IPGC_SHIFL
ID IPGC_SHIFL Reviewed; 155 AA.
AC P0A2U4; P18008;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Chaperone protein IpgC;
GN Name=ipgC; Synonyms=ippI; OrderedLocusNames=CP0129;
OS Shigella flexneri.
OG Plasmid pWR100, Plasmid pMYSH6000, Plasmid pINV_F6_M1382, and
OG Plasmid pCP301.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=M90T / Serotype 5a; PLASMID=pWR100;
RX PubMed=3071655; DOI=10.1016/0882-4010(88)90062-9;
RA Baudry B., Kaczorek M., Sansonetti P.J.;
RT "Nucleotide sequence of the invasion plasmid antigen B and C genes (ipaB
RT and ipaC) of Shigella flexneri.";
RL Microb. Pathog. 4:345-357(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=M90T / Serotype 5a; PLASMID=pWR100;
RX PubMed=3057506; DOI=10.1073/pnas.85.23.9317;
RA Venkatesan M.M., Buysse J.M., Kopecko D.J.;
RT "Characterization of invasion plasmid antigen genes (ipaBCD) from Shigella
RT flexneri.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:9317-9321(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=YSH6000 / Serotype 2a; PLASMID=pMYSH6000;
RX PubMed=2552264; DOI=10.1111/j.1365-2958.1989.tb00269.x;
RA Sasakawa C., Adler B., Tobe T., Okada N., Nagai S., Komatsu K.,
RA Yoshikawa M.;
RT "Functional organization and nucleotide sequence of virulence region-2 on
RT the large virulence plasmid in Shigella flexneri 2a.";
RL Mol. Microbiol. 3:1191-1201(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=M90T / Serotype 5a; PLASMID=pWR100;
RX PubMed=11115111; DOI=10.1046/j.1365-2958.2000.02179.x;
RA Buchrieser C., Glaser P., Rusniok C., Nedjari H., d'Hauteville H.,
RA Kunst F., Sansonetti P.J., Parsot C.;
RT "The virulence plasmid pWR100 and the repertoire of proteins secreted by
RT the type III secretion apparatus of Shigella flexneri.";
RL Mol. Microbiol. 38:760-771(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=M90T / Serotype 5a; PLASMID=pWR100;
RX PubMed=11292750; DOI=10.1128/iai.69.5.3271-3285.2001;
RA Venkatesan M.M., Goldberg M.B., Rose D.J., Grotbeck E.J., Burland V.,
RA Blattner F.R.;
RT "Complete DNA sequence and analysis of the large virulence plasmid of
RT Shigella flexneri.";
RL Infect. Immun. 69:3271-3285(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=M1382 / Serotype 6; PLASMID=pINV_F6_M1382;
RX PubMed=14573649; DOI=10.1128/iai.71.11.6298-6306.2003;
RA Lan R., Stevenson G., Reeves P.R.;
RT "Comparison of two major forms of the Shigella virulence plasmid pINV:
RT positive selection is a major force driving the divergence.";
RL Infect. Immun. 71:6298-6306(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a; PLASMID=pCP301;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [8]
RP FUNCTION.
RX PubMed=7954817; DOI=10.1016/0092-8674(94)90260-7;
RA Menard R., Sansonetti P., Parsot C., Vasselon T.;
RT "Extracellular association and cytoplasmic partitioning of the IpaB and
RT IpaC invasins of S. flexneri.";
RL Cell 79:515-525(1994).
CC -!- FUNCTION: Assists the correct folding of nascent IpaB. Once it is bound
CC to IpaB, it binds to IpaC and impedes their premature association that
CC would lead to their degradation in the absence of IpcG.
CC {ECO:0000269|PubMed:7954817}.
CC -!- INTERACTION:
CC P0A2U4; P18011: ipaB; NbExp=4; IntAct=EBI-1535618, EBI-490239;
CC P0A2U4; P0A2U4: ipgC; NbExp=3; IntAct=EBI-1535618, EBI-1535618;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the LcrH/SycD chaperone family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M86530; AAD15224.1; -; Genomic_DNA.
DR EMBL; M34849; AAA98423.1; -; Genomic_DNA.
DR EMBL; J04117; AAA26521.1; -; Genomic_DNA.
DR EMBL; X15319; CAA33380.1; -; Genomic_DNA.
DR EMBL; AL391753; CAC05804.1; -; Genomic_DNA.
DR EMBL; AF348706; AAK18447.1; -; Genomic_DNA.
DR EMBL; AY206439; AAP78992.1; -; Genomic_DNA.
DR EMBL; AF386526; AAL72340.1; -; Genomic_DNA.
DR PIR; C34965; C34965.
DR RefSeq; NP_085291.1; NC_002698.1.
DR RefSeq; NP_858262.1; NC_004851.1.
DR RefSeq; WP_000055835.1; NZ_WPGS01000043.1.
DR RefSeq; YP_009062486.1; NC_024996.1.
DR PDB; 3GYZ; X-ray; 2.15 A; A/B=1-151.
DR PDB; 3GZ1; X-ray; 2.15 A; A/B=1-151.
DR PDB; 3GZ2; X-ray; 2.65 A; A/B=1-151.
DR PDB; 3KS2; X-ray; 3.30 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R=10-155.
DR PDB; 6SCB; X-ray; 1.58 A; A/B=10-151.
DR PDB; 7AXY; X-ray; 1.63 A; A/B=10-151.
DR PDB; 7AYW; X-ray; 1.78 A; A/B=10-151.
DR PDB; 7AZV; X-ray; 1.68 A; A/B=10-151.
DR PDB; 7B1U; X-ray; 1.59 A; A/B=10-151.
DR PDB; 7NHW; X-ray; 1.92 A; A/B=10-151.
DR PDB; 7NL8; X-ray; 1.59 A; A/B=10-151.
DR PDB; 7NRG; X-ray; 1.57 A; A/B=10-151.
DR PDB; 7O04; X-ray; 1.74 A; A/B=10-151.
DR PDBsum; 3GYZ; -.
DR PDBsum; 3GZ1; -.
DR PDBsum; 3GZ2; -.
DR PDBsum; 3KS2; -.
DR PDBsum; 6SCB; -.
DR PDBsum; 7AXY; -.
DR PDBsum; 7AYW; -.
DR PDBsum; 7AZV; -.
DR PDBsum; 7B1U; -.
DR PDBsum; 7NHW; -.
DR PDBsum; 7NL8; -.
DR PDBsum; 7NRG; -.
DR PDBsum; 7O04; -.
DR AlphaFoldDB; P0A2U4; -.
DR SASBDB; P0A2U4; -.
DR SMR; P0A2U4; -.
DR DIP; DIP-45500N; -.
DR IntAct; P0A2U4; 2.
DR STRING; 198214.CP0129; -.
DR PRIDE; P0A2U4; -.
DR EnsemblBacteria; AAL72340; AAL72340; SF_p0129.
DR GeneID; 1238043; -.
DR KEGG; sfl:CP0129; -.
DR PATRIC; fig|198214.7.peg.5384; -.
DR HOGENOM; CLU_093829_1_0_6; -.
DR OMA; NEPRFPF; -.
DR EvolutionaryTrace; P0A2U4; -.
DR Proteomes; UP000001006; Plasmid pCP301.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR005415; T3SS_Ca_resp_chp_LcrH/SycD.
DR InterPro; IPR016379; T3SS_Ca_resp_chp_LcrH/SycD_sub.
DR InterPro; IPR011716; TPR-3.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR Pfam; PF07720; TPR_3; 2.
DR PIRSF; PIRSF003165; Chaperone_SicA; 1.
DR PRINTS; PR01595; SYCDCHAPRONE.
DR SUPFAM; SSF48452; SSF48452; 1.
DR TIGRFAMs; TIGR02552; LcrH_SycD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chaperone; Cytoplasm; Plasmid; Reference proteome; Virulence.
FT CHAIN 1..155
FT /note="Chaperone protein IpgC"
FT /id="PRO_0000206484"
FT HELIX 10..20
FT /evidence="ECO:0007829|PDB:6SCB"
FT TURN 25..29
FT /evidence="ECO:0007829|PDB:6SCB"
FT HELIX 33..48
FT /evidence="ECO:0007829|PDB:6SCB"
FT HELIX 52..65
FT /evidence="ECO:0007829|PDB:6SCB"
FT HELIX 70..82
FT /evidence="ECO:0007829|PDB:6SCB"
FT HELIX 86..100
FT /evidence="ECO:0007829|PDB:6SCB"
FT HELIX 105..116
FT /evidence="ECO:0007829|PDB:6SCB"
FT HELIX 120..133
FT /evidence="ECO:0007829|PDB:6SCB"
FT HELIX 137..149
FT /evidence="ECO:0007829|PDB:6SCB"
SQ SEQUENCE 155 AA; 17756 MW; F46E39A92B8ADEC7 CRC64;
MSLNITENES ISTAVIDAIN SGATLKDINA IPDDMMDDIY SYAYDFYNKG RIEEAEVFFR
FLCIYDFYNV DYIMGLAAIY QIKEQFQQAA DLYAVAFALG KNDYTPVFHT GQCQLRLKAP
LKAKECFELV IQHSNDEKLK IKAQSYLDAI QDIKE
