ID INLB_LISMO Reviewed; 630 AA.
AC P0DQD2; P25147; Q9EXG1;
DT 13-FEB-2019, integrated into UniProtKB/Swiss-Prot.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Internalin B;
DE Short=InlB;
DE AltName: Full=Invasion protein InlB;
DE Flags: Precursor;
GN Name=inlB; OrderedLocusNames=lmo0434;
OS Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=169963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).
RN [2]
RP SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=11929538; DOI=10.1046/j.1365-2958.2002.02798.x;
RA Bierne H., Mazmanian S.K., Trost M., Pucciarelli M.G., Liu G., Dehoux P.,
RA Jansch L., Garcia-del Portillo F., Schneewind O., Cossart P.;
RT "Inactivation of the srtA gene in Listeria monocytogenes inhibits anchoring
RT of surface proteins and affects virulence.";
RL Mol. Microbiol. 43:869-881(2002).
RN [3]
RP FUNCTION, DOMAIN, AND MUTAGENESIS OF THR-332; 334-ILE--THR-336 AND THR-336.
RX PubMed=27789707; DOI=10.1074/jbc.m116.746685;
RA Bleymueller W.M., Laemmermann N., Ebbes M., Maynard D., Geerds C.,
RA Niemann H.H.;
RT "MET-activating residues in the B-repeat of the Listeria monocytogenes
RT invasion protein InlB.";
RL J. Biol. Chem. 291:25567-25577(2016).
RN [4] {ECO:0007744|PDB:1H6T}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 36-321, AND DOMAIN.
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=11575932; DOI=10.1006/jmbi.2001.4989;
RA Schubert W.D., Goebel G., Diepholz M., Darji A., Kloer D., Hain T.,
RA Chakraborty T., Wehland J., Domann E., Heinz D.W.;
RT "Internalins from the human pathogen Listeria monocytogenes combine three
RT distinct folds into a contiguous internalin domain.";
RL J. Mol. Biol. 312:783-794(2001).
RN [5] {ECO:0007744|PDB:2UZX, ECO:0007744|PDB:2UZY}
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 36-321 IN COMPLEX WITH HUMAN MET,
RP INTERACTION WITH HUMAN MET, AND DOMAIN.
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=17662939; DOI=10.1016/j.cell.2007.05.037;
RA Niemann H.H., Jager V., Butler P.J., van den Heuvel J., Schmidt S.,
RA Ferraris D., Gherardi E., Heinz D.W.;
RT "Structure of the human receptor tyrosine kinase Met in complex with the
RT Listeria invasion protein InlB.";
RL Cell 130:235-246(2007).
RN [6] {ECO:0007744|PDB:2WQU, ECO:0007744|PDB:2WQV, ECO:0007744|PDB:2WQW, ECO:0007744|PDB:2WQX}
RP X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) OF 36-321, FUNCTION, SUBUNIT,
RP DOMAIN, AND MUTAGENESIS OF 199-SER--ALA-227; 200-ASP--ALA-227 AND
RP 206-GLY--ALA-227.
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=19900460; DOI=10.1016/j.jmb.2009.10.074;
RA Ferraris D.M., Gherardi E., Di Y., Heinz D.W., Niemann H.H.;
RT "Ligand-mediated dimerization of the Met receptor tyrosine kinase by the
RT bacterial invasion protein InlB.";
RL J. Mol. Biol. 395:522-532(2010).
RN [7] {ECO:0007744|PDB:2Y5P, ECO:0007744|PDB:2Y5Q}
RP X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 36-392, X-RAY CRYSTALLOGRAPHY
RP (1.30 ANGSTROMS) OF 322-392, FUNCTION, AND DOMAIN.
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=21345802; DOI=10.1074/jbc.m110.189951;
RA Ebbes M., Bleymuller W.M., Cernescu M., Nolker R., Brutschy B.,
RA Niemann H.H.;
RT "Fold and function of the InlB B-repeat.";
RL J. Biol. Chem. 286:15496-15506(2011).
RN [8] {ECO:0007744|PDB:4AW4}
RP X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 36-321 WITH EXTRA LRR REPEAT,
RP SUBUNIT, DOMAIN, AND MUTAGENESIS OF GLN-95.
RX PubMed=22887347; DOI=10.1002/pro.2142;
RA Niemann H.H., Gherardi E., Bleymuller W.M., Heinz D.W.;
RT "Engineered variants of InlB with an additional leucine-rich repeat
RT discriminate between physiologically relevant and packing contacts in
RT crystal structures of the InlB:MET complex.";
RL Protein Sci. 21:1528-1539(2012).
CC -!- FUNCTION: Mediates the entry of L.monocytogenes into normally non-
CC phagocytic mammalian host cells (PubMed:19900460). Its host receptor is
CC hepatocyte growth factor receptor (HGF receptor, a tyrosine kinase,
CC MET) which is tyrosine-phosphorylated in response to InlB. Downstream
CC targets MAPK1/MAPK3 (Erk1/2) and AKT are phosphorylated in response to
CC InlB, which also causes cell colony scattering (PubMed:19900460,
CC PubMed:21345802, PubMed:22887347, PubMed:27789707). Complement
CC component 1 Q subcomponent-binding protein (gC1q-R, C1QBP) has been
CC suggested to also act an InlB receptor, but this is less certain.
CC Stimulation of Tyr-phosphorylation of MET by InlB is potentiated by the
CC InlB GW domains and glycosaminoglycans such as heparin (By similarity).
CC {ECO:0000250|UniProtKB:P0DQD3, ECO:0000269|PubMed:19900460,
CC ECO:0000269|PubMed:21345802, ECO:0000269|PubMed:22887347,
CC ECO:0000269|PubMed:27789707}.
CC -!- SUBUNIT: Interacts via its LRR repeats plus the Ig-like region with the
CC extracellular portion (residues 25-741) of its receptor MET; MET can
CC bind HGF, its endogenous ligand, and InlB simultaneously
CC (PubMed:17662939). Probably forms a dimer upon interaction with host
CC MET, which subsequently allows dimerization of the host MET and
CC subsequent host signaling; dimerization probably occurs via the convex
CC surface of InlB (PubMed:19900460) (Probable). Prevention of
CC dimerization does not block interaction with MET but prevents
CC downstream action (PubMed:19900460). {ECO:0000269|PubMed:17662939,
CC ECO:0000269|PubMed:19900460, ECO:0000305|PubMed:22887347}.
CC -!- INTERACTION:
CC P0DQD2; Q9MZE0: C1QBP; Xeno; NbExp=3; IntAct=EBI-1379295, EBI-6375765;
CC P0DQD2; P08581: MET; Xeno; NbExp=4; IntAct=EBI-1379295, EBI-1039152;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P0DQD3}.
CC Cytoplasm {ECO:0000269|PubMed:11929538}. Cell membrane
CC {ECO:0000269|PubMed:11929538}. Note=Approximately half the protein is
CC secreted. Cell surface association is mediated by the GW domains and
CC can occur when protein is added externally; externally added protein
CC confers invasion competence. Protein is partially buried in the cell
CC membrane; it binds non-covalently to lipoteichoic acid (LTA) on the
CC bacterial membrane, and can be released from the surface by LTA.
CC {ECO:0000250|UniProtKB:P0DQD3}.
CC -!- DOMAIN: The N-terminus (36-79) resembles a truncated EF hand, the LRR
CC region (80-240) has a curved form, while residues 241-321 form an Ig-
CC like region; the whole region forms a curved tube (PubMed:11575932,
CC PubMed:17662939, PubMed:19900460). The LRR domain alone (31-241) binds
CC mammalian MET and stimulates its Tyr-phosphorylation; the LRR plus Ig-
CC like region (36-321) are required for receptor dimerization; adding the
CC B-repeat allows the protein to scatter host cell colonies, and the GW
CC domains, especially GW2 and GW3, potentiate MET activation
CC (PubMed:17662939, PubMed:21345802). The cap, LRR and Ig-like regions
CC all interact with residues 25-656 of host MET (the Sema, PSI and Ig1
CC domains) via the interior (concave surface) of the curved tube
CC (PubMed:17662939). Dimerizes via the exterior (convex surface) of the
CC curved tube which probably induces host receptor dimerization;
CC preventing dimerization prevents host downstream signaling
CC (PubMed:19900460) (Probable). The B repeat region crystallizes in a
CC SUMO-like fold. The B repeat region interacts synergistically with N-
CC terminus of InlB, conferring on it the ability to stimulate cell
CC motility; the B repeat does not bind to MET (PubMed:21345802). Deletion
CC of the B-repeat (exact residues are not given) slightly decreased
CC protein activity in host; the authors suggest the B-repeat probably
CC contributes to homodimerization rather than binding another host cell
CC receptor (PubMed:27789707). {ECO:0000269|PubMed:11575932,
CC ECO:0000269|PubMed:17662939, ECO:0000269|PubMed:19900460,
CC ECO:0000269|PubMed:21345802, ECO:0000269|PubMed:27789707,
CC ECO:0000305|PubMed:22887347}.
CC -!- DISRUPTION PHENOTYPE: Deletion of inlB alone decreases host cell entry;
CC the reduction varies from 99% to 37% depending on the cell line tested.
CC {ECO:0000269|PubMed:11929538}.
CC -!- SIMILARITY: Belongs to the internalin family. {ECO:0000305}.
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DR EMBL; AL591975; CAC98513.1; -; Genomic_DNA.
DR PIR; AC1129; AC1129.
DR RefSeq; NP_463963.1; NC_003210.1.
DR RefSeq; WP_010989463.1; NZ_CP023861.1.
DR PDB; 1H6T; X-ray; 1.60 A; A=36-321.
DR PDB; 2UZX; X-ray; 2.80 A; A/C=36-321.
DR PDB; 2UZY; X-ray; 4.00 A; A/C=36-321.
DR PDB; 2WQU; X-ray; 2.60 A; A/B/C/D/E/F=36-321.
DR PDB; 2WQV; X-ray; 2.80 A; A/B=36-321.
DR PDB; 2WQW; X-ray; 2.24 A; A/B=36-321.
DR PDB; 2WQX; X-ray; 2.03 A; A/B=36-321.
DR PDB; 2Y5P; X-ray; 1.30 A; A/B/C/D=322-392.
DR PDB; 2Y5Q; X-ray; 3.20 A; A=36-392.
DR PDB; 4AW4; X-ray; 1.93 A; A/B/C=36-321.
DR PDB; 4CIL; X-ray; 1.50 A; A=93-321.
DR PDB; 6DBF; X-ray; 1.55 A; A=36-248.
DR PDB; 6DBG; X-ray; 1.51 A; A/B=36-321.
DR PDB; 7NMS; X-ray; 1.80 A; A=36-392.
DR PDB; 7PV8; X-ray; 2.05 A; A=36-392.
DR PDB; 7PV9; X-ray; 3.30 A; A/B/C=36-392.
DR PDBsum; 1H6T; -.
DR PDBsum; 2UZX; -.
DR PDBsum; 2UZY; -.
DR PDBsum; 2WQU; -.
DR PDBsum; 2WQV; -.
DR PDBsum; 2WQW; -.
DR PDBsum; 2WQX; -.
DR PDBsum; 2Y5P; -.
DR PDBsum; 2Y5Q; -.
DR PDBsum; 4AW4; -.
DR PDBsum; 4CIL; -.
DR PDBsum; 6DBF; -.
DR PDBsum; 6DBG; -.
DR PDBsum; 7NMS; -.
DR PDBsum; 7PV8; -.
DR PDBsum; 7PV9; -.
DR AlphaFoldDB; P0DQD2; -.
DR SMR; P0DQD2; -.
DR IntAct; P0DQD2; 2.
DR STRING; 169963.gene:17593085; -.
DR PaxDb; 169963-lmo0434; -.
DR ABCD; P0DQD2; 6 sequenced antibodies.
DR EnsemblBacteria; CAC98513; CAC98513; CAC98513.
DR GeneID; 986892; -.
DR KEGG; lmo:lmo0434; -.
DR OrthoDB; 9816557at2; -.
DR Reactome; R-HSA-8875360; InlB-mediated entry of Listeria monocytogenes into host cell.
DR PHI-base; PHI:9818; -.
DR Proteomes; UP000000817; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; TAS:Reactome.
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 Gene3D; 2.30.30.170; -; 3.
DR Gene3D; 2.60.40.1220; -; 1.
DR Gene3D; 2.60.40.4270; Listeria-Bacteroides repeat domain; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 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; IPR012569; Inl_IR.
DR InterPro; IPR013378; InlB-like_B-rpt.
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; IPR042229; Listeria/Bacterioides_rpt_sf.
DR InterPro; IPR032675; LRR_dom_sf.
DR NCBIfam; NF033202; GW_glycos_SH3; 3.
DR NCBIfam; TIGR02543; List_Bact_rpt; 1.
DR PANTHER; PTHR46652; LEUCINE-RICH REPEAT AND IQ DOMAIN-CONTAINING PROTEIN 1-RELATED; 1.
DR PANTHER; PTHR46652:SF3; LEUCINE-RICH REPEAT-CONTAINING PROTEIN 9 ISOFORM X1; 1.
DR Pfam; PF09479; Flg_new; 1.
DR Pfam; PF13457; GW; 3.
DR Pfam; PF12354; Internalin_N; 1.
DR Pfam; PF12799; LRR_4; 2.
DR Pfam; PF08191; LRR_adjacent; 1.
DR SMART; SM00365; LRR_SD22; 5.
DR SMART; SM00369; LRR_TYP; 5.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
DR SUPFAM; SSF82057; Prokaryotic SH3-related domain; 3.
DR PROSITE; PS51780; GW; 3.
DR PROSITE; PS51450; LRR; 6.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Cytoplasm; Heparin-binding;
KW Leucine-rich repeat; Lipid-binding; Membrane; Reference proteome; Repeat;
KW Secreted; Signal; Virulence.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..630
FT /note="Internalin B"
FT /id="PRO_0000021514"
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:11575932,
FT ECO:0000305|PubMed:17662939, ECO:0000305|PubMed:19900460"
FT REGION 320..392
FT /note="B repeat region"
FT /evidence="ECO:0000305|PubMed:21345802"
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:0000250|UniProtKB:P0DQD3"
FT MUTAGEN 95
FT /note="Q->EYLPNLDQLILNNNSIASIVG: Adds LRRb repeat, N-
FT terminal fragment (36-321) binds MET, wild-type
FT phosphorylation of downstream effectors MAPK1/MAPK3, full-
FT length protein induces wild-type cell scattering."
FT /evidence="ECO:0000269|PubMed:22887347"
FT MUTAGEN 95
FT /note="Q->YLPNLTSLNLSNNQITDISPI: Adds LRRa repeat, N-
FT terminal fragment (36-321) binds MET, slightly reduced
FT phosphorylation of downstream effectors MAPK1/MAPK3."
FT /evidence="ECO:0000269|PubMed:22887347"
FT MUTAGEN 199..227
FT /note="SDIVPLAGLTKLQNLYLSKNHISDLRALA->RRIVPLARLTKLQNLYLSKNH
FT ISDLRALR: A 4 Arg mutant, in vitro wild-type binding of
FT host MET, severely reduced activation of MET and downstream
FT targets."
FT /evidence="ECO:0000269|PubMed:19900460"
FT MUTAGEN 200..227
FT /note="DIVPLAGLTKLQNLYLSKNHISDLRALA->RIVPLARLTKLQNLYLSKNHIS
FT DLRALR: A 3 Arg mutant, in vitro about 100-fold reduced
FT activation of host MET and downstream targets, reduced host
FT cell scattering upon incubation with mutant protein."
FT /evidence="ECO:0000269|PubMed:19900460"
FT MUTAGEN 206..227
FT /note="GLTKLQNLYLSKNHISDLRALA->CLTKLQNLYLSKNHISDLRALC: A 2
FT Cys mutant, forms 2 intermolecular disulfide bonds, about
FT 100-fold more potent activator of MET, increased downstream
FT effector phosphorylation."
FT /evidence="ECO:0000269|PubMed:19900460"
FT MUTAGEN 332
FT /note="T->E: The B-repeat fragment (residues 31-392) no
FT longer scatters host cell colonies, full-length protein
FT reduces MET phosphorylation and downstream activity about
FT 10-fold."
FT /evidence="ECO:0000269|PubMed:27789707"
FT MUTAGEN 334..336
FT /note="IKT->KKL: The B-repeat fragment (residues 31-392) no
FT longer scatters host cell colonies."
FT /evidence="ECO:0000269|PubMed:27789707"
FT MUTAGEN 336
FT /note="T->Y: No effect on cell scattering by the B-repeat
FT fragment (residues 31-392)."
FT /evidence="ECO:0000269|PubMed:27789707"
FT HELIX 44..47
FT /evidence="ECO:0007829|PDB:6DBG"
FT HELIX 51..61
FT /evidence="ECO:0007829|PDB:6DBG"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:6DBG"
FT HELIX 72..76
FT /evidence="ECO:0007829|PDB:6DBG"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:6DBG"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:6DBG"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:4CIL"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:4CIL"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:4CIL"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:4CIL"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:4CIL"
FT HELIX 158..162
FT /evidence="ECO:0007829|PDB:4CIL"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:4CIL"
FT HELIX 180..184
FT /evidence="ECO:0007829|PDB:4CIL"
FT STRAND 189..192
FT /evidence="ECO:0007829|PDB:4CIL"
FT HELIX 202..204
FT /evidence="ECO:0007829|PDB:4CIL"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:4CIL"
FT HELIX 224..226
FT /evidence="ECO:0007829|PDB:4CIL"
FT STRAND 233..243
FT /evidence="ECO:0007829|PDB:4CIL"
FT STRAND 251..256
FT /evidence="ECO:0007829|PDB:4CIL"
FT STRAND 270..273
FT /evidence="ECO:0007829|PDB:4CIL"
FT STRAND 277..279
FT /evidence="ECO:0007829|PDB:4CIL"
FT STRAND 282..286
FT /evidence="ECO:0007829|PDB:4CIL"
FT STRAND 288..290
FT /evidence="ECO:0007829|PDB:2Y5Q"
FT STRAND 292..304
FT /evidence="ECO:0007829|PDB:4CIL"
FT STRAND 307..320
FT /evidence="ECO:0007829|PDB:4CIL"
FT STRAND 322..329
FT /evidence="ECO:0007829|PDB:2Y5P"
FT STRAND 332..339
FT /evidence="ECO:0007829|PDB:2Y5P"
FT STRAND 355..366
FT /evidence="ECO:0007829|PDB:2Y5P"
FT TURN 372..374
FT /evidence="ECO:0007829|PDB:2Y5P"
FT STRAND 382..390
FT /evidence="ECO:0007829|PDB:2Y5P"
SQ SEQUENCE 630 AA; 71147 MW; CA05F31BEFE9748C CRC64;
MKEKHNPRRK YCLISGLAII FSLWIIIGNG AKVQAETITV PTPIKQIFSD DAFAETIKDN
LKKKSVTDAV TQNELNSIDQ IIANNSDIKS VQGIQYLPNV TKLFLNGNKL TDIKPLANLK
NLGWLFLDEN KVKDLSSLKD 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 ETTEKAVNLT RYVKYIRGNA GIYKLPREDN
SLKQGTLASH RCKALTVDRE ARNGGKLWYR LKNIGWTKAE NLSLDRYDKM EYDKGVTAYA
RVRNASGNSV WTKPYNTAGA KHVNKLSVYQ GKNMRILREA KTPITTWYQF SIGGKVIGWV
DTRALNTFYK QSMEKPTRLT RYVSANKAGE SYYKVPVADN PVKRGTLAKY KNQKLIVDCQ
ATIEGQLWYR IRTSSTFIGW TKAANLRAQK
//
