EXSD_PSEAE
ID EXSD_PSEAE Reviewed; 276 AA.
AC Q9I321;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Transcriptional antiactivator ExsD;
GN Name=exsD; OrderedLocusNames=PA1714;
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, AND INTERACTION WITH EXSA.
RX PubMed=12421316; DOI=10.1046/j.1365-2958.2002.03228.x;
RA McCaw M.L., Lykken G.L., Singh P.K., Yahr T.L.;
RT "ExsD is a negative regulator of the Pseudomonas aeruginosa type III
RT secretion regulon.";
RL Mol. Microbiol. 46:1123-1133(2002).
RN [3]
RP FUNCTION, AND INTERACTION WITH EXSC.
RX PubMed=15225323; DOI=10.1111/j.1365-2958.2004.04128.x;
RA Dasgupta N., Lykken G.L., Wolfgang M.C., Yahr T.L.;
RT "A novel anti-anti-activator mechanism regulates expression of the
RT Pseudomonas aeruginosa type III secretion system.";
RL Mol. Microbiol. 53:297-308(2004).
RN [4]
RP FUNCTION, INTERACTION WITH EXSC, AND DISRUPTION PHENOTYPE.
RX PubMed=16980486; DOI=10.1128/jb.00884-06;
RA Lykken G.L., Chen G., Brutinel E.D., Chen L., Yahr T.L.;
RT "Characterization of ExsC and ExsD self-association and heterocomplex
RT formation.";
RL J. Bacteriol. 188:6832-6840(2006).
RN [5]
RP FUNCTION, AND INTERACTION WITH EXSA.
RX PubMed=19369699; DOI=10.1074/jbc.m109.003533;
RA Thibault J., Faudry E., Ebel C., Attree I., Elsen S.;
RT "Anti-activator ExsD forms a 1:1 complex with ExsA to inhibit transcription
RT of type III secretion operons.";
RL J. Biol. Chem. 284:15762-15770(2009).
RN [6]
RP FUNCTION, AND INTERACTION WITH EXSA AND EXSC.
RX PubMed=20008065; DOI=10.1128/jb.01457-09;
RA Brutinel E.D., Vakulskas C.A., Yahr T.L.;
RT "ExsD inhibits expression of the Pseudomonas aeruginosa type III secretion
RT system by disrupting ExsA self-association and DNA binding activity.";
RL J. Bacteriol. 192:1479-1486(2010).
RN [7]
RP FUNCTION, SUBUNIT, AND MUTAGENESIS OF MET-59.
RX PubMed=23279839; DOI=10.1111/febs.12103;
RA Bernhards R.C., Marsden A.E., Esher S.K., Yahr T.L., Schubot F.D.;
RT "Self-trimerization of ExsD limits inhibition of the Pseudomonas aeruginosa
RT transcriptional activator ExsA in vitro.";
RL FEBS J. 280:1084-1094(2013).
CC -!- FUNCTION: Negative regulator of the type III secretion system regulon.
CC Acts by disrupting transcriptional activator ExsA self-association and
CC DNA-binding activity in absence of inducing signals (PubMed:12421316,
CC PubMed:19369699, PubMed:20008065, PubMed:23279839). Upon host cell
CC contact, this interaction is disrupted by the anti-antiactivator
CC protein ExsC leading to ExsA activation (PubMed:15225323,
CC PubMed:16980486). {ECO:0000269|PubMed:12421316,
CC ECO:0000269|PubMed:15225323, ECO:0000269|PubMed:16980486,
CC ECO:0000269|PubMed:19369699, ECO:0000269|PubMed:20008065,
CC ECO:0000269|PubMed:23279839}.
CC -!- SUBUNIT: Can form homotrimer (PubMed:23279839). Interacts with ExsA;
CC this interaction inhibits ExsA activity (PubMed:12421316,
CC PubMed:19369699, PubMed:20008065). Interacts with ExsC; this
CC interaction dissociates the ExsD-ExsA complex (PubMed:15225323,
CC PubMed:16980486, PubMed:20008065). {ECO:0000269|PubMed:12421316,
CC ECO:0000269|PubMed:15225323, ECO:0000269|PubMed:16980486,
CC ECO:0000269|PubMed:19369699, ECO:0000269|PubMed:20008065,
CC ECO:0000269|PubMed:23279839}.
CC -!- INTERACTION:
CC Q9I321; P26993: exsA; NbExp=2; IntAct=EBI-6409805, EBI-6307207;
CC -!- DISRUPTION PHENOTYPE: Absence of ExsD leads to transcription of the
CC type III secretion system (T3SS) regulon derepression.
CC {ECO:0000269|PubMed:12421316}.
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DR EMBL; AE004091; AAG05103.1; -; Genomic_DNA.
DR PIR; B83430; B83430.
DR RefSeq; NP_250405.1; NC_002516.2.
DR RefSeq; WP_003100755.1; NZ_QZGE01000003.1.
DR AlphaFoldDB; Q9I321; -.
DR SMR; Q9I321; -.
DR IntAct; Q9I321; 2.
DR STRING; 287.DR97_173; -.
DR PaxDb; Q9I321; -.
DR DNASU; 880880; -.
DR EnsemblBacteria; AAG05103; AAG05103; PA1714.
DR GeneID; 880880; -.
DR KEGG; pae:PA1714; -.
DR PATRIC; fig|208964.12.peg.1777; -.
DR PseudoCAP; PA1714; -.
DR HOGENOM; CLU_1021707_0_0_6; -.
DR OMA; DRFAMRL; -.
DR BioCyc; PAER208964:G1FZ6-1745-MON; -.
DR PHI-base; PHI:6400; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0071277; P:cellular response to calcium ion; IMP:PseudoCAP.
DR GO; GO:0043392; P:negative regulation of DNA binding; IDA:PseudoCAP.
DR GO; GO:0032091; P:negative regulation of protein binding; IDA:PseudoCAP.
DR GO; GO:0050709; P:negative regulation of protein secretion; IMP:PseudoCAP.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:PseudoCAP.
DR Gene3D; 1.10.8.520; -; 1.
DR Gene3D; 1.20.1270.190; -; 2.
DR InterPro; IPR031835; ExsD.
DR InterPro; IPR043101; ExsD_dom1.
DR InterPro; IPR043102; ExsD_dom2.
DR Pfam; PF16806; ExsD; 1.
PE 1: Evidence at protein level;
KW Reference proteome.
FT CHAIN 1..276
FT /note="Transcriptional antiactivator ExsD"
FT /id="PRO_0000449830"
FT MUTAGEN 59
FT /note="M->R: Complete loss of trimer formation."
FT /evidence="ECO:0000269|PubMed:23279839"
SQ SEQUENCE 276 AA; 31366 MW; A6C56685A704124A CRC64;
MEQEDDKQYS REAVFAGRRV SVVGSDARSR GRVPGYASSS LYRESGIISA RQLALLQRML
PRLRLEQLFR CEWLQQRLAR GLALGREEVR QILLCAAQDD DGWCSELGDR VNLAVPQSMI
DWVLLPVYGW WESLLDQAIP GWRLSLVELE TQSRQLRVKS EFWSRVAELE PEQAREELAR
VAKCQARTQE QVAELAGKLE TASALAKSAW PNWQRGMATL LASGGLAGFE PIPEVLECLW
QPLCRLDDDV GAADAVQAWL HERNLCQAQD HFYWQS
