ICSB_SHIFL
ID ICSB_SHIFL Reviewed; 494 AA.
AC P33546; Q6XVY5; Q8VSH5; Q9AFS3;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2003, sequence version 2.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=N-epsilon-fatty acyltransferase IcsB {ECO:0000305};
DE EC=2.3.1.- {ECO:0000269|PubMed:30061757};
GN Name=icsB {ECO:0000303|PubMed:1495389}; OrderedLocusNames=CP0132;
OS Shigella flexneri.
OG Plasmid pWR100, Plasmid pCP301, and Plasmid pINV_F6_M1382.
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=1495389; DOI=10.1111/j.1365-2958.1992.tb00885.x;
RA Allaoui A., Mounier J., Prevost M.-C., Sansonetti P.J., Parsot C.;
RT "icsB: a Shigella flexneri virulence gene necessary for the lysis of
RT protrusions during intercellular spread.";
RL Mol. Microbiol. 6:1605-1616(1992).
RN [2]
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 [3]
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 [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-19.
RC STRAIN=M90T / Serotype 5a; PLASMID=pWR100;
RX PubMed=8478058; DOI=10.1128/iai.61.5.1707-1714.1993;
RA Allaoui A., Menard R., Sansonetti P.J., Parsot C.;
RT "Characterization of the Shigella flexneri ipgD and ipgF genes, which are
RT located in the proximal part of the mxi locus.";
RL Infect. Immun. 61:1707-1714(1993).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=301 / Serotype 2a;
RX PubMed=12753186; DOI=10.1046/j.1365-2958.2003.03489.x;
RA Ogawa M., Suzuki T., Tatsuno I., Abe H., Sasakawa C.;
RT "IcsB, secreted via the type III secretion system, is chaperoned by IpgA
RT and required at the post-invasion stage of Shigella pathogenicity.";
RL Mol. Microbiol. 48:913-931(2003).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLUL183R LOCATION, ACTIVE SITES, AND
RP MUTAGENESIS OF HIS-145; LYS-183; ASP-195; TYR-297 AND CYS-306.
RX PubMed=30061757; DOI=10.1038/s41564-018-0215-6;
RA Liu W., Zhou Y., Peng T., Zhou P., Ding X., Li Z., Zhong H., Xu Y.,
RA Chen S., Hang H.C., Shao F.;
RT "Nepsilon-fatty acylation of multiple membrane-associated proteins by
RT Shigella IcsB effector to modulate host function.";
RL Nat. Microbiol. 3:996-1009(2018).
CC -!- FUNCTION: Virulence-associated N-epsilon-fatty acyltransferase that
CC mediates lysine-stearoylation of host Rho GTPase proteins, thereby
CC disrupting the host actin cytoskeleton (PubMed:30061757). Required at
CC the post-invasion stage of Shigella pathogenicity (PubMed:12753186).
CC {ECO:0000269|PubMed:12753186, ECO:0000269|PubMed:30061757}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl-/S-(2E,6E,10E)-geranylgeranyl-L-cysteinyl-[protein] +
CC octadecanoyl-CoA = CoA + H(+) + N(6)-octadecanoyl-L-lysyl-/S-
CC (2E,6E,10E)-geranylgeranyl-L-cysteinyl-[protein];
CC Xref=Rhea:RHEA:59764, Rhea:RHEA-COMP:17935, Rhea:RHEA-COMP:17936,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57394, ChEBI:CHEBI:86021, ChEBI:CHEBI:143206;
CC Evidence={ECO:0000269|PubMed:30061757};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59765;
CC Evidence={ECO:0000269|PubMed:30061757};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12753186}. Host
CC vacuole {ECO:0000269|PubMed:30061757}. Note=Secreted via type III
CC secretion system (PubMed:12753186). Requires IpgA as a chaperone for
CC its stability and secretion (PubMed:12753186). Localizes on Shigella-
CC containing host vacuoles and modifies its substrates there
CC (PubMed:30061757). {ECO:0000269|PubMed:12753186,
CC ECO:0000269|PubMed:30061757}.
CC -!- MISCELLANEOUS: The icsB gene can be read-through into the ipgA gene to
CC create a translational fusion protein. The biological significance of
CC this process is unclear. {ECO:0000269|PubMed:12753186}.
CC -!- SIMILARITY: Belongs to the BopA/IcsB family. {ECO:0000305}.
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DR EMBL; M86530; AAD15221.1; -; Genomic_DNA.
DR EMBL; AL391753; CAC05807.1; -; Genomic_DNA.
DR EMBL; AF348706; AAK18450.1; -; Genomic_DNA.
DR EMBL; AY206439; AAP78995.1; -; Genomic_DNA.
DR EMBL; AF386526; AAL72354.1; -; Genomic_DNA.
DR PIR; S22687; S22687.
DR RefSeq; NP_085294.1; NC_002698.1.
DR RefSeq; NP_858265.1; NC_004851.1.
DR RefSeq; WP_010921665.1; NZ_QWST01000007.1.
DR AlphaFoldDB; P33546; -.
DR IntAct; P33546; 1.
DR STRING; 198214.CP0132; -.
DR SwissLipids; SLP:000001952; -.
DR EnsemblBacteria; AAL72354; AAL72354; SF_p0132.
DR GeneID; 1238057; -.
DR KEGG; sfl:CP0132; -.
DR PATRIC; fig|198214.7.peg.5386; -.
DR HOGENOM; CLU_613784_0_0_6; -.
DR Proteomes; UP000001006; Plasmid pCP301.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR InterPro; IPR011070; Globular_prot_asu/bsu.
DR SUPFAM; SSF56568; SSF56568; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Plasmid; Reference proteome; Secreted; Transferase;
KW Virulence.
FT CHAIN 1..494
FT /note="N-epsilon-fatty acyltransferase IcsB"
FT /id="PRO_0000084149"
FT REGION 171..247
FT /note="Involved in binding IpgA"
FT /evidence="ECO:0000269|PubMed:12753186"
FT ACT_SITE 145
FT /evidence="ECO:0000305|PubMed:30061757"
FT ACT_SITE 195
FT /evidence="ECO:0000305|PubMed:30061757"
FT ACT_SITE 306
FT /evidence="ECO:0000305|PubMed:30061757"
FT VARIANT 2
FT /note="S -> I (in plasmid pCP301 and plasmid
FT pINV_F6_M1382)"
FT VARIANT 30
FT /note="I -> V (in plasmid pINV_F6_M1382)"
FT VARIANT 66
FT /note="E -> A (in plasmid pINV_F6_M1382)"
FT VARIANT 76
FT /note="N -> K (in plasmid pINV_F6_M1382)"
FT VARIANT 94
FT /note="A -> V (in plasmid pINV_F6_M1382)"
FT VARIANT 105
FT /note="R -> K (in plasmid pINV_F6_M1382)"
FT VARIANT 116
FT /note="R -> S (in plasmid pINV_F6_M1382)"
FT VARIANT 202
FT /note="E -> D (in plasmid pCP301 and plasmid
FT pINV_F6_M1382)"
FT VARIANT 269
FT /note="H -> Y (in plasmid pINV_F6_M1382)"
FT VARIANT 285
FT /note="K -> Q (in plasmid pINV_F6_M1382)"
FT VARIANT 336
FT /note="D -> N (in plasmid pINV_F6_M1382)"
FT VARIANT 434
FT /note="T -> S (in plasmid pINV_F6_M1382)"
FT VARIANT 443
FT /note="E -> G (in plasmid pINV_F6_M1382)"
FT VARIANT 450
FT /note="E -> V (in plasmid pINV_F6_M1382)"
FT VARIANT 458
FT /note="I -> T (in plasmid pINV_F6_M1382)"
FT VARIANT 482
FT /note="I -> V (in plasmid pINV_F6_M1382)"
FT MUTAGEN 145
FT /note="H->A: Reduced cytotoxicity."
FT /evidence="ECO:0000269|PubMed:30061757"
FT MUTAGEN 183
FT /note="K->A: Does not affect cytotoxicity."
FT /evidence="ECO:0000269|PubMed:30061757"
FT MUTAGEN 195
FT /note="D->A: Reduced cytotoxicity."
FT /evidence="ECO:0000269|PubMed:30061757"
FT MUTAGEN 297
FT /note="Y->A: Does not affect cytotoxicity."
FT /evidence="ECO:0000269|PubMed:30061757"
FT MUTAGEN 306
FT /note="C->A: Abolished N-epsilon-fatty acyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:30061757"
FT CONFLICT 116
FT /note="R -> A (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 494 AA; 56408 MW; D4D2CC5EEC2B5324 CRC64;
MSLKISNFID ASNTKGPIRV EDTEHGPILI AQKFNLKDLF FRTLSTINAK INSQILNEQL
KNYRLENQKS LLLFLNTLAS EKSAESAFAA YEAAKNSIQH SFTGRDIKLM LNTAERFHGI
GTAKNLERHL VFRCWGNRGI THLGHTSISI KNNLLQEPTH TYLSWYPGGN VTKDTEINYL
FEKRSGYSVD TYKQDKLNMI SEQTAERLDA GQEVRNLLNS KQDQNNNKKI FFPRANQKKD
PYGYWGVSAD KVYIPLSGDN KTKDGKISHN LFGLDETNMS KFICKKKADA FRQLANYKLI
SKSENCAGMA LNVLKAGNSE IYFPLPDVKL VATPNDVYAY ANKVRQRIES LNQSYNEIMK
YIESDFDLSR LTQLRRSYLK SFNKINLIHT PKTFKPLSIS LYKHPTENVS SEDFDAVINA
CHSYLVKSAP SNMTRVLNEL KTEATDKKEE IIEKSIKIID YYNSLKSPDL GTKLYIHDLL
QINKLLLNNS HSNI
