IPAB_SHIFL
ID IPAB_SHIFL Reviewed; 580 AA.
AC P18011;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 2.
DT 25-MAY-2022, entry version 148.
DE RecName: Full=Invasin IpaB;
DE AltName: Full=62 kDa antigen;
GN Name=ipaB; OrderedLocusNames=CP0128;
OS Shigella flexneri.
OG Plasmid pWR100, Plasmid pMYSH6000, and 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=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 [4]
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 [5]
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 [6]
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 [7]
RP FUNCTION IN APOPTOSIS.
RX PubMed=9009343; DOI=10.1128/iai.65.2.787-793.1997;
RA Thirumalai K., Kim K.-S., Zychlinsky A.;
RT "IpaB, a Shigella flexneri invasin, colocalizes with interleukin-1 beta-
RT converting enzyme in the cytoplasm of macrophages.";
RL Infect. Immun. 65:787-793(1997).
RN [8]
RP REVIEW.
RX PubMed=11207575; DOI=10.1046/j.1462-5822.2000.00046.x;
RA Tran Van Nhieu G., Bourdet-Sicard R., Dumenil G., Blocker A.,
RA Sansonetti P.J.;
RT "Bacterial signals and cell responses during Shigella entry into epithelial
RT cells.";
RL Cell. Microbiol. 2:187-193(2000).
RN [9]
RP FUNCTION IN ALTERATION OF HOST CELL CYCLE, INTERACTION WITH HOST HUMAN
RP MAD2L2, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASN-61.
RX PubMed=17719540; DOI=10.1016/j.cell.2007.06.043;
RA Iwai H., Kim M., Yoshikawa Y., Ashida H., Ogawa M., Fujita Y., Muller D.,
RA Kirikae T., Jackson P.K., Kotani S., Sasakawa C.;
RT "A bacterial effector targets Mad2L2, an APC inhibitor, to modulate host
RT cell cycling.";
RL Cell 130:611-623(2007).
CC -!- FUNCTION: Effector proteins function to alter host cell physiology and
CC promote bacterial survival in host tissues. Forms a pore with IpaC,
CC which is inserted into the host cell membrane through the Mxi/Spa
CC apparatus, during cell contact. This pore probably allows the
CC translocation of IpaA. IpaB has also been found to be necessary and
CC sufficient to activate macrophage apoptosis by binding to interleukin-1
CC beta converting enzyme (ICE). Has also been shown to be important,
CC along with IpaD, to block or regulate secretion through the Mxi/Spa
CC translocon in the presence or absence of the secretion signal,
CC respectively. Through interaction with host human MAD2L2,
CC constitutively activates the anaphase-promoting complex APC and induces
CC a cell cycle arrest to prevent epithelial renewal in order to promote
CC bacterial colonization. {ECO:0000269|PubMed:17719540,
CC ECO:0000269|PubMed:9009343}.
CC -!- SUBUNIT: Interacts with host human MAD2L2; in the G2/M phase of the
CC cell cycle. {ECO:0000269|PubMed:17719540}.
CC -!- INTERACTION:
CC P18011; P0A2U4: ipgC; NbExp=4; IntAct=EBI-490239, EBI-1535618;
CC P18011; P29452: Casp1; Xeno; NbExp=3; IntAct=EBI-490239, EBI-489700;
CC P18011; P16070: CD44; Xeno; NbExp=4; IntAct=EBI-490239, EBI-490245;
CC P18011; Q9UI95: MAD2L2; Xeno; NbExp=7; IntAct=EBI-490239, EBI-77889;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17719540}. Host cell
CC membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Host
CC nucleus {ECO:0000305|PubMed:17719540}. Note=Secreted through the
CC specialized type-III secretion system Mxi/Spa. Inserted into the host
CC cell membrane. Also secreted into the host cell cytoplasm after the
CC escape of bacteria from phagosome, where it colocalizes with ICE. May
CC localize to host cell nucleus during G2/M phase of the host cell cycle.
CC -!- INDUCTION: Synthesis of this immunogen is repressed at 30 degrees
CC Celsius and restored at 37 degrees Celsius.
CC -!- SIMILARITY: Belongs to the invasin protein B family. {ECO:0000305}.
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DR EMBL; J04117; AAA26522.1; -; Genomic_DNA.
DR EMBL; M34849; AAA98424.1; -; Genomic_DNA.
DR EMBL; AL391753; CAC05803.1; -; Genomic_DNA.
DR EMBL; AF348706; AAK18446.1; -; Genomic_DNA.
DR EMBL; X15319; CAA33381.1; -; Genomic_DNA.
DR EMBL; AF386526; AAL72352.1; -; Genomic_DNA.
DR PIR; A34965; A34965.
DR RefSeq; NP_085290.1; NC_002698.1.
DR RefSeq; NP_858261.1; NC_004851.1.
DR RefSeq; WP_010921663.1; NZ_QWST01000007.1.
DR RefSeq; YP_009062485.1; NC_024996.1.
DR PDB; 3GZ1; X-ray; 2.15 A; P/Q=51-72.
DR PDB; 3GZ2; X-ray; 2.65 A; P=16-72.
DR PDB; 3U0C; X-ray; 2.05 A; A/B=28-226.
DR PDB; 5WKQ; X-ray; 2.10 A; A/B=74-242.
DR PDB; 6KEA; X-ray; 2.35 A; A/B/C/D=49-76.
DR PDBsum; 3GZ1; -.
DR PDBsum; 3GZ2; -.
DR PDBsum; 3U0C; -.
DR PDBsum; 5WKQ; -.
DR PDBsum; 6KEA; -.
DR AlphaFoldDB; P18011; -.
DR SASBDB; P18011; -.
DR SMR; P18011; -.
DR DIP; DIP-45233N; -.
DR IntAct; P18011; 4.
DR STRING; 198214.CP0128; -.
DR PRIDE; P18011; -.
DR EnsemblBacteria; AAL72352; AAL72352; SF_p0128.
DR GeneID; 1238055; -.
DR KEGG; sfl:CP0128; -.
DR PATRIC; fig|198214.7.peg.5383; -.
DR HOGENOM; CLU_027418_0_0_6; -.
DR EvolutionaryTrace; P18011; -.
DR Proteomes; UP000001006; Plasmid pCP301.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR InterPro; IPR032391; SipB_N.
DR InterPro; IPR006972; SseC.
DR InterPro; IPR003895; T3SS_invasion_prot_B.
DR Pfam; PF04888; SseC; 1.
DR Pfam; PF16535; T3SSipB; 1.
DR PRINTS; PR01375; BACINVASINB.
PE 1: Evidence at protein level;
KW 3D-structure; Host cell membrane; Host membrane; Host nucleus; Membrane;
KW Plasmid; Reference proteome; Secreted; Transmembrane; Transmembrane helix;
KW Virulence.
FT CHAIN 1..580
FT /note="Invasin IpaB"
FT /id="PRO_0000219853"
FT TRANSMEM 313..333
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 399..419
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 61..70
FT /note="Mediates interaction with human MAD2L2"
FT VARIANT 18
FT /note="T -> A (in plasmid pMYSH6000 and plasmid pCP301)"
FT MUTAGEN 61
FT /note="N->A: Loss of interaction with human MAD2L2."
FT /evidence="ECO:0000269|PubMed:17719540"
FT CONFLICT 167
FT /note="E -> N (in Ref. 2; AAA26522)"
FT /evidence="ECO:0000305"
FT STRAND 62..67
FT /evidence="ECO:0007829|PDB:6KEA"
FT HELIX 75..90
FT /evidence="ECO:0007829|PDB:3U0C"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:3U0C"
FT HELIX 96..166
FT /evidence="ECO:0007829|PDB:3U0C"
FT HELIX 175..222
FT /evidence="ECO:0007829|PDB:3U0C"
FT HELIX 233..237
FT /evidence="ECO:0007829|PDB:5WKQ"
SQ SEQUENCE 580 AA; 62201 MW; 56325105E4BC0F70 CRC64;
MHNVSTTTTG FPLAKILTST ELGDNTIQAA NDAANKLFSL TIADLTANQN INTTNAHSTS
NILIPELKAP KSLNASSQLT LLIGNLIQIL GEKSLTALTN KITAWKSQQQ ARQQKNLEFS
DKINTLLSET EGLTRDYEKQ INKLKNADSK IKDLENKINQ IQTRLSELDP ESPEKKKLSR
EEIQLTIKKD AAVKDRTLIE QKTLSIHSKL TDKSMQLEKE IDSFSAFSNT ASAEQLSTQQ
KSLTGLASVT QLMATFIQLV GKNNEESLKN DLALFQSLQE SRKTEMERKS DEYAAEVRKA
EELNRVMGCV GKILGALLTI VSVVAAAFSG GASLALAAVG LALMVTDAIV QAATGNSFME
QALNPIMKAV IEPLIKLLSD AFTKMLEGLG VDSKKAKMIG SILGAIAGAL VLVAAVVLVA
TVGKQAAAKL AENIGKIIGK TLTDLIPKFL KNFSSQLDDL ITNAVARLNK FLGAAGDEVI
SKQIISTHLN QAVLLGESVN SATQAGGSVA SAVFQNSAST NLADLTLSKY QVEQLSKYIS
EAIEKFGQLQ EVIADLLASM SNSQANRTDV AKAILQQTTA
