INLB_LISMG
ID INLB_LISMG Reviewed; 630 AA.
AC P0DQD3; P25147; Q9EXG1;
DT 13-FEB-2019, integrated into UniProtKB/Swiss-Prot.
DT 13-FEB-2019, sequence version 1.
DT 03-AUG-2022, entry version 23.
DE RecName: Full=Internalin B {ECO:0000303|PubMed:1905979};
DE Short=InlB;
DE AltName: Full=Invasion protein InlB;
DE Flags: Precursor;
GN Name=inlB;
OS Listeria monocytogenes serotype 1/2a (strain EGD / Mackaness).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=1334565;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], DOMAIN, AND DISRUPTION PHENOTYPE.
RC STRAIN=EGD-SmR / Serovar 1/2a;
RX PubMed=1905979; DOI=10.1016/0092-8674(91)90009-n;
RA Gaillard J.-L., Berche P., Frehel C., Gouin E., Cossart P.;
RT "Entry of L. monocytogenes into cells is mediated by internalin, a repeat
RT protein reminiscent of surface antigens from Gram-positive cocci.";
RL Cell 65:1127-1141(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=EGD / Serovar 1/2a;
RA Hain T., Pashalidis P., Hudel M., Chakraborty T., Domann E.;
RT "Nucleotide sequence of the internalin operon from Listeria monocytogenes
RT EGD.";
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROBABLE FUNCTION IN STIMULATING HOST PI3-KINASE, AND DISRUPTION PHENOTYPE.
RX PubMed=8864117; DOI=10.1126/science.274.5288.780;
RA Ireton K., Payrastre B., Chap H., Ogawa W., Sakaue H., Kasuga M.,
RA Cossart P.;
RT "A role for phosphoinositide 3-kinase in bacterial invasion.";
RL Science 274:780-782(1996).
RN [4]
RP ERRATUM OF PUBMED:8864117, AND CORRECTION OF FIGURE 3.
RA Ireton K., Payrastre B., Chap H., Ogawa W., Sakaue H., Kasuga M.,
RA Cossart P.;
RL Science 275:464-464(1997).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN, AND DISRUPTION PHENOTYPE.
RC STRAIN=EGD-SmR / Serovar 1/2a;
RX PubMed=9282740; DOI=10.1046/j.1365-2958.1997.4621825.x;
RA Braun L., Dramsi S., Dehoux P., Bierne H., Lindahl G., Cossart P.;
RT "InlB: an invasion protein of Listeria monocytogenes with a novel type of
RT surface association.";
RL Mol. Microbiol. 25:285-294(1997).
RN [6]
RP SUBCELLULAR LOCATION, DOMAIN, AND BINDS TO LIPOTEICHOIC ACID.
RC STRAIN=EGD / Mackaness;
RX PubMed=10594817; DOI=10.1046/j.1365-2958.1999.01652.x;
RA Jonquieres R., Bierne H., Fiedler F., Gounon P., Cossart P.;
RT "Interaction between the protein InlB of Listeria monocytogenes and
RT lipoteichoic acid: a novel mechanism of protein association at the surface
RT of Gram-positive bacteria.";
RL Mol. Microbiol. 34:902-914(1999).
RN [7]
RP FUNCTION, INTERACTION WITH MAMMALIAN MET, PROBABLE RECEPTOR, DOMAIN, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=EGD / Mackaness;
RX PubMed=11081636; DOI=10.1016/s0092-8674(00)00141-0;
RA Shen Y., Naujokas M., Park M., Ireton K.;
RT "InIB-dependent internalization of Listeria is mediated by the Met receptor
RT tyrosine kinase.";
RL Cell 103:501-510(2000).
RN [8]
RP FUNCTION, INTERACTION WITH MAMMALIAN C1QBP, AND POSSIBLE RECEPTOR.
RC STRAIN=EGD / Mackaness;
RX PubMed=10747014; DOI=10.1093/emboj/19.7.1458;
RA Braun L., Ghebrehiwet B., Cossart P.;
RT "gC1q-R/p32, a C1q-binding protein, is a receptor for the InlB invasion
RT protein of Listeria monocytogenes.";
RL EMBO J. 19:1458-1466(2000).
RN [9]
RP FUNCTION, SUBUNIT, DOMAIN, AND DISRUPTION PHENOTYPE.
RC STRAIN=EGD / Mackaness;
RX PubMed=15049825; DOI=10.1111/j.1365-2958.2003.03968.x;
RA Banerjee M., Copp J., Vuga D., Marino M., Chapman T., van der Geer P.,
RA Ghosh P.;
RT "GW domains of the Listeria monocytogenes invasion protein InlB are
RT required for potentiation of Met activation.";
RL Mol. Microbiol. 52:257-271(2004).
RN [10]
RP INTERACTION WITH HUMAN MUC2.
RX PubMed=18327567; DOI=10.1007/s00203-008-0358-6;
RA Linden S.K., Bierne H., Sabet C., Png C.W., Florin T.H., McGuckin M.A.,
RA Cossart P.;
RT "Listeria monocytogenes internalins bind to the human intestinal mucin
RT MUC2.";
RL Arch. Microbiol. 190:101-104(2008).
RN [11] {ECO:0007744|PDB:1D0B}
RP X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) OF 36-248 IN COMPLEX WITH CALCIUM,
RP COFACTOR, AND DOMAIN.
RC STRAIN=EGD-SmR / Serovar 1/2a;
RX PubMed=10635330; DOI=10.1016/s1097-2765(00)80234-8;
RA Marino M., Braun L., Cossart P., Ghosh P.;
RT "Structure of the inlB leucine-rich repeats, a domain that triggers host
RT cell invasion by the bacterial pathogen L. monocytogenes.";
RL Mol. Cell 4:1063-1072(1999).
RN [12] {ECO:0007744|PDB:1M9S}
RP X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 36-630, INTERACTION WITH HUMAN
RP C1QBP, DOMAIN, AND HEPARIN-BINDING.
RC STRAIN=EGD / Mackaness;
RX PubMed=12411480; DOI=10.1093/emboj/cdf558;
RA Marino M., Banerjee M., Jonquieres R., Cossart P., Ghosh P.;
RT "GW domains of the Listeria monocytogenes invasion protein InlB are SH3-
RT like and mediate binding to host ligands.";
RL EMBO J. 21:5623-5634(2002).
RN [13] {ECO:0007744|PDB:1OTM, ECO:0007744|PDB:1OTN, ECO:0007744|PDB:1OTO}
RP X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 36-248 MUTANTS FOR
RP CALCIUM-BINDING, COFACTOR, DOMAIN, AND MUTAGENESIS OF 51-ASP--ASP-59;
RP ASP-51 AND ASP-59.
RC STRAIN=EGD / Mackaness;
RX PubMed=15020228; DOI=10.1016/j.bbrc.2004.02.064;
RA Marino M., Banerjee M., Copp J., Dramsi S., Chapman T., van der Geer P.,
RA Cossart P., Ghosh P.;
RT "Characterization of the calcium-binding sites of Listeria monocytogenes
RT InlB.";
RL Biochem. Biophys. Res. Commun. 316:379-386(2004).
CC -!- FUNCTION: Mediates the entry of L.monocytogenes into normally non-
CC phagocytic mammalian host cells (Probable) (PubMed:9282740,
CC PubMed:11081636). Its host receptor is hepatocyte growth factor
CC receptor (HGF receptor, a tyrosine kinase, MET) which is tyrosine-
CC phosphorylated in response to InlB in human, green monkey, mouse and
CC dog cell lines (PubMed:11081636, PubMed:15049825). Downstream adapter
CC proteins GAB1 and CBL are phosphorylated in response to InlB, which
CC also causes cell colony scattering (PubMed:11081636). InlB binding to
CC mammalian cells is saturable and inhibited by EDTA; InlB-coated beads
CC can be taken up by host cells (PubMed:10747014). Complement component 1
CC Q subcomponent-binding protein (gC1q-R, C1QBP) might act as an InlB
CC receptor, leading to activation of PI3-kinase in green monkey cells
CC (PubMed:10747014). Stimulation of Tyr-phosphorylation by InlB is
CC antagonized by C1QBP, showing that potentiation of MET signaling via
CC the GW domains is not mediated by C1QBP; the exact role of C1QBP
CC remains to be determined (PubMed:15049825). Stimulation of Tyr-
CC phosphorylation of MET by InlB is potentiated by the InlB GW domains
CC and glycosaminoglycans such as heparin; exogenously added InlB, or
CC hepatocyte growth factor (HGF) will also substitute for bacterial InlB,
CC suggesting InlB promotes bacterial invasion by mimicking the hormone
CC HGF (PubMed:15049825). May stimulate phosphatidylinositol 4,5-
CC bisphosphate 3-kinase (PI3-kinase) in green monkey cells, has less
CC effect in humans as PI3-kinase is constitutively and highly expressed
CC in Caco cells (Probable). Binds heparin; C1QBP and heparin seem to bind
CC to the GW domains (PubMed:12411480). {ECO:0000269|PubMed:10747014,
CC ECO:0000269|PubMed:11081636, ECO:0000269|PubMed:12411480,
CC ECO:0000269|PubMed:15049825, ECO:0000269|PubMed:9282740,
CC ECO:0000305|PubMed:11081636, ECO:0000305|PubMed:1905979,
CC ECO:0000305|PubMed:8864117}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:10635330, ECO:0000269|PubMed:15020228};
CC Note=Binds 2 Ca(2+) ions; binding site 1 has a 10-fold higher affinity
CC binding site 2 (PubMed:10635330, PubMed:15020228). Loss of Ca(2+)-
CC binding has no measurable effect on host receptor activation or
CC invasion by Listeria, suggesting ion-binding is fortuitous
CC (PubMed:15020228). {ECO:0000269|PubMed:10635330,
CC ECO:0000269|PubMed:15020228};
CC -!- SUBUNIT: Monomer (PubMed:15049825). Interacts via its LRR repeats with
CC the extracellular portion of mammalian host MET; MET can bind HGF, its
CC endogenous ligand, and InlB simultaneously (PubMed:11081636). Probably
CC forms a dimer upon interaction with host MET, which subsequently allows
CC dimerization of the host MET and subsequent host signaling;
CC dimerization probably occurs via the convex surface of InlB (By
CC similarity). Interacts with host complement component 1 Q subcomponent-
CC binding protein (C1QBP) (PubMed:10747014, PubMed:12411480). Interacts
CC in vitro with human intestinal mucin-2 (MUC2) but not with mucin-1
CC (PubMed:18327567). {ECO:0000250|UniProtKB:P0DQD2,
CC ECO:0000269|PubMed:10747014, ECO:0000269|PubMed:11081636,
CC ECO:0000269|PubMed:12411480, ECO:0000269|PubMed:15049825,
CC ECO:0000269|PubMed:18327567}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10594817,
CC ECO:0000269|PubMed:9282740}. Cell surface {ECO:0000269|PubMed:9282740}.
CC Cell membrane {ECO:0000269|PubMed:10594817}. Note=Approximately half
CC the protein is secreted (PubMed:9282740, PubMed:10594817). Cell surface
CC association is mediated by the GW domains and can occur when protein is
CC added externally; externally added protein confers invasion competence
CC (PubMed:9282740, PubMed:10594817, PubMed:15049825). Replacement of the
CC GW region with that of the Ami protein, which has 8 GW domains,
CC localizes all the protein to the cell surface (PubMed:9282740,
CC PubMed:10594817). Replacement of the GW region with GW5 and 6 of the
CC Ami protein restores cell invasion when bacteria plus protein are added
CC externally (PubMed:15049825). Protein is homogenously distributed but
CC partially buried in the cell membrane; it binds non-covalently to
CC lipoteichoic acid (LTA) on the bacterial membrane, and can be released
CC from the surface by LTA (PubMed:10594817).
CC {ECO:0000269|PubMed:10594817, ECO:0000269|PubMed:15049825,
CC ECO:0000269|PubMed:9282740}.
CC -!- DOMAIN: Has an N-terminal region with 8 leucine-rich repeats (LRR) and
CC has 3 GW repeats in the C-terminus (Probable). Residues 241-319 form an
CC Ig-like region, followed by a 72 residue-long flexible B repeat region
CC (PubMed:12411480) (Probable). The GW repeats mediate non-covalent
CC binding of the protein to lipoteichoic acid (LTA) on the bacterial
CC membrane (PubMed:10594817). The GW domain mediates binding to host
CC complement component 1 Q subcomponent-binding protein (gC1q-R, C1QBP)
CC and to heparin; heparin binding dissociates InlB from the bacterial
CC surface (PubMed:12411480). The LRR domain forms a curved tube, the N-
CC terminus of which has a cap that binds 2 Ca(2+) ions (PubMed:10635330,
CC PubMed:15020228). The LRR domain alone (31-241) binds mammalian MET and
CC stimulates its Tyr-phosphorylation; the LRR plus Ig-like region (31-
CC 321) are required for receptor dimerization, and the GW domains,
CC especially GW2 and GW3, potentiate MET activation (PubMed:11081636,
CC PubMed:15049825). {ECO:0000269|PubMed:10594817,
CC ECO:0000269|PubMed:10635330, ECO:0000269|PubMed:11081636,
CC ECO:0000269|PubMed:12411480, ECO:0000269|PubMed:15020228,
CC ECO:0000269|PubMed:15049825, ECO:0000305|PubMed:15049825,
CC ECO:0000305|PubMed:1905979, ECO:0000305|PubMed:9282740}.
CC -!- DISRUPTION PHENOTYPE: Deletion of both inlA and inlB prevents uptake of
CC Listeria by human enterocyte-like cell line Caco-2 (PubMed:1905979).
CC Single inlB deletion no longer invades various cell lines
CC (PubMed:9282740, PubMed:15049825, PubMed:8864117). Decreased synthesis
CC of phosphatidylinositol 3,4,5-trisphosphate (PIP3) in green monkey
CC cells, decreased infection of host cells, decreased association of host
CC PI3-kinase catalytic subunit with tyrosine-phosphorylated proteins
CC (PubMed:8864117). Deletion no longer Tyr-phosphorylates mammalian MET
CC (PubMed:11081636, PubMed:15049825). {ECO:0000269|PubMed:11081636,
CC ECO:0000269|PubMed:15049825, ECO:0000269|PubMed:1905979,
CC ECO:0000269|PubMed:8864117, ECO:0000269|PubMed:9282740}.
CC -!- SIMILARITY: Belongs to the internalin 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; M67471; AAA25290.1; -; Genomic_DNA.
DR EMBL; AJ012346; CAC20629.1; -; Genomic_DNA.
DR PIR; C39930; C39930.
DR RefSeq; WP_014930830.1; NC_022568.1.
DR PDB; 1D0B; X-ray; 1.86 A; A=36-248.
DR PDB; 1M9S; X-ray; 2.65 A; A=36-630.
DR PDB; 1OTM; X-ray; 1.93 A; A=36-248.
DR PDB; 1OTN; X-ray; 1.97 A; A=36-248.
DR PDB; 1OTO; X-ray; 1.96 A; A=36-248.
DR PDB; 6GCU; X-ray; 6.00 A; B/E=36-321.
DR PDB; 6U12; X-ray; 1.56 A; A=36-248.
DR PDBsum; 1D0B; -.
DR PDBsum; 1M9S; -.
DR PDBsum; 1OTM; -.
DR PDBsum; 1OTN; -.
DR PDBsum; 1OTO; -.
DR PDBsum; 6GCU; -.
DR PDBsum; 6U12; -.
DR AlphaFoldDB; P0DQD3; -.
DR SASBDB; P0DQD3; -.
DR SMR; P0DQD3; -.
DR ABCD; P0DQD3; 12 sequenced antibodies.
DR Reactome; R-HSA-8875360; InlB-mediated entry of Listeria monocytogenes into host cell.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 2.30.30.170; -; 3.
DR Gene3D; 2.60.40.1220; -; 1.
DR Gene3D; 2.60.40.4270; -; 1.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR014755; Cu-Rt/internalin_Ig-like.
DR InterPro; IPR025987; GW_dom.
DR InterPro; IPR038200; GW_dom_sf.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR024634; Internalin_N.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR025875; Leu-rich_rpt_4.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR013378; Listeria/Bacterioides_rpt.
DR InterPro; IPR042229; Listeria/Bacterioides_rpt_sf.
DR InterPro; IPR012569; LRR-contain_adjacent_dom.
DR InterPro; IPR032675; LRR_dom_sf.
DR Pfam; PF09479; Flg_new; 1.
DR Pfam; PF13457; GW; 3.
DR Pfam; PF12354; Internalin_N; 1.
DR Pfam; PF12799; LRR_4; 1.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF08191; LRR_adjacent; 1.
DR SMART; SM00369; LRR_TYP; 5.
DR SUPFAM; SSF81296; SSF81296; 1.
DR TIGRFAMs; TIGR02543; List_Bact_rpt; 1.
DR PROSITE; PS51780; GW; 3.
DR PROSITE; PS51450; LRR; 6.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Cell membrane; Heparin-binding; Leucine-rich repeat;
KW Lipid-binding; Membrane; Metal-binding; Repeat; Secreted; Signal;
KW Virulence.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..630
FT /note="Internalin B"
FT /id="PRO_0000446289"
FT DOMAIN 31..76
FT /note="LRRNT"
FT REPEAT 75..97
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 98..121
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 123..141
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 142..163
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 164..187
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 189..207
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 208..231
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT DOMAIN 241..330
FT /note="LRRCT"
FT DOMAIN 393..467
FT /note="GW 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01116"
FT DOMAIN 472..550
FT /note="GW 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01116"
FT DOMAIN 553..630
FT /note="GW 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01116"
FT REGION 241..319
FT /note="Ig-like region"
FT /evidence="ECO:0000305|PubMed:12411480,
FT ECO:0000305|PubMed:15049825"
FT REGION 320..392
FT /note="B repeat region"
FT /evidence="ECO:0000305|PubMed:12411480,
FT ECO:0000305|PubMed:15049825"
FT REGION 399..630
FT /note="GW repeat region, necessary and sufficient for cell
FT surface attachment, interacts with host C1QBP and with
FT heparin"
FT /evidence="ECO:0000269|PubMed:10594817,
FT ECO:0000269|PubMed:12411480, ECO:0000269|PubMed:9282740,
FT ECO:0000303|PubMed:1905979"
FT BINDING 49
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:10635330,
FT ECO:0000269|PubMed:15020228, ECO:0007744|PDB:1D0B,
FT ECO:0007744|PDB:1OTO"
FT BINDING 51
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:10635330,
FT ECO:0000269|PubMed:15020228, ECO:0007744|PDB:1D0B,
FT ECO:0007744|PDB:1OTO"
FT BINDING 55
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:10635330,
FT ECO:0000269|PubMed:15020228, ECO:0007744|PDB:1D0B,
FT ECO:0007744|PDB:1OTN"
FT BINDING 59
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:10635330,
FT ECO:0000269|PubMed:15020228, ECO:0007744|PDB:1D0B,
FT ECO:0007744|PDB:1OTN"
FT MUTAGEN 51..59
FT /note="DAFAETIKD->AAFAETIKA: No Ca(2+) binding, no change
FT in Tyr-phosphorylation of host MET, wild-type invasion of
FT host Vero cells."
FT /evidence="ECO:0000269|PubMed:15020228"
FT MUTAGEN 51
FT /note="D->A: Only binds 1 Ca(2+), no change in Tyr-
FT phosphorylation of host MET, wild-type invasion of host
FT Vero cells."
FT /evidence="ECO:0000269|PubMed:15020228"
FT MUTAGEN 59
FT /note="D->A: No Ca(2+) binding, no change in Tyr-
FT phosphorylation of host MET, wild-type invasion of host
FT Vero cells."
FT /evidence="ECO:0000269|PubMed:15020228"
FT CONFLICT 41
FT /note="S -> P (in Ref. 2; CAC20629)"
FT CONFLICT 49
FT /note="P -> S (in Ref. 2; CAC20629)"
FT CONFLICT 117
FT /note="T -> A (in Ref. 2; CAC20629)"
FT CONFLICT 132
FT /note="I -> V (in Ref. 2; CAC20629)"
FT CONFLICT 396
FT /note="T -> A (in Ref. 2; CAC20629)"
FT HELIX 44..47
FT /evidence="ECO:0007829|PDB:6U12"
FT HELIX 51..60
FT /evidence="ECO:0007829|PDB:6U12"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:6U12"
FT HELIX 72..76
FT /evidence="ECO:0007829|PDB:6U12"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:6U12"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:6U12"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:6U12"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:6U12"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:6U12"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:6U12"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:6U12"
FT HELIX 158..162
FT /evidence="ECO:0007829|PDB:6U12"
FT STRAND 167..170
FT /evidence="ECO:0007829|PDB:6U12"
FT HELIX 180..184
FT /evidence="ECO:0007829|PDB:6U12"
FT STRAND 189..192
FT /evidence="ECO:0007829|PDB:6U12"
FT HELIX 202..204
FT /evidence="ECO:0007829|PDB:6U12"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:6U12"
FT HELIX 224..226
FT /evidence="ECO:0007829|PDB:6U12"
FT STRAND 233..236
FT /evidence="ECO:0007829|PDB:6U12"
SQ SEQUENCE 630 AA; 71221 MW; EFBDCF52DBAF0C45 CRC64;
MKEKHNPRRK YCLISGLAII FSLWIIIGNG AKVQAETITV STPIKQIFPD DAFAETIKDN
LKKKSVTDAV TQNELNSIDQ IIANNSDIKS VQGIQYLPNV TKLFLNGNKL TDIKPLTNLK
NLGWLFLDEN KIKDLSSLKD LKKLKSLSLE HNGISDINGL VHLPQLESLY LGNNKITDIT
VLSRLTKLDT LSLEDNQISD IVPLAGLTKL QNLYLSKNHI SDLRALAGLK NLDVLELFSQ
ECLNKPINHQ SNLVVPNTVK NTDGSLVTPE IISDDGDYEK PNVKWHLPEF TNEVSFIFYQ
PVTIGKAKAR FHGRVTQPLK EVYTVSYDVD GTVIKTKVEA GTRITAPKPP TKQGYVFKGW
YTEKNGGHEW NFNTDYMSGN DFTLYAVFKA ETTEKTVNLT RYVKYIRGNA GIYKLPREDN
SLKQGTLASH RCKALTVDRE ARNGGKLWYR LKNIGWTKAE NLSLDRYDKM EYDKGVTAYA
RVRNASGNSV WTKPYNTAGA KHVNKLSVYQ GKNMRILREA KTPITTWYQF SIGGKVIGWV
DTRALNTFYK QSMEKPTRLT RYVSANKAGE SYYKVPVADN PVKRGTLAKY KNQKLIVDCQ
ATIEGQLWYR IRTSSTFIGW TKAANLRAQK
