EXSE_PSEAE
ID EXSE_PSEAE Reviewed; 81 AA.
AC Q9I322;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Type III secretion regulatory protein ExsE {ECO:0000303|PubMed:15985546};
GN Name=exsE; OrderedLocusNames=PA1711;
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 [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 [2]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP EXSC.
RX PubMed=15911752; DOI=10.1073/pnas.0503005102;
RA Rietsch A., Vallet-Gely I., Dove S.L., Mekalanos J.J.;
RT "ExsE, a secreted regulator of type III secretion genes in Pseudomonas
RT aeruginosa.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:8006-8011(2005).
RN [3]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH EXSC.
RX PubMed=15985546; DOI=10.1073/pnas.0504405102;
RA Urbanowski M.L., Lykken G.L., Yahr T.L.;
RT "A secreted regulatory protein couples transcription to the secretory
RT activity of the Pseudomonas aeruginosa type III secretion system.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:9930-9935(2005).
RN [4] {ECO:0007744|PDB:3KXY}
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 16-81, AND INTERACTION WITH EXSC.
RX PubMed=20536183; DOI=10.1021/bi100432e;
RA Vogelaar N.J., Jing X., Robinson H.H., Schubot F.D.;
RT "Analysis of the crystal structure of the ExsC.ExsE complex reveals
RT distinctive binding interactions of the Pseudomonas aeruginosa type III
RT secretion chaperone ExsC with ExsE and ExsD.";
RL Biochemistry 49:5870-5879(2010).
CC -!- FUNCTION: Acts as a negative regulator of the type III secretion
CC regulon (T3SS) expression (PubMed:15911752). In the absence of inducing
CC signals such as low Ca(2+) or host cell contact, the T3SS/injectisome
CC is expressed at a low basal level and exists in a quiescent state due
CC to ExsA sequestration by ExsD. ExsE binding to ExsC disrupts the
CC complex between ExsC and ExsD, thereby allowing free ExsD to bind ExsA
CC (PubMed:15911752, PubMed:15985546). Upon inducing signal, ExsE is
CC secreted allowing ExsC to bind ExsD. In turn, ExsD cannot bind ExsA and
CC prevent ExsA-mediated transcriptional activation of the type III
CC secretion system (PubMed:15911752, PubMed:15985546).
CC {ECO:0000269|PubMed:15911752, ECO:0000269|PubMed:15985546}.
CC -!- SUBUNIT: Interacts with ExsC. {ECO:0000269|PubMed:15911752,
CC ECO:0000269|PubMed:15985546, ECO:0000269|PubMed:20536183}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15911752}. Secreted
CC {ECO:0000269|PubMed:15911752}. Note=Secreted under low-calcium
CC conditions. {ECO:0000269|PubMed:15911752}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutant deregulates expression of the
CC type III secretion genes. {ECO:0000269|PubMed:15911752,
CC ECO:0000269|PubMed:15985546}.
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DR EMBL; AE004091; AAG05100.1; -; Genomic_DNA.
DR PIR; D83433; D83433.
DR RefSeq; NP_250402.1; NC_002516.2.
DR RefSeq; WP_003100766.1; NZ_QZGE01000003.1.
DR PDB; 3KXY; X-ray; 2.80 A; T/U/V/W/X/Y=16-81.
DR PDBsum; 3KXY; -.
DR AlphaFoldDB; Q9I322; -.
DR SMR; Q9I322; -.
DR STRING; 287.DR97_176; -.
DR PaxDb; Q9I322; -.
DR DNASU; 880941; -.
DR EnsemblBacteria; AAG05100; AAG05100; PA1711.
DR GeneID; 880941; -.
DR KEGG; pae:PA1711; -.
DR PATRIC; fig|208964.12.peg.1773; -.
DR PseudoCAP; PA1711; -.
DR HOGENOM; CLU_195301_0_0_6; -.
DR BioCyc; PAER208964:G1FZ6-1742-MON; -.
DR EvolutionaryTrace; Q9I322; -.
DR PHI-base; PHI:3520; -.
DR PHI-base; PHI:6401; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0051087; F:chaperone binding; IDA:PseudoCAP.
DR GO; GO:0071277; P:cellular response to calcium ion; IDA:PseudoCAP.
DR GO; GO:0050709; P:negative regulation of protein secretion; IMP:PseudoCAP.
DR GO; GO:0030254; P:protein secretion by the type III secretion system; IMP:PseudoCAP.
DR DisProt; DP01147; -.
DR InterPro; IPR040866; T3SS_ExsE.
DR Pfam; PF18286; T3SS_ExsE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Reference proteome; Secreted.
FT CHAIN 1..81
FT /note="Type III secretion regulatory protein ExsE"
FT /id="PRO_0000449831"
FT REGION 55..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:3KXY"
FT STRAND 26..31
FT /evidence="ECO:0007829|PDB:3KXY"
FT HELIX 41..51
FT /evidence="ECO:0007829|PDB:3KXY"
FT HELIX 58..67
FT /evidence="ECO:0007829|PDB:3KXY"
FT HELIX 73..75
FT /evidence="ECO:0007829|PDB:3KXY"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:3KXY"
SQ SEQUENCE 81 AA; 8696 MW; 53AE3CEBF36A5576 CRC64;
MKIESISPVQ PSQDAGAEAV GHFEGRSVTR AAVRGEDRSS VAGLARWLAR NVAGDPRSEQ
ALQRLADGDG TPLEARTVRR R
