERACTION WITH DOTL, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=Philadelphia 1 / Lp02;
RX PubMed=23028312; DOI=10.1371/journal.ppat.1002910;
RA Sutherland M.C., Nguyen T.L., Tseng V., Vogel J.P.;
RT "The Legionella IcmSW complex directly interacts with DotL to mediate
RT translocation of adaptor-dependent substrates.";
RL PLoS Pathog. 8:e1002910-e1002910(2012).
RN [9]
RP FUNCTION, AND SUBUNIT.
RC STRAIN=Philadelphia 1 / Lp01;
RX PubMed=32513920; DOI=10.1038/s41467-020-16681-z;
RA Meir A., Mace K., Lukoyanova N., Chetrit D., Hospenthal M.K., Redzej A.,
RA Roy C., Waksman G.;
RT "Mechanism of effector capture and delivery by the type IV secretion system
RT from Legionella pneumophila.";
RL Nat. Commun. 11:2864-2864(2020).
RN [10] {ECO:0007744|PDB:5X1E, ECO:0007744|PDB:5X90}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 2-149 IN COMPLEXES WITH DOTL;
RP ICMS AND LVGA, AND SUBUNIT.
RC STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513;
RX PubMed=28714967; DOI=10.1038/nmicrobiol.2017.114;
RA Kwak M.J., Kim J.D., Kim H., Kim C., Bowman J.W., Kim S., Joo K., Lee J.,
RA Jin K.S., Kim Y.G., Lee N.K., Jung J.U., Oh B.H.;
RT "Architecture of the type IV coupling protein complex of Legionella
RT pneumophila.";
RL Nat. Microbiol. 2:17114-17114(2017).
RN [11] {ECO:0007744|PDB:5XNB}
RP X-RAY CRYSTALLOGRAPHY (2.59 ANGSTROMS) IN COMPLEX WITH DOTL AND ICMS,
RP SUBUNIT, AND INTERACTION WITH LVGA.
RX PubMed=29203674; DOI=10.1073/pnas.1706883115;
RA Xu J., Xu D., Wan M., Yin L., Wang X., Wu L., Liu Y., Liu X., Zhou Y.,
RA Zhu Y.;
RT "Structural insights into the roles of the IcmS-IcmW complex in the type
RT IVb secretion system of Legionella pneumophila.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:13543-13548(2017).
RN [12] {ECO:0007744|PDB:7BWK}
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) IN COMPLEX WITH DOTL; ICMS; LVGA AND
RP VPDB, AND SUBUNIT.
RX PubMed=32457311; DOI=10.1038/s41467-020-16397-0;
RA Kim H., Kubori T., Yamazaki K., Kwak M.J., Park S.Y., Nagai H., Vogel J.P.,
RA Oh B.H.;
RT "Structural basis for effector protein recognition by the Dot/Icm Type IVB
RT coupling protein complex.";
RL Nat. Commun. 11:2623-2623(2020).
CC -!- FUNCTION: Component of the Dot/Icm type IVB secretion system (T4BSS),
CC which is used to inject bacterial effector proteins into eukaryotic
CC host cells (PubMed:15661013, PubMed:18069892, PubMed:17040490,
CC PubMed:22694730, PubMed:32513920). Part of a subcomplex which recruits
CC effector proteins and delivers them to the core transmembrane
CC subcomplex (PubMed:23028312, PubMed:32513920). The IcmS/IcmW protein
CC complex plays an important role in protein translocation by interacting
CC with multiple Dot/Icm effector proteins to facilitate their
CC translocation into host cells (PubMed:15661013, PubMed:18069892).
CC Interaction promotes conformational changes in the effector protein,
CC which may facilitate display of a C-terminal translocation signal
CC (PubMed:18069892). May maintain the substrates in a translocation
CC competent form (PubMed:23028312). Required for intracellular growth in
CC host cells, replicative phagosome formation and phagosome trafficking
CC (PubMed:10361301, PubMed:11115108). {ECO:0000269|PubMed:10361301,
CC ECO:0000269|PubMed:11115108, ECO:0000269|PubMed:15661013,
CC ECO:0000269|PubMed:17040490, ECO:0000269|PubMed:18069892,
CC ECO:0000269|PubMed:22694730, ECO:0000269|PubMed:23028312,
CC ECO:0000269|PubMed:32513920}.
CC -!- ACTIVITY REGULATION: Interaction with DotL is critical for the export
CC of IcmSW-dependent substrates. {ECO:0000269|PubMed:23028312}.
CC -!- SUBUNIT: The T4BSS is a complex nanomachine composed of several
CC subcomplexes. This subunit is part of the Type IV Coupling Complex
CC (T4CC), a subcomplex composed of the DotLMNYZ core and the IcmSW-LvgA
CC adapter subunits, linked by the C-terminal tail of DotL
CC (PubMed:17040490, PubMed:22694730, PubMed:28714967, PubMed:32457311,
CC PubMed:32513920). Interacts with IcmS (PubMed:11115108,
CC PubMed:15661013, PubMed:29203674). IcmS and IcmW form a stable complex
CC (PubMed:15661013). Interaction with IcmS greatly enhances the stability
CC of IcmW (PubMed:15661013, PubMed:29203674). Interacts directly with the
CC type 4 coupling protein DotL (PubMed:23028312, PubMed:29203674,
CC PubMed:32513920). Interacts with LvgA (PubMed:29203674). Interacts with
CC effector proteins (PubMed:15661013, PubMed:18069892, PubMed:29203674).
CC {ECO:0000269|PubMed:11115108, ECO:0000269|PubMed:15661013,
CC ECO:0000269|PubMed:17040490, ECO:0000269|PubMed:18069892,
CC ECO:0000269|PubMed:22694730, ECO:0000269|PubMed:23028312,
CC ECO:0000269|PubMed:28714967, ECO:0000269|PubMed:29203674,
CC ECO:0000269|PubMed:32457311, ECO:0000269|PubMed:32513920}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10361301,
CC ECO:0000269|PubMed:15661013, ECO:0000269|PubMed:17040490}.
CC Note=Associates with the inner membrane at the poles in a
CC DotL/DotM/DotN-dependent manner. {ECO:0000269|PubMed:22694730,
CC ECO:0000269|PubMed:23028312}.
CC -!- DISRUPTION PHENOTYPE: Deletion of the gene leads to a strong decrease
CC in intracellular growth in human monocytes (PubMed:10361301,
CC PubMed:11115108). Mutant is unable to evade phagosome lysosome fusion,
CC but retains the pore-forming activity (PubMed:10361301,
CC PubMed:11115108). Mutation severely impairs the translocation into host
CC cells of multiple effector proteins, including SidA, SidB, SidC, SidD,
CC SidE, SidG, SidH, WipA and WipB (PubMed:15661013, PubMed:18069892).
CC Loss of this gene has an effect on the levels of IcmS
CC (PubMed:17040490). {ECO:0000269|PubMed:10361301,
CC ECO:0000269|PubMed:11115108, ECO:0000269|PubMed:15661013,
CC ECO:0000269|PubMed:17040490, ECO:0000269|PubMed:18069892}.
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DR EMBL; AE017354; AAU28746.1; -; Genomic_DNA.
DR RefSeq; WP_010948388.1; NC_002942.5.
DR RefSeq; YP_096693.1; NC_002942.5.
DR PDB; 5X1E; X-ray; 2.00 A; B/E=2-149.
DR PDB; 5X90; X-ray; 2.80 A; B=2-149, F=2-150.
DR PDB; 5XNB; X-ray; 2.59 A; C/F/I/L/O/R=1-151.
DR PDB; 7BWK; X-ray; 2.80 A; C/H=1-151.
DR PDBsum; 5X1E; -.
DR PDBsum; 5X90; -.
DR PDBsum; 5XNB; -.
DR PDBsum; 7BWK; -.
DR SMR; Q5ZS31; -.
DR DIP; DIP-59159N; -.
DR IntAct; Q5ZS31; 1.
DR STRING; 272624.lpg2688; -.
DR TCDB; 3.A.7.9.1; the type iv (conjugal dna-protein transfer or virb) secretory pathway (ivsp) family.
DR PaxDb; Q5ZS31; -.
DR EnsemblBacteria; AAU28746; AAU28746; lpg2688.
DR GeneID; 66491862; -.
DR KEGG; lpn:lpg2688; -.
DR PATRIC; fig|272624.6.peg.2870; -.
DR eggNOG; ENOG5033XTW; Bacteria.
DR HOGENOM; CLU_1746563_0_0_6; -.
DR OMA; HDPAGFF; -.
DR Proteomes; UP000000609; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Protein transport; Reference proteome; Transport;
KW Virulence.
FT CHAIN 1..151
FT /note="Type 4 adapter protein IcmW"
FT /id="PRO_0000455596"
SQ SEQUENCE 151 AA; 17329 MW; 8593EFD79E009F41 CRC64;
MPDLSHEASA KYWFEYLDPM IYRVITFMES VENWTLDGNP ELEEAMKQLG QELDDIEKID
LGLLAEEDKF IRIVGNIKSG RGLRLLQAID TVHPGSASRV LIHAEETSLS SSDPAGFFLK
RNIVFERLRL LSRVFCQYRL KLVLRALEGD E
