SSPB_STRGN
ID SSPB_STRGN Reviewed; 1500 AA.
AC P16952; Q54184;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Agglutinin receptor;
DE AltName: Full=Adhesin SspB {ECO:0000303|PubMed:20138058};
DE AltName: Full=SSP-5 {ECO:0000303|PubMed:2185241};
DE Flags: Precursor;
GN Name=sspB {ECO:0000303|PubMed:8733238};
GN Synonyms=ssp5 {ECO:0000303|PubMed:2185241};
OS Streptococcus gordonii.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1302;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=M5;
RX PubMed=2185241; DOI=10.1016/s0021-9258(19)39087-8;
RA Demuth D.R., Golub E.E., Malamud D.;
RT "Streptococcal-host interactions. Structural and functional analysis of a
RT Streptococcus sanguis receptor for a human salivary glycoprotein.";
RL J. Biol. Chem. 265:7120-7126(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SEQUENCE REVISION.
RC STRAIN=M5;
RX PubMed=8733238; DOI=10.1111/j.1365-2958.1996.tb02627.x;
RA Demuth D.R., Duan Y., Brooks W., Holmes A.R., McNab R., Jenkinson H.F.;
RT "Tandem genes encode cell-surface polypeptides SspA and SspB which mediate
RT adhesion of the oral bacterium Streptococcus gordonii to human and
RT bacterial receptors.";
RL Mol. Microbiol. 20:403-413(1996).
RN [3]
RP S.GORDONII IN INFECTIVE ENDOCARDITIS.
RX PubMed=8366515; DOI=10.1099/00222615-39-3-179;
RA Douglas C.W., Heath J., Hampton K.K., Preston F.E.;
RT "Identity of viridans streptococci isolated from cases of infective
RT endocarditis.";
RL J. Med. Microbiol. 39:179-182(1993).
RN [4]
RP INTERACTION WITH P.GINGIVALIS MFA1.
RX PubMed=11083792; DOI=10.1128/iai.68.12.6758-6762.2000;
RA Chung W.O., Demuth D.R., Lamont R.J.;
RT "Identification of a Porphyromonas gingivalis receptor for the
RT Streptococcus gordonii SspB protein.";
RL Infect. Immun. 68:6758-6762(2000).
RN [5]
RP INTERACTION WITH P.GINGIVALIS MFA1.
RX PubMed=15972485; DOI=10.1128/iai.73.7.3983-3989.2005;
RA Park Y., Simionato M.R., Sekiya K., Murakami Y., James D., Chen W.,
RA Hackett M., Yoshimura F., Demuth D.R., Lamont R.J.;
RT "Short fimbriae of Porphyromonas gingivalis and their role in coadhesion
RT with Streptococcus gordonii.";
RL Infect. Immun. 73:3983-3989(2005).
RN [6] {ECO:0007744|PDB:2WD6}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 449-797 IN COMPLEX WITH CALCIUM.
RX PubMed=19609934; DOI=10.1002/pro.200;
RA Forsgren N., Lamont R.J., Persson K.;
RT "Crystal structure of the variable domain of the Streptococcus gordonii
RT surface protein SspB.";
RL Protein Sci. 18:1896-1905(2009).
RN [7] {ECO:0007744|PDB:2WOY, ECO:0007744|PDB:2WQS, ECO:0007744|PDB:2WZA}
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 1061-1413 IN COMPLEX WITH
RP CALCIUM.
RX PubMed=20138058; DOI=10.1016/j.jmb.2010.01.065;
RA Forsgren N., Lamont R.J., Persson K.;
RT "Two intramolecular isopeptide bonds are identified in the crystal
RT structure of the Streptococcus gordonii SspB C-terminal domain.";
RL J. Mol. Biol. 397:740-751(2010).
RN [8] {ECO:0007744|PDB:7L0O}
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 913-1406 IN COMPLEX WITH CALCIUM.
RX PubMed=34473090; DOI=10.1107/s2059798321008135;
RA Schormann N., Purushotham S., Mieher J.L., Patel M., Wu H.,
RA Deivanayagam C.;
RT "Structural and functional analysis of the C-terminal region of
RT Streptococcus gordonii SspB.";
RL Acta Crystallogr. D 77:1206-1215(2021).
CC -!- FUNCTION: May bind sialic acid residues of salivary agglutinin (SAG) in
CC a calcium-dependent reaction. The interaction of SAG with its receptor
CC in various oral streptococci modulate bacterial colonization of oral
CC tissue and is associated with reduced levels of dental caries.
CC -!- SUBUNIT: Interacts with P.gingivalis fimbrial protein Mfa1.
CC {ECO:0000269|PubMed:11083792, ECO:0000269|PubMed:15972485}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|PROSITE-
CC ProRule:PRU00477}; Peptidoglycan-anchor {ECO:0000255|PROSITE-
CC ProRule:PRU00477}.
CC -!- MISCELLANEOUS: S.gordonii, a commensal oral cavity bacteria, is among
CC the bacteria most frequently identified as being the primary
CC etiological agents of subacute infective endocarditis (found in 13% of
CC cases). {ECO:0000269|PubMed:8366515}.
CC -!- SIMILARITY: Belongs to the antigen I/II family. {ECO:0000305}.
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DR EMBL; U40026; AAC44100.1; -; Genomic_DNA.
DR PIR; A35186; A35186.
DR PDB; 2WD6; X-ray; 2.30 A; A/B=449-797.
DR PDB; 2WOY; X-ray; 1.50 A; A=1083-1413.
DR PDB; 2WQS; X-ray; 1.70 A; A=1083-1413.
DR PDB; 2WZA; X-ray; 2.08 A; A=1061-1413.
DR PDB; 6Q2K; X-ray; 2.00 A; A=460-777.
DR PDB; 6Q2L; X-ray; 1.80 A; A=460-763.
DR PDB; 7L0O; X-ray; 2.70 A; A/B=913-1406.
DR PDBsum; 2WD6; -.
DR PDBsum; 2WOY; -.
DR PDBsum; 2WQS; -.
DR PDBsum; 2WZA; -.
DR PDBsum; 6Q2K; -.
DR PDBsum; 6Q2L; -.
DR PDBsum; 7L0O; -.
DR AlphaFoldDB; P16952; -.
DR SMR; P16952; -.
DR EvolutionaryTrace; P16952; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 2.60.530.10; -; 1.
DR InterPro; IPR026345; Adh_isopep-form_adh_dom.
DR InterPro; IPR041324; AgI/II_N.
DR InterPro; IPR032300; Antigen_C.
DR InterPro; IPR021197; Cross-wall-target_lipo_motif.
DR InterPro; IPR013574; Glucan-bd_C/Surface_Ag-I/II_V.
DR InterPro; IPR019931; LPXTG_anchor.
DR InterPro; IPR036234; SA_I/II_PAC_V_sf.
DR InterPro; IPR009578; Surface_Ag_rpt.
DR Pfam; PF18652; Adhesin_P1_N; 1.
DR Pfam; PF17998; AgI_II_C2; 1.
DR Pfam; PF16364; Antigen_C; 1.
DR Pfam; PF08363; GbpC; 1.
DR Pfam; PF00746; Gram_pos_anchor; 1.
DR Pfam; PF06696; Strep_SA_rep; 6.
DR SUPFAM; SSF74914; SSF74914; 1.
DR TIGRFAMs; TIGR04228; isopep_sspB_C2; 1.
DR TIGRFAMs; TIGR03726; strep_RK_lipo; 1.
DR PROSITE; PS51965; AG_I_II_AR; 4.
DR PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Cell wall; Isopeptide bond; Metal-binding;
KW Peptidoglycan-anchor; Repeat; Secreted; Signal.
FT SIGNAL 1..38
FT /evidence="ECO:0000255"
FT CHAIN 39..1470
FT /note="Agglutinin receptor"
FT /evidence="ECO:0000255"
FT /id="PRO_0000005669"
FT PROPEP 1471..1500
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT /id="PRO_0000005670"
FT REPEAT 146..220
FT /note="Ag I/II A 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01310"
FT REPEAT 221..302
FT /note="Ag I/II A 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01310"
FT REPEAT 303..384
FT /note="Ag I/II A 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01310"
FT REPEAT 385..466
FT /note="Ag I/II A 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01310"
FT REGION 164..470
FT /note="4 X approximate tandem repeats, HR1"
FT /evidence="ECO:0000269|PubMed:2185241"
FT REGION 764..906
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 771..887
FT /note="3 X approximate tandem repeats, PR1"
FT /evidence="ECO:0000269|PubMed:2185241"
FT REGION 1167..1193
FT /note="BAR region involved in interaction with Mfa1"
FT /evidence="ECO:0000305|PubMed:20138058"
FT REGION 1410..1473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1467..1471
FT /note="LPXTG sorting signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT COMPBIAS 783..799
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 822..838
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 861..877
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 884..906
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1427..1447
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 648
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:19609934,
FT ECO:0007744|PDB:2WD6"
FT BINDING 650
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:19609934,
FT ECO:0007744|PDB:2WD6"
FT BINDING 664
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:19609934,
FT ECO:0007744|PDB:2WD6"
FT BINDING 1077
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:20138058,
FT ECO:0000269|PubMed:34473090, ECO:0007744|PDB:2WZA,
FT ECO:0007744|PDB:7L0O"
FT BINDING 1110
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:20138058,
FT ECO:0007744|PDB:2WZA"
FT BINDING 1112
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:20138058,
FT ECO:0007744|PDB:2WZA"
FT BINDING 1113
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:20138058,
FT ECO:0007744|PDB:2WZA"
FT BINDING 1133
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:20138058,
FT ECO:0000269|PubMed:34473090, ECO:0007744|PDB:2WOY,
FT ECO:0007744|PDB:2WZA, ECO:0007744|PDB:7L0O"
FT BINDING 1134
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:20138058,
FT ECO:0000269|PubMed:34473090, ECO:0007744|PDB:2WOY,
FT ECO:0007744|PDB:2WZA, ECO:0007744|PDB:7L0O"
FT BINDING 1136
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:20138058,
FT ECO:0000269|PubMed:34473090, ECO:0007744|PDB:2WOY,
FT ECO:0007744|PDB:2WZA, ECO:0007744|PDB:7L0O"
FT BINDING 1186
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:20138058,
FT ECO:0000269|PubMed:34473090, ECO:0007744|PDB:2WOY,
FT ECO:0007744|PDB:2WZA, ECO:0007744|PDB:7L0O"
FT BINDING 1188
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:20138058,
FT ECO:0000269|PubMed:34473090, ECO:0007744|PDB:2WOY,
FT ECO:0007744|PDB:2WZA, ECO:0007744|PDB:7L0O"
FT BINDING 1308
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:20138058,
FT ECO:0000269|PubMed:34473090, ECO:0007744|PDB:2WOY,
FT ECO:0007744|PDB:2WZA, ECO:0007744|PDB:7L0O"
FT BINDING 1309
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:20138058,
FT ECO:0000269|PubMed:34473090, ECO:0007744|PDB:2WOY,
FT ECO:0007744|PDB:2WZA, ECO:0007744|PDB:7L0O"
FT BINDING 1311
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:20138058,
FT ECO:0000269|PubMed:34473090, ECO:0007744|PDB:2WOY,
FT ECO:0007744|PDB:2WZA, ECO:0007744|PDB:7L0O"
FT BINDING 1354
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:20138058,
FT ECO:0000269|PubMed:34473090, ECO:0007744|PDB:2WOY,
FT ECO:0007744|PDB:2WZA, ECO:0007744|PDB:7L0O"
FT BINDING 1355
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:20138058,
FT ECO:0000269|PubMed:34473090, ECO:0007744|PDB:2WOY,
FT ECO:0007744|PDB:2WZA, ECO:0007744|PDB:7L0O"
FT MOD_RES 1470
FT /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT CROSSLNK 927..1042
FT /note="Isoaspartyl lysine isopeptide (Lys-Asn)"
FT /evidence="ECO:0000269|PubMed:34473090"
FT CROSSLNK 1082..1232
FT /note="Isoaspartyl lysine isopeptide (Lys-Asn)"
FT /evidence="ECO:0000269|PubMed:20138058,
FT ECO:0000269|PubMed:34473090"
FT CROSSLNK 1259..1393
FT /note="Isoaspartyl lysine isopeptide (Lys-Asn)"
FT /evidence="ECO:0000269|PubMed:20138058"
FT HELIX 464..478
FT /evidence="ECO:0007829|PDB:6Q2L"
FT TURN 479..481
FT /evidence="ECO:0007829|PDB:6Q2L"
FT STRAND 485..488
FT /evidence="ECO:0007829|PDB:6Q2L"
FT STRAND 503..505
FT /evidence="ECO:0007829|PDB:6Q2L"
FT HELIX 515..524
FT /evidence="ECO:0007829|PDB:6Q2L"
FT HELIX 534..547
FT /evidence="ECO:0007829|PDB:6Q2L"
FT STRAND 552..558
FT /evidence="ECO:0007829|PDB:6Q2L"
FT STRAND 563..568
FT /evidence="ECO:0007829|PDB:6Q2L"
FT STRAND 582..592
FT /evidence="ECO:0007829|PDB:6Q2L"
FT STRAND 597..604
FT /evidence="ECO:0007829|PDB:6Q2L"
FT TURN 608..610
FT /evidence="ECO:0007829|PDB:6Q2L"
FT STRAND 612..615
FT /evidence="ECO:0007829|PDB:6Q2L"
FT STRAND 619..630
FT /evidence="ECO:0007829|PDB:6Q2L"
FT STRAND 643..646
FT /evidence="ECO:0007829|PDB:6Q2L"
FT TURN 656..658
FT /evidence="ECO:0007829|PDB:6Q2L"
FT STRAND 663..668
FT /evidence="ECO:0007829|PDB:6Q2L"
FT STRAND 670..674
FT /evidence="ECO:0007829|PDB:6Q2L"
FT STRAND 680..684
FT /evidence="ECO:0007829|PDB:6Q2L"
FT TURN 685..687
FT /evidence="ECO:0007829|PDB:6Q2L"
FT STRAND 688..693
FT /evidence="ECO:0007829|PDB:6Q2L"
FT HELIX 698..700
FT /evidence="ECO:0007829|PDB:6Q2L"
FT HELIX 706..709
FT /evidence="ECO:0007829|PDB:6Q2L"
FT STRAND 711..713
FT /evidence="ECO:0007829|PDB:6Q2L"
FT HELIX 717..720
FT /evidence="ECO:0007829|PDB:6Q2L"
FT STRAND 722..725
FT /evidence="ECO:0007829|PDB:6Q2L"
FT STRAND 728..739
FT /evidence="ECO:0007829|PDB:6Q2L"
FT STRAND 741..745
FT /evidence="ECO:0007829|PDB:6Q2L"
FT STRAND 753..755
FT /evidence="ECO:0007829|PDB:2WD6"
FT HELIX 916..918
FT /evidence="ECO:0007829|PDB:7L0O"
FT STRAND 925..930
FT /evidence="ECO:0007829|PDB:7L0O"
FT STRAND 947..954
FT /evidence="ECO:0007829|PDB:7L0O"
FT STRAND 967..972
FT /evidence="ECO:0007829|PDB:7L0O"
FT STRAND 977..979
FT /evidence="ECO:0007829|PDB:7L0O"
FT HELIX 981..986
FT /evidence="ECO:0007829|PDB:7L0O"
FT STRAND 991..996
FT /evidence="ECO:0007829|PDB:7L0O"
FT TURN 997..1000
FT /evidence="ECO:0007829|PDB:7L0O"
FT STRAND 1001..1006
FT /evidence="ECO:0007829|PDB:7L0O"
FT HELIX 1008..1014
FT /evidence="ECO:0007829|PDB:7L0O"
FT STRAND 1028..1033
FT /evidence="ECO:0007829|PDB:7L0O"
FT STRAND 1039..1042
FT /evidence="ECO:0007829|PDB:7L0O"
FT STRAND 1045..1048
FT /evidence="ECO:0007829|PDB:7L0O"
FT TURN 1049..1051
FT /evidence="ECO:0007829|PDB:7L0O"
FT STRAND 1059..1062
FT /evidence="ECO:0007829|PDB:7L0O"
FT STRAND 1081..1083
FT /evidence="ECO:0007829|PDB:2WZA"
FT STRAND 1102..1109
FT /evidence="ECO:0007829|PDB:2WOY"
FT HELIX 1112..1114
FT /evidence="ECO:0007829|PDB:2WOY"
FT HELIX 1121..1124
FT /evidence="ECO:0007829|PDB:2WOY"
FT STRAND 1128..1133
FT /evidence="ECO:0007829|PDB:2WOY"
FT TURN 1136..1138
FT /evidence="ECO:0007829|PDB:2WOY"
FT STRAND 1139..1141
FT /evidence="ECO:0007829|PDB:2WOY"
FT HELIX 1143..1145
FT /evidence="ECO:0007829|PDB:2WOY"
FT STRAND 1147..1149
FT /evidence="ECO:0007829|PDB:2WOY"
FT STRAND 1159..1165
FT /evidence="ECO:0007829|PDB:2WOY"
FT TURN 1167..1169
FT /evidence="ECO:0007829|PDB:2WOY"
FT HELIX 1172..1181
FT /evidence="ECO:0007829|PDB:2WOY"
FT STRAND 1189..1196
FT /evidence="ECO:0007829|PDB:2WOY"
FT HELIX 1197..1203
FT /evidence="ECO:0007829|PDB:2WOY"
FT TURN 1204..1208
FT /evidence="ECO:0007829|PDB:2WOY"
FT STRAND 1211..1219
FT /evidence="ECO:0007829|PDB:2WOY"
FT HELIX 1221..1225
FT /evidence="ECO:0007829|PDB:2WOY"
FT STRAND 1228..1238
FT /evidence="ECO:0007829|PDB:2WOY"
FT STRAND 1241..1252
FT /evidence="ECO:0007829|PDB:2WOY"
FT STRAND 1258..1265
FT /evidence="ECO:0007829|PDB:2WOY"
FT STRAND 1282..1288
FT /evidence="ECO:0007829|PDB:2WOY"
FT STRAND 1294..1298
FT /evidence="ECO:0007829|PDB:2WOY"
FT STRAND 1303..1308
FT /evidence="ECO:0007829|PDB:2WOY"
FT TURN 1311..1313
FT /evidence="ECO:0007829|PDB:2WOY"
FT STRAND 1314..1326
FT /evidence="ECO:0007829|PDB:2WOY"
FT STRAND 1328..1330
FT /evidence="ECO:0007829|PDB:2WOY"
FT HELIX 1343..1345
FT /evidence="ECO:0007829|PDB:2WOY"
FT STRAND 1346..1351
FT /evidence="ECO:0007829|PDB:2WOY"
FT TURN 1352..1355
FT /evidence="ECO:0007829|PDB:2WOY"
FT STRAND 1356..1361
FT /evidence="ECO:0007829|PDB:2WOY"
FT HELIX 1363..1366
FT /evidence="ECO:0007829|PDB:2WOY"
FT STRAND 1377..1385
FT /evidence="ECO:0007829|PDB:2WOY"
FT STRAND 1387..1393
FT /evidence="ECO:0007829|PDB:2WOY"
FT STRAND 1396..1399
FT /evidence="ECO:0007829|PDB:2WOY"
FT STRAND 1402..1405
FT /evidence="ECO:0007829|PDB:2WOY"
FT STRAND 1409..1413
FT /evidence="ECO:0007829|PDB:2WOY"
SQ SEQUENCE 1500 AA; 164553 MW; DCF190E7D44D889F CRC64;
MKNKKEVYGF RKSKVAKTLC GAVLGTALIA FADKAVFADE VTETTSTSTV EVATTGNPAT
NLPEAQGEMS QVAKESQAKA GSKESALPVE VSSADLDKAV ADAKSAGVKV VQDETKDKGT
ATTATDNAQK QDEIKSDYAK QAEEIKTTTE AYKKEVAAHQ AETDKINAEN KAADDKYQKD
LKSHQEEVEK INTANATAKA EYEAKLAQYQ KDLATVKKAN EDSQQDYQNK LSAYQTELAR
VQKANAEAKE AYEKAVKENT AKNEALKVEN EAIKQRNETA KATYEAAMKQ YEADLAAIKK
ANEDNDADYQ AKLAAYQTEL ARVQKANAEA KEAYDKAVKE NTAKNTAIQA ENEAIKQRNE
TAKATYDAAV KKYEADLAAV KQANATNEAD YQAKLAAYQT ELARVQKANA DAKATYEKAV
EDNKAKNAAI KAENEEIKQR NAVAKTDYEA KLAKYEADLA KYKKEFAAYT AALAEAESKK
KQDGYLSEPR SQSLNFKSEP NAIRTIDSSV HQYGQQELDA LVKSWGISPT NPDRKKSRAY
SYFNAINSNN TYAKLVLEKD KPVDVTYTGL KNSSFNGKKI SKVVYTYTLK ETGFNDGTKM
TMFASSDPTV TAWYNDYFTS TNINVKVKFY DEEGQLMNLT GGLVNFSSLN RGNGSGAIDK
DAIESVRNFN GRYIPISGSS IKIHENNSAY ADSSNAEKSL GARWNTSEWD TTSSPNNWYG
AIVGEITQSE ISFNMASSKS GNIWFAFNSN INAIGVPTKP VAPTAPTQPM YETEKPLEPA
PVAPSYENEP TPPVKTPDQP EPSKPEEPTY ETEKPLEPAP VAPSYENEPT PPVKTPDQPE
PSKPEEPNYE TEKPLEPAPV APSYENEPTP PVKIPDQPEP SKPEEPTYDP LPTPPLAPTP
KQLPTPPVVP TVHFHYSSLL AQPQINKEIK NEDGVDIDRT LVAKQSIVKF ELKTEALTAG
RPKTTSFVLV DPLPTGYKFD LDATKAASTG FDTTYDEASH TVTFKATDET LATYNADLTK
PVETLHPTVV GRVLNDGATY TNNFTLTVND AYGIKSNVVR VTTPGKPNDP DNPNNNYIKP
TKVNKNKEGL NIDGKEVLAG STNYYELTWD LDQYKGDKSS KEAIQNGFYY VDDYPEEALD
VRPDLVKVAD EKGNQVSGVS VQQYDSLEAA PKKVQDLLKK ANITVKGAFQ LFSADNPEEF
YKQYVATGTS LVITDPMTVK SEFGKTGGKY ENKAYQIDFG NGYATEVVVN NVPKITPKKD
VTVSLDPTSE NLDGQTVQLY QTFNYRLIGG LIPQNHSEEL EDYSFVDDYD QAGDQYTGNY
KTFSSLNLTM KDGSVIKAGT DLTSQTTAET DATNGIVTVR FKEDFLQKIS LDSPFQAETY
LQMRRIAIGT FENTYVNTVN KVAYASNTVR TTTPIPRTPD KPTPIPTPKP KDPDKPETPK
EPKVPSPKVE DPSAPIPVSV GKELTTLPKT GTNDATYMPY LGLAALVGFL GLGLAKRKED
