EXSC_PSEAE
ID EXSC_PSEAE Reviewed; 145 AA.
AC P26995;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Transcriptional anti-antiactivator ExsC;
GN Name=exsC; OrderedLocusNames=PA1710;
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=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=1655713; DOI=10.1128/jb.173.20.6460-6468.1991;
RA Frank D.W., Iglewski B.H.;
RT "Cloning and sequence analysis of a trans-regulatory locus required for
RT exoenzyme S synthesis in Pseudomonas aeruginosa.";
RL J. Bacteriol. 173:6460-6468(1991).
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, AND DISRUPTION PHENOTYPE.
RX PubMed=9045825; DOI=10.1128/jb.179.5.1646-1654.1997;
RA Goranson J., Hovey A.K., Frank D.W.;
RT "Functional analysis of exsC and exsB in regulation of exoenzyme S
RT production by Pseudomonas aeruginosa.";
RL J. Bacteriol. 179:1646-1654(1997).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH EXSD, AND SUBCELLULAR
RP LOCATION.
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 [5]
RP FUNCTION, AND INTERACTION WITH EXSD.
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 [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16714561; DOI=10.1128/iai.00090-06;
RA Dasgupta N., Ashare A., Hunninghake G.W., Yahr T.L.;
RT "Transcriptional induction of the Pseudomonas aeruginosa type III secretion
RT system by low Ca2+ and host cell contact proceeds through two distinct
RT signaling pathways.";
RL Infect. Immun. 74:3334-3341(2006).
RN [7]
RP SUBUNIT, INTERACTION WITH EXSE AND EXSD, AND ACTIVITY REGULATION.
RX PubMed=17197437; DOI=10.1074/jbc.m611664200;
RA Zheng Z., Chen G., Joshi S., Brutinel E.D., Yahr T.L., Chen L.;
RT "Biochemical characterization of a regulatory cascade controlling
RT transcription of the Pseudomonas aeruginosa type III secretion system.";
RL J. Biol. Chem. 282:6136-6142(2007).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 1-131, AND INTERACTION WITH EXSE.
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: Part of the regulatory cascade that plays a role in the
CC transcriptional regulation of the type III secretion system (T3SS)
CC (PubMed:16714561, PubMed:9045825). Interacts with antiactivator ExsD to
CC inhibit its activity leading to ExsA-mediated transcription
CC (PubMed:15225323, PubMed:16980486). {ECO:0000269|PubMed:15225323,
CC ECO:0000269|PubMed:16714561, ECO:0000269|PubMed:16980486,
CC ECO:0000269|PubMed:9045825}.
CC -!- ACTIVITY REGULATION: In the absence of inducing signals, ExsE interacts
CC with and inhibits ExsC activity. {ECO:0000269|PubMed:17197437}.
CC -!- SUBUNIT: Homodimer (PubMed:17197437). Interacts with ExsE
CC (PubMed:17197437, PubMed:20536183). Interacts directly with ExsD to
CC form a heterotetrameric complex (PubMed:17197437, PubMed:15225323,
CC PubMed:16980486). {ECO:0000269|PubMed:15225323,
CC ECO:0000269|PubMed:16980486, ECO:0000269|PubMed:17197437,
CC ECO:0000269|PubMed:20536183}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15225323}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutant results in a two to three-fold
CC reduction in extracellular exoenzyme S activity representing the
CC efficiency of type III secretion system (T3SS) (PubMed:9045825,
CC PubMed:15225323). Mutant also demonstrates a lag in the induction of
CC cytotoxicity towards Chinese hamster ovary cells and is attenuated for
CC virulence in a mouse pneumonia model (PubMed:16714561).
CC {ECO:0000269|PubMed:15225323, ECO:0000269|PubMed:16714561,
CC ECO:0000269|PubMed:9045825}.
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DR EMBL; M64975; AAA25814.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG05099.1; -; Genomic_DNA.
DR PIR; A41047; A41047.
DR RefSeq; NP_250401.1; NC_002516.2.
DR RefSeq; WP_003100769.1; NZ_QZGE01000003.1.
DR PDB; 3KXY; X-ray; 2.80 A; A/B/C/D/E/F/G/H/I/J/K/L=1-131.
DR PDBsum; 3KXY; -.
DR AlphaFoldDB; P26995; -.
DR SMR; P26995; -.
DR IntAct; P26995; 1.
DR STRING; 287.DR97_177; -.
DR PaxDb; P26995; -.
DR PRIDE; P26995; -.
DR DNASU; 878452; -.
DR EnsemblBacteria; AAG05099; AAG05099; PA1710.
DR GeneID; 878452; -.
DR KEGG; pae:PA1710; -.
DR PATRIC; fig|208964.12.peg.1772; -.
DR PseudoCAP; PA1710; -.
DR HOGENOM; CLU_1785211_0_0_6; -.
DR OMA; TQSESWE; -.
DR BioCyc; PAER208964:G1FZ6-1741-MON; -.
DR EvolutionaryTrace; P26995; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:PseudoCAP.
DR GO; GO:0030254; P:protein secretion by the type III secretion system; IMP:PseudoCAP.
DR InterPro; IPR010261; Tir_chaperone.
DR Pfam; PF05932; CesT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Reference proteome.
FT CHAIN 1..145
FT /note="Transcriptional anti-antiactivator ExsC"
FT /id="PRO_0000021219"
FT HELIX 3..18
FT /evidence="ECO:0007829|PDB:3KXY"
FT STRAND 29..35
FT /evidence="ECO:0007829|PDB:3KXY"
FT TURN 36..38
FT /evidence="ECO:0007829|PDB:3KXY"
FT STRAND 39..46
FT /evidence="ECO:0007829|PDB:3KXY"
FT TURN 47..50
FT /evidence="ECO:0007829|PDB:3KXY"
FT STRAND 51..60
FT /evidence="ECO:0007829|PDB:3KXY"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:3KXY"
FT HELIX 68..77
FT /evidence="ECO:0007829|PDB:3KXY"
FT HELIX 78..81
FT /evidence="ECO:0007829|PDB:3KXY"
FT STRAND 85..88
FT /evidence="ECO:0007829|PDB:3KXY"
FT TURN 90..92
FT /evidence="ECO:0007829|PDB:3KXY"
FT STRAND 94..102
FT /evidence="ECO:0007829|PDB:3KXY"
FT TURN 103..105
FT /evidence="ECO:0007829|PDB:3KXY"
FT HELIX 108..128
FT /evidence="ECO:0007829|PDB:3KXY"
SQ SEQUENCE 145 AA; 16229 MW; A53BEB27270EA737 CRC64;
MDLTSKVNRL LAEFAGRIGL PSLSLDEEGM ASLLFDEQVG VTLLLLAERE RLLLEADVAG
IDVLGEGIFR QLASFNRHWH RFDLHFGFDE LTGKVQLYAQ ILAAQLTLEC FEATLANLLD
HAEFWQRLLP CDSDREAVAA VGMRV
