DOTL_LEGPH
ID DOTL_LEGPH Reviewed; 783 AA.
AC Q5ZYC6;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Type 4 coupling protein DotL {ECO:0000303|PubMed:22694730};
DE Short=T4CP {ECO:0000303|PubMed:23028312};
GN Name=dotL {ECO:0000303|PubMed:17040490};
GN Synonyms=icmO {ECO:0000312|EMBL:AAU26543.1};
GN OrderedLocusNames=lpg0446 {ECO:0000312|EMBL:AAU26543.1};
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, SUBUNIT, AND SUBCELLULAR LOCATION.
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 [3]
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 [4]
RP FUNCTION, SUBUNIT, INTERACTION WITH ICMS AND ICMW, AND MUTAGENESIS OF
RP GLN-222 AND 726-ALA--THR-783.
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 [5] {ECO:0007744|PDB:5X1E, ECO:0007744|PDB:5X42, ECO:0007744|PDB:5X90}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 590-659 IN COMPLEXES WITH DOTN;
RP ICMS; ICMW AND LVGA, SUBUNIT, AND INTERACTION WITH DOTN; ICMS; ICMW AND
RP LVGA.
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 [6] {ECO:0007744|PDB:5XNB}
RP X-RAY CRYSTALLOGRAPHY (2.59 ANGSTROMS) OF 661-773 IN COMPLEX WITH ICMS AND
RP ICMW, AND SUBUNIT.
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 [7] {ECO:0007744|PDB:7BWK}
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 656-783 IN COMPLEX WITH ICMS;
RP ICMW; LVGA AND 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).
RN [8] {ECO:0007744|PDB:6SZ9}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.70 ANGSTROMS), FUNCTION, SUBUNIT, AND
RP MUTAGENESIS OF 363-ALA--ASP-366.
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).
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:17040490, PubMed:22694730, PubMed:32513920). Part of
CC a subcomplex which recruits effector proteins and delivers them to the
CC core transmembrane subcomplex (PubMed:23028312, PubMed:32513920). Plays
CC a central role in the assembly of the subcomplex (PubMed:32513920).
CC Required for the recruitment of IcmS and IcmW to the inner membrane and
CC for the translocation of adapter-dependent substrates
CC (PubMed:23028312). May have ATPase activity (Probable).
CC {ECO:0000269|PubMed:17040490, ECO:0000269|PubMed:22694730,
CC ECO:0000269|PubMed:23028312, ECO:0000269|PubMed:32513920,
CC ECO:0000305|PubMed:32513920}.
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:23028312, PubMed:28714967,
CC PubMed:32457311, PubMed:32513920). Six DotLMNYZ hetero-pentameric units
CC may assemble into an hexameric nanomachine, forming an inner membrane
CC channel for effectors to pass through (PubMed:32513920). Interacts
CC directly with DotM (PubMed:22694730, PubMed:32513920). Interacts
CC directly, via its C-terminal region, with the type IV adapter proteins
CC IcmS and IcmW (PubMed:23028312, PubMed:28714967, PubMed:29203674,
CC PubMed:32513920). Also interacts with DotN and LvgA via its C-terminal
CC region (PubMed:28714967, PubMed:32513920).
CC {ECO:0000269|PubMed:17040490, ECO:0000269|PubMed:22694730,
CC ECO:0000269|PubMed:23028312, ECO:0000269|PubMed:28714967,
CC ECO:0000269|PubMed:29203674, ECO:0000269|PubMed:32457311,
CC ECO:0000269|PubMed:32513920}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:17040490,
CC ECO:0000269|PubMed:22694730}; Single-pass membrane protein
CC {ECO:0000255}. Note=Localizes to the poles of the cell.
CC {ECO:0000269|PubMed:22694730}.
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DR EMBL; AE017354; AAU26543.1; -; Genomic_DNA.
DR RefSeq; WP_010946195.1; NC_002942.5.
DR RefSeq; YP_094490.1; NC_002942.5.
DR PDB; 5X1E; X-ray; 2.00 A; C=672-773, F=674-773.
DR PDB; 5X42; X-ray; 1.80 A; B/D=590-659.
DR PDB; 5X90; X-ray; 2.80 A; C=672-778, G=672-779.
DR PDB; 5XNB; X-ray; 2.59 A; A/D/G/J/M/P=661-773.
DR PDB; 6SZ9; EM; 3.70 A; A=1-783.
DR PDB; 7BWK; X-ray; 2.80 A; A/F=656-783.
DR PDB; 7OVB; EM; 3.61 A; A=1-783.
DR PDBsum; 5X1E; -.
DR PDBsum; 5X42; -.
DR PDBsum; 5X90; -.
DR PDBsum; 5XNB; -.
DR PDBsum; 6SZ9; -.
DR PDBsum; 7BWK; -.
DR PDBsum; 7OVB; -.
DR SMR; Q5ZYC6; -.
DR STRING; 272624.lpg0446; -.
DR TCDB; 3.A.7.9.1; the type iv (conjugal dna-protein transfer or virb) secretory pathway (ivsp) family.
DR PaxDb; Q5ZYC6; -.
DR PRIDE; Q5ZYC6; -.
DR EnsemblBacteria; AAU26543; AAU26543; lpg0446.
DR GeneID; 66489642; -.
DR KEGG; lpn:lpg0446; -.
DR PATRIC; fig|272624.6.peg.462; -.
DR eggNOG; COG3505; Bacteria.
DR HOGENOM; CLU_016768_1_0_6; -.
DR OMA; PFATGNA; -.
DR Proteomes; UP000000609; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR019476; T4SS_TraD_DNA-bd.
DR InterPro; IPR032689; TraG-D_C.
DR Pfam; PF12696; TraG-D_C; 1.
DR Pfam; PF10412; TrwB_AAD_bind; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Membrane;
KW Protein transport; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport; Virulence.
FT CHAIN 1..783
FT /note="Type 4 coupling protein DotL"
FT /id="PRO_0000455590"
FT TRANSMEM 47..67
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 100..500
FT /note="ATPase domain"
FT /evidence="ECO:0000305|PubMed:32513920"
FT REGION 671..773
FT /note="Interaction with IcmS/IcmW"
FT /evidence="ECO:0000303|PubMed:23028312"
FT MUTAGEN 222
FT /note="Q->R: Shows intracellular growth defects. Can still
FT recruit type IV adapter proteins IcmS/IcmW to the inner
FT membrane."
FT /evidence="ECO:0000269|PubMed:23028312"
FT MUTAGEN 363..366
FT /note="AEVD->RRVR: Abolishes intracellular growth in
FT A.castellanii."
FT /evidence="ECO:0000269|PubMed:32513920"
FT MUTAGEN 726..783
FT /note="Missing: Shows intracellular growth defects. Does
FT not interact with type IV adapter proteins IcmS/IcmW and is
FT unable to recruit them to the inner membrane. Can still
FT export the IcmSW-independent effectors, but exhibits a
FT specific defect in secretion of IcmSW-dependent
FT substrates."
FT /evidence="ECO:0000269|PubMed:23028312"
SQ SEQUENCE 783 AA; 87503 MW; 18C0E8FEC0D8EF15 CRC64;
MMRGIDSRHE LDPTLLLRDT RTFTQRLADF FADPTNISIV LISLAAVSYY FSEAATFLLI
MGGIFFLYSY TRKQKLPFRL PQISRAKDYN DLKPGINKPN IARGITFFGN DRKTGEELWF
ANDDMRTHAL IFGSTGSGKT ETLVSLSYNA LVQGSGFIYV DGKGDNSLYA KVFSMVRSMG
REDDLLLINF MTGARDIVGP QEKRLSNTLN PFCQGSSSML TQLVVSLMGS SGQSSDGDMW
KGRAIAFVEA LMRLLVYMRD EGAILLDANT IRNYFDLQRL ESIVIDKVFP RDDQESVNIE
TIPKLVTDPL RNYLNTLPGY NKEKKGKQVS QVLEQHGFIT MQLVRSFSSL ADTYGHIIRT
NLAEVDFKDV VLNRRILVVL LPALEKSPDE LSNLGKIIVS SLKAMMAAGL GEEVEGDYRD
VILRKPTNAP TPYMCILDEY GYYAVQGFAV VPAQARSLGF SAIFAGQDLP AFQKASKEEA
ASIGANTNIK ICMKLEDPTE TWDFFTKTAG EAYVTKVDSF QTKETSIANS YMDTKSSSFE
KRARVDLLDL KEQTEGEAHI FFKSKIVRAR MFYANPKPVK QLKINQFLKV EPPPDDYLMK
LQKQLASFQS ILESGDLSIN KAVENEEITL ISKALKESTI VEPIERGVAA LIAFHGQNEP
EPVEDIVEEE VEGALTIFSK LRIDPNAPPI LVADKEVFSE PLLPINETRN QMITIERLAG
AKDKYAGTVA NELIKDFQIA TSYPPEERDV IDVQELTGII RDLSAKISAE REKANKKAAE
ELT
