ICSA_SHIFL
ID ICSA_SHIFL Reviewed; 1102 AA.
AC Q7BCK4; Q52298; Q6WE27; Q99Q93;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 125.
DE RecName: Full=Outer membrane protein IcsA autotransporter;
DE Contains:
DE RecName: Full=Outer membrane protein IcsA;
DE Contains:
DE RecName: Full=Outer membrane protein IcsA translocator;
DE Flags: Precursor;
GN Name=icsA; Synonyms=virG; OrderedLocusNames=CP0182;
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=YSH6000 / Serotype 2a; PLASMID=pMYSH6000;
RX PubMed=2644195; DOI=10.1128/jb.171.1.353-359.1989;
RA Lett M.-C., Sasakawa C., Okada N., Sakai T., Makino S., Yamada M.,
RA Komatsu K., Yoshikawa M.;
RT "virG, a plasmid-coded virulence gene of Shigella flexneri: identification
RT of the virG protein and determination of the complete coding sequence.";
RL J. Bacteriol. 171:353-359(1989).
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 [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 [5]
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 [6]
RP PROTEIN SEQUENCE OF 53-56, AND UNIPOLAR LOCALIZATION.
RC STRAIN=M90T / Serotype 5a; PLASMID=pWR100;
RX PubMed=8468279; DOI=10.1128/jb.175.8.2189-2196.1993;
RA Goldberg M.B., Barzu O., Parsot C., Sansonetti P.J.;
RT "Unipolar localization and ATPase activity of IcsA, a Shigella flexneri
RT protein involved in intracellular movement.";
RL J. Bacteriol. 175:2189-2196(1993).
RN [7]
RP PROTEIN SEQUENCE OF 759-766, FUNCTION, AND MUTAGENESIS OF 758-ARG-ARG-759.
RC STRAIN=YSH6000 / Serotype 2a; PLASMID=pMYSH6000;
RX PubMed=7896693; DOI=10.1128/jb.177.7.1719-1726.1995;
RA Fukuda I., Suzuki T., Munakata H., Hayashi N., Katayama E., Yoshikawa M.,
RA Sasakawa C.;
RT "Cleavage of Shigella surface protein VirG occurs at a specific site, but
RT the secretion is not essential for intracellular spreading.";
RL J. Bacteriol. 177:1719-1726(1995).
RN [8]
RP REGULATION BY VIRF.
RC STRAIN=YSH6000 / Serotype 2a; PLASMID=pMYSH6000;
RX PubMed=2474742; DOI=10.1111/j.1365-2958.1989.tb00210.x;
RA Adler B., Sasakawa C., Tobe T., Makino S., Komatsu K., Yoshikawa M.;
RT "A dual transcriptional activation system for the 230 kb plasmid genes
RT coding for virulence-associated antigens of Shigella flexneri.";
RL Mol. Microbiol. 3:627-635(1989).
RN [9]
RP FUNCTION.
RC STRAIN=M90T / Serotype 5a; PLASMID=pWR100;
RX PubMed=2542950; DOI=10.1073/pnas.86.10.3867;
RA Bernardini M.L., Mounier J., d'Hauteville H., Coquis-Rondon M.,
RA Sansonetti P.J.;
RT "Identification of icsA, a plasmid locus of Shigella flexneri that governs
RT bacterial intra- and intercellular spread through interaction with F-
RT actin.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:3867-3871(1989).
RN [10]
RP FUNCTION, PHOSPHORYLATION, AND MUTAGENESIS OF 756-SER--SER-762.
RC STRAIN=M90T / Serotype 5a; PLASMID=pWR100;
RX PubMed=1602963; DOI=10.1111/j.1365-2958.1992.tb01534.x;
RA d'Hauteville H., Sansonetti P.J.;
RT "Phosphorylation of IcsA by cAMP-dependent protein kinase and its effect on
RT intracellular spread of Shigella flexneri.";
RL Mol. Microbiol. 6:833-841(1992).
RN [11]
RP TOPOLOGY OF THE BETA DOMAIN, AND MUTAGENESIS OF ALA-50 AND ALA-52.
RC STRAIN=YSH6000 / Serotype 2a; PLASMID=pMYSH6000;
RX PubMed=8537341; DOI=10.1074/jbc.270.52.30874;
RA Suzuki T., Lett M.-C., Sasakawa C.;
RT "Extracellular transport of VirG protein in Shigella.";
RL J. Biol. Chem. 270:30874-30880(1995).
RN [12]
RP FUNCTION, AND INTERACTION WITH WASL.
RC STRAIN=YSH6000 / Serotype 2a; PLASMID=pMYSH6000;
RX PubMed=9582270; DOI=10.1093/emboj/17.10.2767;
RA Suzuki T., Miki H., Takenawa T., Sasakawa C.;
RT "Neural Wiskott-Aldrich syndrome protein is implicated in the actin-based
RT motility of Shigella flexneri.";
RL EMBO J. 17:2767-2776(1998).
RN [13]
RP ICSA-WASL-ARP2/3 COMPLEX FORMATION.
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a, and M90T / Serotype 5a;
RC PLASMID=pWR100;
RX PubMed=10491394; DOI=10.1083/jcb.146.6.1319;
RA Egile C., Loisel T.P., Laurent V., Li R., Pantaloni D., Sansonetti P.J.,
RA Carlier M.-F.;
RT "Activation of the CDC42 effector N-WASP by the Shigella flexneri IcsA
RT protein promotes actin nucleation by Arp2/3 complex and bacterial actin-
RT based motility.";
RL J. Cell Biol. 146:1319-1332(1999).
RN [14]
RP SUBCELLULAR LOCATION, AND CLEAVAGE BY ICSP.
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a, and M90T / Serotype 5a;
RC PLASMID=pWR100;
RX PubMed=10231492; DOI=10.1046/j.1365-2958.1999.01356.x;
RA Steinhauer J., Agha R., Pham T., Varga A.W., Goldberg M.B.;
RT "The unipolar Shigella surface protein IcsA is targeted directly to the
RT bacterial old pole: IcsP cleavage of IcsA occurs over the entire bacterial
RT surface.";
RL Mol. Microbiol. 32:367-377(1999).
RN [15]
RP POLAR TARGETING, AND MUTAGENESIS BY DOMAIN DELETION.
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a; PLASMID=pWR100;
RX PubMed=11481451; DOI=10.1073/pnas.171310498;
RA Charles M., Perez M., Kobil J.H., Goldberg M.B.;
RT "Polar targeting of Shigella virulence factor IcsA in Enterobacteriacae and
RT Vibrio.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9871-9876(2001).
RN [16]
RP POLAR TARGETING, AND MUTAGENESIS OF GLY-40; LEU-44 AND LEU-45.
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a; PLASMID=pWR100;
RX PubMed=14507362; DOI=10.1046/j.1365-2958.2003.03674.x;
RA Brandon L.D., Goehring N., Janakiraman A., Yan A.W., Wu T., Beckwith J.,
RA Goldberg M.B.;
RT "IcsA, a polarly localized autotransporter with an atypical signal peptide,
RT uses the Sec apparatus for secretion, although the Sec apparatus is
RT circumferentially distributed.";
RL Mol. Microbiol. 50:45-60(2003).
RN [17]
RP FUNCTION, AND MUTAGENESIS BY DOMAIN DELETION.
RC STRAIN=YSH6000 / Serotype 2a; PLASMID=pMYSH6000;
RX PubMed=15576571; DOI=10.1126/science.1106036;
RA Ogawa M., Yoshimori T., Suzuki T., Sagara H., Mizushima N., Sasakawa C.;
RT "Escape of intracellular Shigella from autophagy.";
RL Science 307:727-731(2005).
CC -!- FUNCTION: Essential for bacterial spreading by eliciting polar
CC deposition of filamentous actin (actin-based motility). Inside the host
CC cell mediates nucleation and polymerization of actin molecules on the
CC bacterial surface, which provides the propulsive force for
CC intracellular movement and intercellular dissemination of the
CC bacterium. During invasion of mammalian cells, triggers autophagy by
CC binding to APG5L. Interaction with IcsB leads to escape from the
CC autophagic host defense system. Also binds ATP and displays weak ATPase
CC activity. {ECO:0000269|PubMed:15576571, ECO:0000269|PubMed:1602963,
CC ECO:0000269|PubMed:2542950, ECO:0000269|PubMed:7896693,
CC ECO:0000269|PubMed:9582270}.
CC -!- SUBUNIT: Forms a ternary complex with host WASL (neural Wiskott-Aldrich
CC syndrome protein) and ARP2/3. IcsA enhances the affinity of WASL for
CC ARP2/3, thus assembling a tight complex which has maximal activity in
CC actin assembly. Also binds directly to host vinculin, which may serve
CC as an actin filament recruiter.
CC -!- SUBCELLULAR LOCATION: [Outer membrane protein IcsA autotransporter]:
CC Periplasm.
CC -!- SUBCELLULAR LOCATION: [Outer membrane protein IcsA]: Secreted. Cell
CC surface. Note=The alpha domain is localized as a cap over the old pole
CC of the bacterial surface.
CC -!- SUBCELLULAR LOCATION: [Outer membrane protein IcsA translocator]: Cell
CC outer membrane {ECO:0000305}; Multi-pass membrane protein
CC {ECO:0000305}. Note=The cleaved C-terminal fragment (autotransporter
CC domain) is localized in the outer membrane.
CC -!- INDUCTION: Transcriptionally regulated by VirF.
CC -!- DOMAIN: The signal peptide, cleaved at the inner membrane, guides the
CC autotransporter protein to the periplasmic space. Then, insertion of
CC the C-terminal translocator domain (or beta domain) in the outer
CC membrane forms a hydrophilic pore for the translocation of the
CC passenger domain (or alpha domain) to the bacterial cell surface, where
CC IcsA is cleaved by IcsP (SopA) and released into the extracellular
CC medium. This cleavage is important for the maintenance of the sharply
CC polarized distribution of IcsA but is not a prerequisite for
CC intracellular spreading.
CC -!- DOMAIN: The glycine-rich domain interacts with the WASL CRIB domain.
CC -!- PTM: Phosphorylated by host cAMP-dependent protein kinase, which may
CC represent a host defense mechanism during the invasion process.
CC {ECO:0000269|PubMed:10231492, ECO:0000269|PubMed:1602963}.
CC -!- MISCELLANEOUS: Secretion across inner membrane is dependent on the SecA
CC and SecYEG apparatus. However, the polar localization comes before
CC secretion and is independent of SecA.
CC -!- MISCELLANEOUS: Deletion experiments show that amino acids 58-103, 505-
CC 537 and 507-729 are required for polar localization and that amino
CC acids 102-779 are responsible for interaction with APG5L and IcsB.
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DR EMBL; M22802; AAA26547.1; -; Genomic_DNA.
DR EMBL; AL391753; CAC05837.1; -; Genomic_DNA.
DR EMBL; AF348706; AAK18502.1; -; Genomic_DNA.
DR EMBL; AY294290; AAQ57625.1; -; Genomic_DNA.
DR EMBL; AF386526; AAL72293.1; -; Genomic_DNA.
DR PIR; A32247; A32247.
DR RefSeq; NP_858315.1; NC_004851.1.
DR RefSeq; WP_001071795.1; NZ_WPGT01000147.1.
DR RefSeq; WP_010921691.1; NZ_QWST01000255.1.
DR PDB; 3ML3; X-ray; 2.00 A; A=591-758.
DR PDB; 5KE1; X-ray; 1.90 A; A/B=419-758.
DR PDBsum; 3ML3; -.
DR PDBsum; 5KE1; -.
DR AlphaFoldDB; Q7BCK4; -.
DR SASBDB; Q7BCK4; -.
DR SMR; Q7BCK4; -.
DR STRING; 198214.CP0182; -.
DR TCDB; 1.B.12.1.2; the autotransporter-1 (at-1) family.
DR EnsemblBacteria; AAL72293; AAL72293; SF_p0182.
DR GeneID; 1238021; -.
DR KEGG; sfl:CP0182; -.
DR PATRIC; fig|198214.7.peg.5433; -.
DR HOGENOM; CLU_002551_8_0_6; -.
DR OMA; DAWLQYG; -.
DR PHI-base; PHI:4647; -.
DR Proteomes; UP000001006; Plasmid pCP301.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0051286; C:cell tip; IDA:CACAO.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR CDD; cd01344; PL2_Passenger_AT; 1.
DR Gene3D; 2.160.20.20; -; 1.
DR Gene3D; 2.40.128.130; -; 1.
DR InterPro; IPR043990; AC_1.
DR InterPro; IPR005546; Autotransporte_beta.
DR InterPro; IPR036709; Autotransporte_beta_dom_sf.
DR InterPro; IPR012332; Autotransporter_pectin_lyase_C.
DR InterPro; IPR013425; Autotrns_rpt.
DR InterPro; IPR006315; OM_autotransptr_brl.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR Pfam; PF18883; AC_1; 1.
DR Pfam; PF03797; Autotransporter; 1.
DR Pfam; PF12951; PATR; 1.
DR SMART; SM00869; Autotransporter; 1.
DR SUPFAM; SSF103515; SSF103515; 1.
DR SUPFAM; SSF51126; SSF51126; 1.
DR TIGRFAMs; TIGR01414; autotrans_barl; 1.
DR TIGRFAMs; TIGR02601; autotrns_rpt; 1.
DR PROSITE; PS51208; AUTOTRANSPORTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell outer membrane; Direct protein sequencing; Membrane;
KW Periplasm; Phosphoprotein; Plasmid; Reference proteome; Secreted; Signal;
KW Transmembrane; Transmembrane beta strand; Virulence.
FT SIGNAL 1..52
FT /evidence="ECO:0000269|PubMed:8468279"
FT CHAIN 53..1102
FT /note="Outer membrane protein IcsA autotransporter"
FT /id="PRO_0000387574"
FT CHAIN 53..758
FT /note="Outer membrane protein IcsA"
FT /id="PRO_0000002700"
FT CHAIN 759..1102
FT /note="Outer membrane protein IcsA translocator"
FT /id="PRO_0000002701"
FT TOPO_DOM 53..807
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 808..816
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 817..818
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 819..827
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 828..845
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 846..854
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 855..862
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 863..871
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 872..911
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 912..920
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 921..924
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 925..933
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 934..941
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 942..950
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 951..954
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 955..963
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 964..968
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 969..977
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 978..981
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 982..990
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 991..1002
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1003..1011
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1012..1026
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1027..1035
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1036..1059
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1060..1068
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1069..1071
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1072..1080
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1081..1093
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1094..1102
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT DOMAIN 814..1102
FT /note="Autotransporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00556"
FT REGION 53..758
FT /note="Alpha"
FT REGION 320..433
FT /note="Interaction with APG5L and IcsB"
FT REGION 741..763
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 758..759
FT /note="Cleavage; by IcsP"
FT VARIANT 53
FT /note="T -> I (in plasmid pINV_F6_M1382)"
FT VARIANT 279
FT /note="V -> I (in plasmid pINV_F6_M1382)"
FT VARIANT 667
FT /note="A -> T (in plasmid pINV_F6_M1382)"
FT VARIANT 725
FT /note="V -> A (in plasmid pWR100)"
FT VARIANT 923
FT /note="S -> G (in plasmid pINV_F6_M1382)"
FT VARIANT 961
FT /note="A -> T (in plasmid pINV_F6_M1382)"
FT VARIANT 1000
FT /note="G -> V (in plasmid pINV_F6_M1382)"
FT VARIANT 1016
FT /note="Q -> H (in plasmid pINV_F6_M1382)"
FT MUTAGEN 40
FT /note="G->E: Disrupts targeting to outer membrane."
FT /evidence="ECO:0000269|PubMed:14507362"
FT MUTAGEN 44
FT /note="L->R: Disrupts targeting to outer membrane."
FT /evidence="ECO:0000269|PubMed:14507362"
FT MUTAGEN 45
FT /note="L->R: Disrupts targeting to outer membrane."
FT /evidence="ECO:0000269|PubMed:14507362"
FT MUTAGEN 50
FT /note="A->R: Disrupts targeting to outer membrane."
FT /evidence="ECO:0000269|PubMed:8537341"
FT MUTAGEN 52
FT /note="A->R: Disrupts targeting to outer membrane."
FT /evidence="ECO:0000269|PubMed:8537341"
FT MUTAGEN 756..762
FT /note="SSRRASS->WQDDAPR: Loss of phosphorylation."
FT /evidence="ECO:0000269|PubMed:1602963"
FT MUTAGEN 758..759
FT /note="RR->DD: Abolishes cleavage by IcsP. Loss of
FT phosphorylation."
FT /evidence="ECO:0000269|PubMed:7896693"
FT MUTAGEN 758
FT /note="R->D: Abolishes cleavage by IcsP."
FT MUTAGEN 759
FT /note="R->D: Loss of phosphorylation."
FT STRAND 421..426
FT /evidence="ECO:0007829|PDB:5KE1"
FT STRAND 430..432
FT /evidence="ECO:0007829|PDB:5KE1"
FT STRAND 434..441
FT /evidence="ECO:0007829|PDB:5KE1"
FT HELIX 444..447
FT /evidence="ECO:0007829|PDB:5KE1"
FT HELIX 451..453
FT /evidence="ECO:0007829|PDB:5KE1"
FT STRAND 454..457
FT /evidence="ECO:0007829|PDB:5KE1"
FT STRAND 468..473
FT /evidence="ECO:0007829|PDB:5KE1"
FT STRAND 477..483
FT /evidence="ECO:0007829|PDB:5KE1"
FT HELIX 484..486
FT /evidence="ECO:0007829|PDB:5KE1"
FT STRAND 495..498
FT /evidence="ECO:0007829|PDB:5KE1"
FT STRAND 503..506
FT /evidence="ECO:0007829|PDB:5KE1"
FT STRAND 527..537
FT /evidence="ECO:0007829|PDB:5KE1"
FT STRAND 545..549
FT /evidence="ECO:0007829|PDB:5KE1"
FT STRAND 551..556
FT /evidence="ECO:0007829|PDB:5KE1"
FT STRAND 558..562
FT /evidence="ECO:0007829|PDB:5KE1"
FT STRAND 566..570
FT /evidence="ECO:0007829|PDB:5KE1"
FT STRAND 574..577
FT /evidence="ECO:0007829|PDB:5KE1"
FT STRAND 583..597
FT /evidence="ECO:0007829|PDB:5KE1"
FT STRAND 601..604
FT /evidence="ECO:0007829|PDB:3ML3"
FT STRAND 608..617
FT /evidence="ECO:0007829|PDB:5KE1"
FT STRAND 621..623
FT /evidence="ECO:0007829|PDB:5KE1"
FT HELIX 628..630
FT /evidence="ECO:0007829|PDB:3ML3"
FT STRAND 634..639
FT /evidence="ECO:0007829|PDB:5KE1"
FT STRAND 641..652
FT /evidence="ECO:0007829|PDB:5KE1"
FT STRAND 663..682
FT /evidence="ECO:0007829|PDB:5KE1"
FT STRAND 692..700
FT /evidence="ECO:0007829|PDB:5KE1"
FT STRAND 704..707
FT /evidence="ECO:0007829|PDB:5KE1"
FT STRAND 711..713
FT /evidence="ECO:0007829|PDB:5KE1"
FT STRAND 716..723
FT /evidence="ECO:0007829|PDB:5KE1"
FT STRAND 732..739
FT /evidence="ECO:0007829|PDB:5KE1"
SQ SEQUENCE 1102 AA; 116244 MW; 5F6A1E353B105B9F CRC64;
MNQIHKFFCN MTQCSQGGAG ELPTVKEKTC KLSFSPFVVG ASLLLGGPIA FATPLSGTQE
LHFSEDNYEK LLTPVDGLSP LGAGEDGMDA WYITSSNPSH ASRTKLRINS DIMISAGHGG
AGDNNDGNSC GGNGGDSITG SDLSIINQGM ILGGSGGSGA DHNGDGGEAV TGDNLFIING
EIISGGHGGD SYSDSDGGNG GDAVTGVNLP IINKGTISGG NGGNNYGEGD GGNGGDAITG
SSLSVINKGT FAGGNGGAAY GYGYDGYGGN AITGDNLSVI NNGAILGGNG GHWGDAINGS
NMTIANSGYI ISGKEDDGTQ NVAGNAIHIT GGNNSLILHE GSVITGDVQV NNSSILKIIN
NDYTGTTPTI EGDLCAGDCT TVSLSGNKFT VSGDVSFGEN SSLNLAGISS LEASGNMSFG
NNVKVEAIIN NWAQKDYKLL SADKGITGFS VSNISIINPL LTTGAIDYTK SYISDQNKLI
YGLSWNDTDG DSHGEFNLKE NAELTVSTIL ADNLSHHNIN SWDGKSLTKS GEGTLILAEK
NTYSGFTNIN AGILKMGTVE AMTRTAGVIV NKGATLNFSG MNQTVNTLLN SGTVLINNIN
APFLPDPVIV TGNMTLEKNG HVILNNSSSN VGQTYVQKGN WHGKGGILSL GAVLGNDNSK
TDRLEIAGHA SGITYVAVTN EGGSGDKTLE GVQIISTDSS DKNAFIQKGR IVAGSYDYRL
KQGTVSGLNT NKWYLTSQMD NQESKQMSNQ ESTQMSSRRA SSQLVSSLNL GEGSIHTWRP
EAGSYIANLI AMNTMFSPSL YDRHGSTIVD PTTGQLSETT MWIRTVGGHN EHNLADRQLK
TTANRMVYQI GGDILKTNFT DHDGLHVGIM GAYGYQDSKT HNKYTSYSSR GTVSGYTAGL
YSSWFQDEKE RTGLYMDAWL QYSWFNNTVK GDGLTGEKYS SKGITGALEA GYIYPTIRWT
AHNNIDNALY LNPQVQITRH GVKANDYIEH NGTMVTSSGG NNIQAKLGLR TSLISQSCID
KETLRKFEPF LEVNWKWSSK QYGVIMNGMS NHQIGNRNVI ELKTGVGGRL ADNLSIWGNV
SQQLGNNSYR DTQGILGVKY TF
