PSCG_PSEAE
ID PSCG_PSEAE Reviewed; 115 AA.
AC P95435; Q7DCE7;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Type III export protein PscG;
DE AltName: Full=Pseudomonas secretion protein G;
GN Name=pscG; OrderedLocusNames=PA1720;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=388;
RX PubMed=8971719; DOI=10.1046/j.1365-2958.1996.01554.x;
RA Yahr T.L., Goranson J., Frank D.W.;
RT "Exoenzyme S of Pseudomonas aeruginosa is secreted by a type III pathway.";
RL Mol. Microbiol. 22:991-1003(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [3]
RP FUNCTION, SUBUNIT, MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC STRAIN=CHA;
RX PubMed=16115870; DOI=10.1074/jbc.m508089200;
RA Quinaud M., Chabert J., Faudry E., Neumann E., Lemaire D., Pastor A.,
RA Elsen S., Dessen A., Attree I.;
RT "The PscE-PscF-PscG complex controls type III secretion needle biogenesis
RT in Pseudomonas aeruginosa.";
RL J. Biol. Chem. 280:36293-36300(2005).
RN [4]
RP FUNCTION, INTERACTION WITH PSCG, MUTAGENESIS OF LEU-5 AND LEU-9, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=20494986; DOI=10.1128/jb.00117-10;
RA Ple S., Job V., Dessen A., Attree I.;
RT "Cochaperone interactions in export of the type III needle component PscF
RT of Pseudomonas aeruginosa.";
RL J. Bacteriol. 192:3801-3808(2010).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS), AND INTERACTION WITH PSCE AND PSCF.
RX PubMed=17470796; DOI=10.1073/pnas.0610098104;
RA Quinaud M., Ple S., Job V., Contreras-Martel C., Simorre J.P., Attree I.,
RA Dessen A.;
RT "Structure of the heterotrimeric complex that regulates type III secretion
RT needle formation.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:7803-7808(2007).
CC -!- FUNCTION: Chaperone of the type III secretion (T3S) injectisome that
CC translocates effector toxins into host cells, facilitating the
CC establishment and dissemination of infection. Prevents premature
CC polymerization of PscF, along with PscE, within the cytoplasm
CC (PubMed:20494986). Required for type III secretion needle assembly.
CC Also required for cytotoxicity by influencing PscF levels.
CC {ECO:0000269|PubMed:16115870, ECO:0000269|PubMed:20494986}.
CC -!- SUBUNIT: Forms a stable heterotrimeric complex with PscE and PscF in
CC the cytoplasm (PubMed:17470796). Co-stabilized by PscE.
CC {ECO:0000269|PubMed:16115870, ECO:0000269|PubMed:17470796,
CC ECO:0000269|PubMed:20494986}.
CC -!- INTERACTION:
CC P95435; Q9I317: pscE; NbExp=3; IntAct=EBI-6411621, EBI-6411628;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16115870}.
CC -!- MASS SPECTROMETRY: Mass=12451; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:16115870};
CC -!- DISRUPTION PHENOTYPE: Deletion mutant looses the capacity to lyse
CC macrophages, indicating the absence of a functional T3SS.
CC {ECO:0000269|PubMed:20494986}.
CC -!- SIMILARITY: Belongs to the YscG family. {ECO:0000305}.
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DR EMBL; U56077; AAC44778.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG05109.1; -; Genomic_DNA.
DR PIR; H83430; H83430.
DR RefSeq; NP_250411.1; NC_002516.2.
DR RefSeq; WP_003100735.1; NZ_QZGE01000003.1.
DR PDB; 2UWJ; X-ray; 2.00 A; G=1-115.
DR PDBsum; 2UWJ; -.
DR AlphaFoldDB; P95435; -.
DR SMR; P95435; -.
DR DIP; DIP-60935N; -.
DR IntAct; P95435; 1.
DR STRING; 287.DR97_167; -.
DR PaxDb; P95435; -.
DR PRIDE; P95435; -.
DR DNASU; 881982; -.
DR EnsemblBacteria; AAG05109; AAG05109; PA1720.
DR GeneID; 881982; -.
DR KEGG; pae:PA1720; -.
DR PATRIC; fig|208964.12.peg.1782; -.
DR PseudoCAP; PA1720; -.
DR HOGENOM; CLU_2108092_0_0_6; -.
DR OMA; WLALCEW; -.
DR BioCyc; PAER208964:G1FZ6-1751-MON; -.
DR EvolutionaryTrace; P95435; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030254; P:protein secretion by the type III secretion system; IGC:PseudoCAP.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR013348; T3SS_YscG.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR Pfam; PF09477; Type_III_YscG; 1.
DR TIGRFAMs; TIGR02508; type_III_yscG; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Reference proteome; Virulence.
FT CHAIN 1..115
FT /note="Type III export protein PscG"
FT /id="PRO_0000250213"
FT MUTAGEN 5
FT /note="L->S: About 20% loss of cytotoxicity; in association
FT with S-9."
FT /evidence="ECO:0000269|PubMed:20494986"
FT MUTAGEN 9
FT /note="L->S: About 20% loss of cytotoxicity; in association
FT with S-5."
FT /evidence="ECO:0000269|PubMed:20494986"
FT HELIX 4..17
FT /evidence="ECO:0007829|PDB:2UWJ"
FT TURN 18..20
FT /evidence="ECO:0007829|PDB:2UWJ"
FT HELIX 22..34
FT /evidence="ECO:0007829|PDB:2UWJ"
FT HELIX 38..51
FT /evidence="ECO:0007829|PDB:2UWJ"
FT HELIX 55..59
FT /evidence="ECO:0007829|PDB:2UWJ"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:2UWJ"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:2UWJ"
FT HELIX 71..80
FT /evidence="ECO:0007829|PDB:2UWJ"
FT HELIX 84..95
FT /evidence="ECO:0007829|PDB:2UWJ"
FT HELIX 100..113
FT /evidence="ECO:0007829|PDB:2UWJ"
SQ SEQUENCE 115 AA; 12451 MW; 3F546AA0645050B7 CRC64;
MDTSLIRELA ELALAGSGQH CHEEALCIAE WLERLGQDEA ARLIRISSLA NQGRYQEALA
FAHGNPWPAL EPWFALCEWH LGLGAALDRR LAGLGGSSDP ALADFAAGMR AQVRT
