SPA_STAA8
ID SPA_STAA8 Reviewed; 516 AA.
AC P02976; Q2G1N8;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 3.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Immunoglobulin G-binding protein A;
DE Short=IgG-binding protein A;
DE AltName: Full=Staphylococcal protein A;
DE Short=SpA;
DE Flags: Precursor;
GN Name=spa; OrderedLocusNames=SAOUHSC_00069;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=8325-4;
RX PubMed=6319407; DOI=10.1016/s0021-9258(17)43463-6;
RA Uhlen M., Guss B., Nilsson B., Gatenbeck S., Philipson L., Lindberg M.;
RT "Complete sequence of the staphylococcal gene encoding protein A. A gene
RT evolved through multiple duplications.";
RL J. Biol. Chem. 259:1695-1702(1984).
RN [2]
RP ERRATUM OF PUBMED:6319407, AND SEQUENCE REVISION.
RA Uhlen M., Guss B., Nilsson B., Gatenbeck S., Philipson L., Lindberg M.;
RL J. Biol. Chem. 259:13628-13628(1984).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-186.
RC STRAIN=8325-4;
RX PubMed=6338496; DOI=10.1073/pnas.80.3.697;
RA Loefdahl S., Guss B., Uhlen M., Philipson L., Lindberg M.;
RT "Gene for staphylococcal protein A.";
RL Proc. Natl. Acad. Sci. U.S.A. 80:697-701(1983).
RN [5]
RP PROTEIN SEQUENCE OF 37-42, FUNCTION, SUBCELLULAR LOCATION, AND
RP IMMUNOGLOBULIN-BINDING.
RC STRAIN=A676;
RX PubMed=2938951; DOI=10.1111/j.1432-1033.1986.tb09625.x;
RA Moks T., Abrahmsen L., Nilsson B., Hellman U., Sjoequist J., Uhlen M.;
RT "Staphylococcal protein A consists of five IgG-binding domains.";
RL Eur. J. Biochem. 156:637-643(1986).
RN [6]
RP FUNCTION, AND IMMUNOGLOBULIN-BINDING.
RC STRAIN=ATCC 12598 / Cowan 1 / DSM 20372 / NCIMB 11787 / NCTC 8530;
RX PubMed=4163007;
RA Forsgren A., Sjoequist J.;
RT "'Protein A' from S. aureus. I. Pseudo-immune reaction with human gamma-
RT globulin.";
RL J. Immunol. 97:822-827(1966).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=8325-4;
RX PubMed=3679545; DOI=10.1128/iai.55.12.3103-3110.1987;
RA Patel A.H., Nowlan P., Weavers E.D., Foster T.;
RT "Virulence of protein A-deficient and alpha-toxin-deficient mutants of
RT Staphylococcus aureus isolated by allele replacement.";
RL Infect. Immun. 55:3103-3110(1987).
RN [8]
RP PROTEIN SEQUENCE OF 37-47, SUBCELLULAR LOCATION, DOMAIN, TOPOLOGY, AND
RP MUTAGENESIS OF LYS-478; 482-LEU--LEU-516; 482-LEU--GLU-487; PRO-483;
RP THR-485; 488-GLU--LEU-516; 514-ARG--LEU-516; 515-GLU-LEU-516 AND LEU-516.
RC STRAIN=8325-4, and RN4220;
RX PubMed=1638631; DOI=10.1016/0092-8674(92)90101-h;
RA Schneewind O., Model P., Fischetti V.A.;
RT "Sorting of protein A to the staphylococcal cell wall.";
RL Cell 70:267-281(1992).
RN [9]
RP SUBCELLULAR LOCATION, AND CLEAVAGE SITE.
RC STRAIN=8325-4;
RX PubMed=7830549; DOI=10.1111/j.1365-2958.1994.tb01271.x;
RA Navarre W.W., Schneewind O.;
RT "Proteolytic cleavage and cell wall anchoring at the LPXTG motif of surface
RT proteins in gram-positive bacteria.";
RL Mol. Microbiol. 14:115-121(1994).
RN [10]
RP SUBCELLULAR LOCATION, AND PEPTIDOGLYCAN CROSS-LINK.
RX PubMed=7701329; DOI=10.1126/science.7701329;
RA Schneewind O., Fowler A., Faull K.F.;
RT "Structure of the cell wall anchor of surface proteins in Staphylococcus
RT aureus.";
RL Science 268:103-106(1995).
RN [11]
RP SUBCELLULAR LOCATION, AND PEPTIDOGLYCAN CROSS-LINK.
RX PubMed=9786922; DOI=10.1074/jbc.273.44.29135;
RA Navarre W.W., Ton-That H., Faull K.F., Schneewind O.;
RT "Anchor structure of staphylococcal surface proteins. II. Cooh-terminal
RT structure of muramidase and amidase-solubilized surface protein.";
RL J. Biol. Chem. 273:29135-29142(1998).
RN [12]
RP SUBCELLULAR LOCATION, AND PROCESSING BY SORTASE A.
RC STRAIN=RN4220 / OS2;
RX PubMed=10427003; DOI=10.1126/science.285.5428.760;
RA Mazmanian S.K., Liu G., Ton-That H., Schneewind O.;
RT "Staphylococcus aureus sortase, an enzyme that anchors surface proteins to
RT the cell wall.";
RL Science 285:760-763(1999).
RN [13]
RP SUBCELLULAR LOCATION, DOMAIN, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP 7-TYR--ARG-10; GLY-15 AND SER-18.
RC STRAIN=RN4220;
RX PubMed=12700270; DOI=10.1128/jb.185.9.2910-2919.2003;
RA Bae T., Schneewind O.;
RT "The YSIRK-G/S motif of staphylococcal protein A and its role in efficiency
RT of signal peptide processing.";
RL J. Bacteriol. 185:2910-2919(2003).
RN [14]
RP SUBCELLULAR LOCATION.
RC STRAIN=RN4220;
RX PubMed=17416657; DOI=10.1128/jb.00227-07;
RA DeDent A.C., McAdow M., Schneewind O.;
RT "Distribution of protein A on the surface of Staphylococcus aureus.";
RL J. Bacteriol. 189:4473-4484(2007).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND INDUCTION.
RC STRAIN=RN4220;
RX PubMed=20472795; DOI=10.1128/jb.01452-09;
RA Sibbald M.J., Winter T., van der Kooi-Pol M.M., Buist G., Tsompanidou E.,
RA Bosma T., Schafer T., Ohlsen K., Hecker M., Antelmann H., Engelmann S.,
RA van Dijl J.M.;
RT "Synthetic effects of secG and secY2 mutations on exoproteome biogenesis in
RT Staphylococcus aureus.";
RL J. Bacteriol. 192:3788-3800(2010).
RN [16]
RP DISRUPTION PHENOTYPE.
RC STRAIN=SA564;
RX PubMed=22447609; DOI=10.1128/aem.00202-12;
RA Redder P., Linder P.;
RT "New range of vectors with a stringent 5-fluoroorotic acid-based
RT counterselection system for generating mutants by allelic replacement in
RT Staphylococcus aureus.";
RL Appl. Environ. Microbiol. 78:3846-3854(2012).
RN [17] {ECO:0007744|PDB:1DEE}
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 100-153 IN COMPLEX WITH FAB
RP FRAGMENT, AND FUNCTION.
RX PubMed=10805799; DOI=10.1073/pnas.97.10.5399;
RA Graille M., Stura E.A., Corper A.L., Sutton B.J., Taussig M.J.,
RA Charbonnier J.B., Silverman G.J.;
RT "Crystal structure of a Staphylococcus aureus protein A domain complexed
RT with the Fab fragment of a human IgM antibody: structural basis for
RT recognition of B-cell receptors and superantigen activity.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:5399-5404(2000).
CC -!- FUNCTION: Plays a role in the inhibition of the host innate and
CC adaptive immune responses. Possesses five immunoglobulin-binding
CC domains that capture both the fragment crystallizable region (Fc
CC region) and the Fab region (part of Ig that identifies antigen) of
CC immunoglobulins (PubMed:2938951, PubMed:4163007, PubMed:10805799). In
CC turn, Staphylococcus aureus is protected from phagocytic killing via
CC inhibition of Ig Fc region. In addition, the host elicited B-cell
CC response is prevented due to a decrease of antibody-secreting cell
CC proliferation that enter the bone marrow, thereby decreasing long-term
CC antibody production. Inhibits osteogenesis by preventing osteoblast
CC proliferation and expression of alkaline phosphatase, type I collagen,
CC osteopontin and osteocalcin. Acts directly as a pro-inflammatory factor
CC in the lung through its ability to bind and activate tumor necrosis
CC factor alpha receptor 1/TNFRSF1A (By similarity).
CC {ECO:0000250|UniProtKB:A0A0H3K686, ECO:0000269|PubMed:10805799,
CC ECO:0000269|PubMed:2938951, ECO:0000269|PubMed:4163007}.
CC -!- SUBUNIT: Interacts with host TNFRSF1A; this interaction leads to the
CC stimulation of both surface expression and shedding of TNFRSF1A.
CC {ECO:0000250|UniProtKB:A0A0H3K686}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:10427003,
CC ECO:0000269|PubMed:12700270, ECO:0000269|PubMed:1638631,
CC ECO:0000269|PubMed:17416657, ECO:0000269|PubMed:3679545,
CC ECO:0000269|PubMed:4163007, ECO:0000269|PubMed:9786922,
CC ECO:0000305|PubMed:20472795, ECO:0000305|PubMed:7701329,
CC ECO:0000305|PubMed:7830549}; Peptidoglycan-anchor
CC {ECO:0000269|PubMed:10427003, ECO:0000269|PubMed:12700270,
CC ECO:0000269|PubMed:17416657, ECO:0000269|PubMed:9786922,
CC ECO:0000305|PubMed:1638631, ECO:0000305|PubMed:20472795,
CC ECO:0000305|PubMed:7701329}; Extracellular side
CC {ECO:0000269|PubMed:1638631, ECO:0000305|PubMed:7701329}. Secreted
CC {ECO:0000269|PubMed:2938951, ECO:0000269|PubMed:3679545}. Note=Cell
CC wall anchoring is confered by the LPXTG motif and following sequences
CC (PubMed:1638631). Anchored by sortase A (PubMed:10427003). SpA from
CC strains A676 and V-I is secreted whereas SpA from Cowan 1 and 8325-4 is
CC mostly attached to the cell wall (Probable). Newly synthesized protein
CC is deposited at 2-4 foci/cell and eventually is distributed in a ring
CC around the cell (PubMed:17416657). {ECO:0000269|PubMed:10427003,
CC ECO:0000269|PubMed:1638631, ECO:0000269|PubMed:17416657,
CC ECO:0000305|PubMed:2938951}.
CC -!- INDUCTION: More protein is secreted in a secG or double secG/secY2
CC mutant (at protein level). {ECO:0000269|PubMed:20472795}.
CC -!- DOMAIN: Each of the immunoglobulin-binding region repeats can bind the
CC Fc region of an immunoglobulin (PubMed:2938951). Cell wall anchoring is
CC confered by the LPXTG motif and following sequences (residues 482-516)
CC which are necessary and sufficient to target other proteins to the cell
CC wall (PubMed:1638631). The YSIRK-G/S motif in the signal sequence plays
CC a role in the secretion efficiency for SpA, it may have a specialized
CC recognition mode (Probable). {ECO:0000269|PubMed:1638631,
CC ECO:0000269|PubMed:2938951, ECO:0000305|PubMed:12700270}.
CC -!- DISRUPTION PHENOTYPE: Decreased virulence in mice (PubMed:3679545).
CC Bacteria do not bind IgG (PubMed:12700270). No visible phenotype during
CC growth in liquid culture (PubMed:22447609).
CC {ECO:0000269|PubMed:12700270, ECO:0000269|PubMed:22447609,
CC ECO:0000269|PubMed:3679545}.
CC -!- BIOTECHNOLOGY: Important immunodiagnostic reagent because of its
CC ability to bind the Fab and Fc fragments of a wide range of mammalian
CC immunoglobulins. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the immunoglobulin-binding protein SpA family.
CC {ECO:0000305}.
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DR EMBL; J01786; AAA26676.1; -; Genomic_DNA.
DR EMBL; CP000253; ABD29253.1; -; Genomic_DNA.
DR EMBL; V01287; CAA24596.1; -; Genomic_DNA.
DR PIR; A58531; QVSAA.
DR RefSeq; WP_000728764.1; NZ_LS483365.1.
DR RefSeq; YP_498670.1; NC_007795.1.
DR PDB; 1DEE; X-ray; 2.70 A; G/H=100-153.
DR PDB; 4Y4Y; X-ray; 3.00 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z/a/b/c/d=158-211, A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z/a/b/c/d=219-354, A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z/a/b/c/d=236-459.
DR PDB; 4Y5Z; X-ray; 2.95 A; 0/1/2/3/4/5/6/7/A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V=158-211.
DR PDB; 5U3D; X-ray; 1.77 A; C=101-151.
DR PDB; 5U4Y; X-ray; 2.50 A; C/D=215-268.
DR PDB; 5U5F; X-ray; 1.81 A; C=101-151.
DR PDB; 5U5M; X-ray; 1.88 A; C=101-151.
DR PDB; 5U6A; X-ray; 1.74 A; C=101-151.
DR PDB; 6B9Y; X-ray; 2.14 A; C=101-151.
DR PDB; 6B9Z; X-ray; 1.82 A; C=101-151.
DR PDB; 6BAE; X-ray; 2.14 A; C=101-151.
DR PDB; 6BAH; X-ray; 1.90 A; C=101-151.
DR PDB; 6K3M; X-ray; 1.80 A; H=100-150.
DR PDB; 6K64; X-ray; 1.93 A; C/H=100-151.
DR PDB; 6K65; X-ray; 1.65 A; A=218-266.
DR PDB; 6K68; X-ray; 3.20 A; E/H/I/L=100-145.
DR PDB; 6K6A; X-ray; 1.94 A; C/D=100-151.
DR PDB; 6K6B; X-ray; 2.06 A; B=90-152.
DR PDB; 6SOW; NMR; -; A=271-327.
DR PDBsum; 1DEE; -.
DR PDBsum; 4Y4Y; -.
DR PDBsum; 4Y5Z; -.
DR PDBsum; 5U3D; -.
DR PDBsum; 5U4Y; -.
DR PDBsum; 5U5F; -.
DR PDBsum; 5U5M; -.
DR PDBsum; 5U6A; -.
DR PDBsum; 6B9Y; -.
DR PDBsum; 6B9Z; -.
DR PDBsum; 6BAE; -.
DR PDBsum; 6BAH; -.
DR PDBsum; 6K3M; -.
DR PDBsum; 6K64; -.
DR PDBsum; 6K65; -.
DR PDBsum; 6K68; -.
DR PDBsum; 6K6A; -.
DR PDBsum; 6K6B; -.
DR PDBsum; 6SOW; -.
DR AlphaFoldDB; P02976; -.
DR SMR; P02976; -.
DR MINT; P02976; -.
DR STRING; 93061.SAOUHSC_00069; -.
DR PRIDE; P02976; -.
DR ABCD; P02976; 1 sequenced antibody.
DR EnsemblBacteria; ABD29253; ABD29253; SAOUHSC_00069.
DR GeneID; 3919448; -.
DR KEGG; sao:SAOUHSC_00069; -.
DR PATRIC; fig|93061.5.peg.59; -.
DR eggNOG; COG1388; Bacteria.
DR HOGENOM; CLU_024983_0_0_9; -.
DR OMA; QRNGYIQ; -.
DR EvolutionaryTrace; P02976; -.
DR PHI-base; PHI:4570; -.
DR PRO; PR:P02976; -.
DR Proteomes; UP000008816; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0019864; F:IgG binding; IEA:UniProtKB-KW.
DR CDD; cd00118; LysM; 1.
DR Gene3D; 3.10.350.10; -; 1.
DR InterPro; IPR009063; Ig/albumin-bd_sf.
DR InterPro; IPR019931; LPXTG_anchor.
DR InterPro; IPR018392; LysM_dom.
DR InterPro; IPR036779; LysM_dom_sf.
DR InterPro; IPR005038; Octapeptide.
DR InterPro; IPR003132; Protein_A_Ig-bd.
DR InterPro; IPR005877; YSIRK_signal_dom.
DR Pfam; PF02216; B; 5.
DR Pfam; PF00746; Gram_pos_anchor; 1.
DR Pfam; PF01476; LysM; 1.
DR Pfam; PF03373; Octapeptide; 12.
DR Pfam; PF04650; YSIRK_signal; 1.
DR SMART; SM00257; LysM; 1.
DR SUPFAM; SSF46997; SSF46997; 5.
DR SUPFAM; SSF54106; SSF54106; 1.
DR TIGRFAMs; TIGR01168; YSIRK_signal; 1.
DR PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
DR PROSITE; PS51782; LYSM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell wall; Direct protein sequencing; IgG-binding protein;
KW Peptidoglycan-anchor; Reference proteome; Repeat; Secreted; Signal;
KW Virulence.
FT SIGNAL 1..36
FT /evidence="ECO:0000269|PubMed:1638631,
FT ECO:0000269|PubMed:2938951"
FT CHAIN 37..485
FT /note="Immunoglobulin G-binding protein A"
FT /id="PRO_0000005653"
FT PROPEP 486..516
FT /note="Removed by sortase A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477,
FT ECO:0000269|PubMed:10427003, ECO:0000305|PubMed:7830549"
FT /id="PRO_0000005654"
FT REPEAT 37..92
FT /note="Immunoglobulin-binding region E"
FT /evidence="ECO:0000305|PubMed:2938951"
FT REPEAT 93..153
FT /note="Immunoglobulin-binding region D"
FT /evidence="ECO:0000305|PubMed:2938951"
FT REPEAT 154..211
FT /note="Immunoglobulin-binding region A"
FT /evidence="ECO:0000305|PubMed:2938951"
FT REPEAT 212..269
FT /note="Immunoglobulin-binding region B"
FT /evidence="ECO:0000305|PubMed:2938951"
FT REPEAT 270..327
FT /note="Immunoglobulin-binding region C"
FT /evidence="ECO:0000305|PubMed:2938951"
FT REPEAT 333..340
FT /note="2-1"
FT REPEAT 341..348
FT /note="2-2"
FT REPEAT 349..356
FT /note="2-3"
FT REPEAT 357..364
FT /note="2-4"
FT REPEAT 365..372
FT /note="2-5"
FT REPEAT 373..380
FT /note="2-6"
FT REPEAT 381..388
FT /note="2-7"
FT REPEAT 389..396
FT /note="2-8"
FT REPEAT 397..404
FT /note="2-9"
FT REPEAT 405..412
FT /note="2-10"
FT REPEAT 413..420
FT /note="2-11"
FT DOMAIN 421..465
FT /note="LysM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT REGION 318..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 333..420
FT /note="11 X 8 AA approximate tandem repeats"
FT REGION 467..487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 7..18
FT /note="YSIRK-G/S signaling motif"
FT /evidence="ECO:0000305|PubMed:12700270"
FT MOTIF 482..486
FT /note="LPXTG sorting signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477,
FT ECO:0000269|PubMed:1638631"
FT COMPBIAS 318..423
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 485
FT /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477,
FT ECO:0000305|PubMed:7701329, ECO:0000305|PubMed:9786922"
FT MUTAGEN 7..10
FT /note="Missing: Wild-type anchoring to cell wall, decreased
FT signal peptide processing rate, decreased amount of protein
FT on cell surface, overall IgG-binding capacity is slightly
FT decreased."
FT /evidence="ECO:0000269|PubMed:12700270"
FT MUTAGEN 15
FT /note="G->A: Altered processing of signal peptide,
FT precursor accumulates in membrane. More aberrant
FT processing; when associated with 18-A or deletion of 7-10."
FT /evidence="ECO:0000269|PubMed:12700270"
FT MUTAGEN 18
FT /note="S->A: Altered processing of signal peptide,
FT precursor accumulates in membrane and cytoplasm. More
FT aberrant processing; when associated with 15-A or deletion
FT of 7-10."
FT /evidence="ECO:0000269|PubMed:12700270"
FT MUTAGEN 478
FT /note="K->E: Wild-type anchoring to cell wall."
FT /evidence="ECO:0000269|PubMed:1638631"
FT MUTAGEN 482..516
FT /note="Missing: Protein secreted, no longer anchored to
FT cell wall."
FT /evidence="ECO:0000269|PubMed:1638631"
FT MUTAGEN 482..487
FT /note="Missing: Protein mis-sorted, found in cytoplasm,
FT membrane and cell wall, cells bind Ig poorly."
FT /evidence="ECO:0000269|PubMed:1638631"
FT MUTAGEN 483
FT /note="P->N: Protein mis-sorted, found in cytoplasm,
FT membrane and cell wall, cells bind Ig poorly."
FT /evidence="ECO:0000269|PubMed:1638631"
FT MUTAGEN 485
FT /note="T->A: Wild-type anchoring to cell wall."
FT /evidence="ECO:0000269|PubMed:1638631"
FT MUTAGEN 488..516
FT /note="Missing: Protein secreted, no longer anchored to
FT cell wall."
FT /evidence="ECO:0000269|PubMed:1638631"
FT MUTAGEN 512..516
FT /note="Missing: Protein secreted, no longer anchored to
FT cell wall."
FT /evidence="ECO:0000269|PubMed:1638631"
FT MUTAGEN 514..516
FT /note="Missing: Protein secreted, no longer anchored to
FT cell wall."
FT /evidence="ECO:0000269|PubMed:1638631"
FT MUTAGEN 515..516
FT /note="Missing: Protein mis-sorted, found in cytoplasm,
FT membrane and cell wall, cells bind Ig poorly."
FT /evidence="ECO:0000269|PubMed:1638631"
FT MUTAGEN 516
FT /note="L->C: Protein secreted, no longer anchored to cell
FT wall."
FT /evidence="ECO:0000269|PubMed:1638631"
FT MUTAGEN 516
FT /note="Missing: Wild-type anchoring to cell wall."
FT /evidence="ECO:0000269|PubMed:1638631"
FT CONFLICT 101
FT /note="N -> D (in Ref. 4; CAA24596)"
FT /evidence="ECO:0000305"
FT CONFLICT 370
FT /note="D -> DNNKPGKED (in Ref. 1; AAA26676)"
FT /evidence="ECO:0000305"
FT HELIX 102..113
FT /evidence="ECO:0007829|PDB:5U6A"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:1DEE"
FT HELIX 119..131
FT /evidence="ECO:0007829|PDB:5U6A"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:5U6A"
FT HELIX 136..149
FT /evidence="ECO:0007829|PDB:5U6A"
FT HELIX 218..229
FT /evidence="ECO:0007829|PDB:6K65"
FT HELIX 235..247
FT /evidence="ECO:0007829|PDB:6K65"
FT HELIX 249..251
FT /evidence="ECO:0007829|PDB:6K65"
FT HELIX 252..266
FT /evidence="ECO:0007829|PDB:6K65"
FT HELIX 276..287
FT /evidence="ECO:0007829|PDB:6SOW"
FT HELIX 295..305
FT /evidence="ECO:0007829|PDB:6SOW"
FT HELIX 307..309
FT /evidence="ECO:0007829|PDB:6SOW"
FT HELIX 310..324
FT /evidence="ECO:0007829|PDB:6SOW"
SQ SEQUENCE 516 AA; 56437 MW; C6FEFFF9E54BE1F0 CRC64;
MKKKNIYSIR KLGVGIASVT LGTLLISGGV TPAANAAQHD EAQQNAFYQV LNMPNLNADQ
RNGFIQSLKD DPSQSANVLG EAQKLNDSQA PKADAQQNNF NKDQQSAFYE ILNMPNLNEA
QRNGFIQSLK DDPSQSTNVL GEAKKLNESQ APKADNNFNK EQQNAFYEIL NMPNLNEEQR
NGFIQSLKDD PSQSANLLSE AKKLNESQAP KADNKFNKEQ QNAFYEILHL PNLNEEQRNG
FIQSLKDDPS QSANLLAEAK KLNDAQAPKA DNKFNKEQQN AFYEILHLPN LTEEQRNGFI
QSLKDDPSVS KEILAEAKKL NDAQAPKEED NNKPGKEDNN KPGKEDNNKP GKEDNNKPGK
EDNNKPGKED GNKPGKEDNK KPGKEDGNKP GKEDNKKPGK EDGNKPGKED GNKPGKEDGN
GVHVVKPGDT VNDIAKANGT TADKIAADNK LADKNMIKPG QELVVDKKQP ANHADANKAQ
ALPETGEENP FIGTTVFGGL SLALGAALLA GRRREL
