PSRP_STRPN
ID PSRP_STRPN Reviewed; 4776 AA.
AC A0A0H2URK1;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 25-MAY-2022, entry version 34.
DE RecName: Full=Pneumococcal serine-rich repeat protein {ECO:0000303|PubMed:16861665};
DE Short=PsrP {ECO:0000303|PubMed:16861665};
DE AltName: Full=Adhesin PsrP {ECO:0000305};
DE AltName: Full=Serine-rich repeat protein PsrP;
DE Flags: Precursor;
GN Name=psrP {ECO:0000303|PubMed:16861665}; OrderedLocusNames=SP_1772;
OS Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=170187;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], DISCUSSION OF SEQUENCE, AND
RP DOMAIN.
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=11463916; DOI=10.1126/science.1061217;
RA Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT "Complete genome sequence of a virulent isolate of Streptococcus
RT pneumoniae.";
RL Science 293:498-506(2001).
RN [2]
RP FUNCTION, DOMAIN, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=16861665; DOI=10.1128/iai.00316-06;
RA Obert C., Sublett J., Kaushal D., Hinojosa E., Barton T., Tuomanen E.I.,
RA Orihuela C.J.;
RT "Identification of a candidate Streptococcus pneumoniae core genome and
RT regions of diversity correlated with invasive pneumococcal disease.";
RL Infect. Immun. 74:4766-4777(2006).
RN [3]
RP FUNCTION IN HOST CELL ADHERENCE, DOMAIN, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=18507531; DOI=10.1086/589775;
RA Rose L., Shivshankar P., Hinojosa E., Rodriguez A., Sanchez C.J.,
RA Orihuela C.J.;
RT "Antibodies against PsrP, a novel Streptococcus pneumoniae adhesin, block
RT adhesion and protect mice against pneumococcal challenge.";
RL J. Infect. Dis. 198:375-383(2008).
RN [4]
RP DISCUSSION OF SEQUENCE.
RX PubMed=19202081; DOI=10.1099/mic.0.025221-0;
RA Zhou M., Wu H.;
RT "Glycosylation and biogenesis of a family of serine-rich bacterial
RT adhesins.";
RL Microbiology 155:317-327(2009).
RN [5]
RP FUNCTION, INTERACTION WITH HUMAN AND MOUSE KERATIN 10, SUBCELLULAR
RP LOCATION, INDUCTION, GLYCOSYLATION, DOMAIN, AND BIOTECHNOLOGY.
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=19627498; DOI=10.1111/j.1365-2958.2009.06796.x;
RA Shivshankar P., Sanchez C., Rose L.F., Orihuela C.J.;
RT "The Streptococcus pneumoniae adhesin PsrP binds to keratin 10 on lung
RT cells.";
RL Mol. Microbiol. 73:663-679(2009).
RN [6]
RP FUNCTION IN BIOFILM FORMATION, INDUCTION DURING BIOFILM FORMATION, DOMAIN,
RP AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=20714350; DOI=10.1371/journal.ppat.1001044;
RA Sanchez C.J., Shivshankar P., Stol K., Trakhtenbroit S., Sullam P.M.,
RA Sauer K., Hermans P.W., Orihuela C.J.;
RT "The pneumococcal serine-rich repeat protein is an intra-species bacterial
RT adhesin that promotes bacterial aggregation in vivo and in biofilms.";
RL PLoS Pathog. 6:E1001044-E1001044(2010).
RN [7]
RP GLYCOSYLATION AT SER-73; SER-75; SER-76; SER-78; SER-80; SER-82; SER-94;
RP SER-100; SER-108; SER-110; SER-118; SER-120 AND SER-121.
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=24936067; DOI=10.1074/jbc.m114.581934;
RA Shi W.W., Jiang Y.L., Zhu F., Yang Y.H., Shao Q.Y., Yang H.B., Ren Y.M.,
RA Wu H., Chen Y., Zhou C.Z.;
RT "Structure of a novel O-linked N-acetyl-D-glucosamine (O-GlcNAc)
RT transferase, GtfA, reveals insights into the glycosylation of pneumococcal
RT serine-rich repeat adhesins.";
RL J. Biol. Chem. 289:20898-20907(2014).
RN [8]
RP DISRUPTION PHENOTYPE.
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=28456649; DOI=10.1016/j.micinf.2017.04.003;
RA Bandara M., Skehel J.M., Kadioglu A., Collinson I., Nobbs A.H.,
RA Blocker A.J., Jenkinson H.F.;
RT "The accessory Sec system (SecY2A2) in Streptococcus pneumoniae is involved
RT in export of pneumolysin toxin, adhesion and biofilm formation.";
RL Microbes Infect. 19:402-412(2017).
RN [9]
RP COMPLEX GLYCOSYLATION.
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=28246170; DOI=10.1074/jbc.m116.770446;
RA Jiang Y.L., Jin H., Yang H.B., Zhao R.L., Wang S., Chen Y., Zhou C.Z.;
RT "Defining the enzymatic pathway for polymorphic O-glycosylation of the
RT pneumococcal serine-rich repeat protein PsrP.";
RL J. Biol. Chem. 292:6213-6224(2017).
RN [10] {ECO:0007744|PDB:3ZGH, ECO:0007744|PDB:3ZGI}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 187-385, INTERACTION WITH HUMAN
RP KERATIN 10, DOMAIN, AND MUTAGENESIS OF LYS-230; MET-276; VAL-289; ILE-293;
RP TYR-304; MET-309; TYR-316; TRP-318; ASN-320; MET-324 AND PHE-328.
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=24430336; DOI=10.1098/rsob.130090;
RA Schulte T., Lofling J., Mikaelsson C., Kikhney A., Hentrich K.,
RA Diamante A., Ebel C., Normark S., Svergun D., Henriques-Normark B.,
RA Achour A.;
RT "The basic keratin 10-binding domain of the virulence-associated
RT pneumococcal serine-rich protein PsrP adopts a novel MSCRAMM fold.";
RL Open Biol. 4:130090-130090(2014).
RN [11]
RP ERRATUM OF PUBMED:24430336.
RX DOI=10.1098/rsob.140172;
RA Schulte T., Lofling J., Mikaelsson C., Kikhney A., Hentrich K.,
RA Diamante A., Ebel C., Normark S., Svergun D., Henriques-Normark B.,
RA Achour A.;
RL Open Biol. 4:140172-140172(2014).
RN [12] {ECO:0007744|PDB:5JUI}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 187-378, FUNCTION, DOMAIN,
RP DNA-BINDING, PROTEOLYTIC CLEAVAGE BY HOST FURIN, AND MUTAGENESIS OF
RP 165-ARG--ARG-168.
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=27582320; DOI=10.1038/srep32371;
RA Schulte T., Mikaelsson C., Beaussart A., Kikhney A., Deshmukh M.,
RA Wolniak S., Pathak A., Ebel C., Lofling J., Fogolari F.,
RA Henriques-Normark B., Dufrene Y.F., Svergun D., Nygren P.A., Achour A.;
RT "The BR domain of PsrP interacts with extracellular DNA to promote
RT bacterial aggregation; structural insights into pneumococcal biofilm
RT formation.";
RL Sci. Rep. 6:32371-32371(2016).
CC -!- FUNCTION: Protein that allows bacteria to adhere to mammalian host
CC cells. Required for full virulence in mouse infection models when
CC infected intranasally (PubMed:16861665). Required for adhesion to host
CC cells in vitro and for persistence in the lower respiratory tract
CC (PubMed:18507531). Binds host keratin 10 (KRT10) on lung cells which
CC mediates adhesion via the C-terminus of the basic region (BR, residues
CC 273-341); glycosylation of either protein is not required for the
CC interaction (PubMed:19627498). A region in the N-terminus (residues
CC 122-166) self aggregates, contributing to mature biofilm formation
CC (PubMed:20714350). The basic region (BR, residues 187-385) also self
CC aggregates; the BR binds DNA which enhances self aggregation
CC (PubMed:27582320). {ECO:0000269|PubMed:16861665,
CC ECO:0000269|PubMed:18507531, ECO:0000269|PubMed:19627498,
CC ECO:0000269|PubMed:20714350, ECO:0000269|PubMed:27582320}.
CC -!- SUBUNIT: Binds to human and mouse protein keratin 10 (KRT10).
CC {ECO:0000269|PubMed:19627498, ECO:0000269|PubMed:24430336}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|PROSITE-
CC ProRule:PRU00477, ECO:0000269|PubMed:19627498}; Peptidoglycan-anchor
CC {ECO:0000255|PROSITE-ProRule:PRU00477}. Cell surface
CC {ECO:0000269|PubMed:19627498}.
CC -!- INDUCTION: Expressed in exponential phase (at protein level)
CC (PubMed:19627498). About 47-fold induced during biofilm formation
CC versus planktonic (in liquid culture) (PubMed:20714350).
CC {ECO:0000269|PubMed:19627498, ECO:0000269|PubMed:20714350}.
CC -!- DOMAIN: Has 3 domains; serine-rich repeat region 1 (SRR1) with 8
CC imperfect repeats of the sequence SASASAST, a basic region (BR) and
CC serine-rich repeat region 2 (SRR2) with 539 imperfect repeats of the
CC sequence SASASAST (PubMed:11463916) (Probable). A construct expressing
CC SRR1 plus BR binds to a human pneumocyte cell line and prevents
CC bacteria binding to human pneumocyte cells in a dose-dependent manner;
CC antibodies against the same domain partially inhibit host cell
CC adherence (PubMed:18507531). The BR domain mediates host cell adhesion;
CC its deletion prevents binding to unencapsulated host cells. A BR
CC subdomain (residues 273-341) binds to host keratin 10 (KRT10)
CC (PubMed:19627498). The KRT10-binding subdomain forms a compressed
CC barrel, which probably binds the C-terminus of KRT10 via a series of
CC ordered loops (PubMed:24430336). The SRR2 domain probably extends the
CC BR domain outside of the bacterial capsular polysaccharide, possibly by
CC forming a long filament (Probable). The BR domain is also required for
CC PsrP to be able to mediate biofilm formation. A subdomain (residues
CC 122-166) binds to itself, suggesting it may be responsible for self
CC aggregation; self interaction occurs whether the protein is
CC glycosylated or not. The self aggregation and K10 subdomains function
CC independently of each other (PubMed:20714350). Another subfragment of
CC the BR domain (residues 187-385) binds DNA and may be important in self
CC aggregation (PubMed:27582320). The predicted pI of the basic region is
CC 9.91 (PubMed:19202081). {ECO:0000269|PubMed:11463916,
CC ECO:0000269|PubMed:18507531, ECO:0000269|PubMed:19627498,
CC ECO:0000269|PubMed:20714350, ECO:0000269|PubMed:24430336,
CC ECO:0000269|PubMed:27582320, ECO:0000303|PubMed:19202081,
CC ECO:0000305|PubMed:16861665, ECO:0000305|PubMed:19627498}.
CC -!- PTM: Glycosylated (PubMed:19627498). Only truncated substrates greater
CC than 25 residues long are glycosylated by the Gtf1-Gtf2 complex in
CC vitro; only Ser residues have been seen to be glycosylated. Based on
CC electrophoretic mobility it is probable that most of the Ser residues
CC in SSR1 and SSR2 are O-GlcNAcylated (PubMed:24936067). Subsequent
CC glycosylation by up to 7 sugar transferases (Gtf3 and GlyAT, GlyB,
CC GlyD, GlyE, GlyF and GlyG) is able to generate very high sugar
CC polymorphism (PubMed:28246170). {ECO:0000269|PubMed:19627498,
CC ECO:0000269|PubMed:24936067, ECO:0000269|PubMed:28246170}.
CC -!- PTM: Can be cleaved by human furin protease; this fragment contributes
CC to self-aggregation and possibly biofilm formation in vitro.
CC {ECO:0000269|PubMed:27582320}.
CC -!- DISRUPTION PHENOTYPE: Significantly improved survival of intranasally
CC infected female BALB/cJ mice; bacteria infect nasal tissues normally
CC but do not progress into the blood (PubMed:16861665). Single deletion
CC or deletion of 15 genes (from psrP, SP_1772 to SP_1756, includes the
CC accessory Sec export proteins SecA2 and SecY2) and infection of female
CC BALB/cJ mice, shows the psrP-secY2A2 region is required for lung
CC infection and for infection to progress to blood. Mice infected
CC intraperitoneally with either deletion showed wild-type infection. Both
CC deletions have decreased adherence to lung but not pharynx or brain
CC cells. The psrP-secY2A2 region deletion has no effect on bacterial
CC growth rate, capsule levels, autolysis, or transformation
CC (PubMed:18507531). About 5-fold decreased aggregation of bacteria in
CC infected mouse nasopharynx and lung tissue. In vitro, significantly
CC decreased mature biofilm formation is seen; the large deletion mutant
CC (SP_1772 to SP_1756) is no more affected than the single psrP deletion.
CC Biofilm formation is partially restored by a truncated PsrP (residues
CC 1-734); the BR domain is required for this partial restoration
CC (PubMed:20714350). About 60% decreased biofilm formation, no change in
CC adherence to human lung pneumocytes (PubMed:28456649).
CC {ECO:0000269|PubMed:16861665, ECO:0000269|PubMed:18507531,
CC ECO:0000269|PubMed:20714350, ECO:0000269|PubMed:28456649}.
CC -!- BIOTECHNOLOGY: Mice vaccinated with residues 72-395 were protected
CC against subsequent infection, suggesting this would be a good candidate
CC for vaccine inclusion. {ECO:0000269|PubMed:19627498}.
CC -!- MISCELLANEOUS: Encoded in RD10, a pathogenicity island with an atypical
CC GC content that is associated with invasive pneumococcal disease.
CC Pathogenicity islands account for greater than half the genomic
CC diversity observed between isolates (PubMed:11463916, PubMed:16861665,
CC PubMed:19627498). The main function of this island seems to be correct
CC synthesis and export of this protein (PubMed:18507531,
CC PubMed:20714350). {ECO:0000269|PubMed:18507531,
CC ECO:0000269|PubMed:20714350, ECO:0000303|PubMed:11463916,
CC ECO:0000303|PubMed:16861665, ECO:0000303|PubMed:19627498}.
CC -!- MISCELLANEOUS: Normally a commensal colonizing bacteria of the
CC nasopharynx, invasive pneumococcal disease (IPD) is characterized by
CC bacterial spread from the nasopharynx to normally sterile sites such as
CC the lungs, blood, and brain. The young, the elderly and the
CC immunocompromised are at greatest risk for IPD.
CC {ECO:0000303|PubMed:18507531}.
CC -!- SIMILARITY: Belongs to the serine-rich repeat protein (SRRP) family.
CC {ECO:0000305}.
CC -!- CAUTION: O-glycosylation sites are annotated in SSR1 only. Residues at
CC similar position are probably glycosylated in SRR2 also. Experimental
CC sites were determined in a synthetic peptide glycosylated by addition
CC of GlcNAc in vitro by GtfA-GtfB; only 13 of 26 possible Ser and no Thr
CC were modified with GlcNAc in this experiment (PubMed:24936067). The
CC GlcNAc residues are subsequently further modified but the positions
CC were not proven in that experiment (PubMed:28246170).
CC {ECO:0000269|PubMed:24936067, ECO:0000269|PubMed:28246170}.
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DR EMBL; AE005672; AAK75846.1; -; Genomic_DNA.
DR PDB; 3ZGH; X-ray; 2.00 A; A=187-385.
DR PDB; 3ZGI; X-ray; 2.25 A; A/B/C=187-385.
DR PDB; 5JUI; X-ray; 2.10 A; A/B/C=187-378.
DR PDBsum; 3ZGH; -.
DR PDBsum; 3ZGI; -.
DR PDBsum; 5JUI; -.
DR SASBDB; A0A0H2URK1; -.
DR SMR; A0A0H2URK1; -.
DR STRING; 170187.SP_1772; -.
DR iPTMnet; A0A0H2URK1; -.
DR EnsemblBacteria; AAK75846; AAK75846; SP_1772.
DR KEGG; spn:SP_1772; -.
DR OMA; GNWSIDL; -.
DR Proteomes; UP000000585; Chromosome.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0009275; C:Gram-positive-bacterium-type cell wall; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0052031; P:modulation by symbiont of host defense response; IMP:UniProtKB.
DR GO; GO:0044010; P:single-species biofilm formation; IDA:UniProtKB.
DR InterPro; IPR019931; LPXTG_anchor.
DR InterPro; IPR026465; Ser_adhes_glycop.
DR Pfam; PF00746; Gram_pos_anchor; 1.
DR TIGRFAMs; TIGR04224; ser_adhes_Nterm; 1.
DR PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell adhesion; Cell wall; DNA-binding; Glycoprotein;
KW Peptidoglycan-anchor; Repeat; Secreted; Signal; Virulence.
FT SIGNAL 1..72
FT /evidence="ECO:0000305|PubMed:16861665"
FT CHAIN 73..4776
FT /note="Pneumococcal serine-rich repeat protein"
FT /id="PRO_0000447031"
FT PROPEP 4744..4776
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT /id="PRO_0000447032"
FT REGION 73..121
FT /note="Serine-rich repeat region 1, SRR1"
FT /evidence="ECO:0000303|PubMed:16861665"
FT REGION 86..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 122..394
FT /note="Basic region, BR"
FT /evidence="ECO:0000303|PubMed:16861665"
FT REGION 122..166
FT /note="Self aggregating domain"
FT /evidence="ECO:0000269|PubMed:20714350"
FT REGION 273..341
FT /note="Keratin 10-binding domain, cell-type specific
FT binding to lung-derived cells"
FT /evidence="ECO:0000269|PubMed:19627498"
FT REGION 395..4712
FT /note="Serine-rich repeat region 2, SRR2"
FT /evidence="ECO:0000303|PubMed:16861665"
FT REGION 481..627
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 861..889
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 925..965
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1052..1085
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1123..1153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1171..1199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1311..1357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1671..1731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1792..1863
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2105..2133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2169..2209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2296..2329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2367..2397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2415..2443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2571..2631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2737..2805
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2855..3113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3347..3375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3411..3451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3538..3571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3609..3639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3657..3685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3797..3843
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4167..4197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4215..4243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4355..4401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4706..4747
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 164..168
FT /note="Host furin cleavage recognition"
FT /evidence="ECO:0000269|PubMed:27582320"
FT MOTIF 4740..4744
FT /note="LPXTG sorting signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT MOD_RES 4743
FT /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT CARBOHYD 73
FT /note="O-linked (GlcNAc...) serine"
FT /evidence="ECO:0000305|PubMed:24936067,
FT ECO:0000305|PubMed:28246170"
FT CARBOHYD 75
FT /note="O-linked (GlcNAc...) serine"
FT /evidence="ECO:0000305|PubMed:24936067,
FT ECO:0000305|PubMed:28246170"
FT CARBOHYD 76
FT /note="O-linked (GlcNAc...) serine"
FT /evidence="ECO:0000305|PubMed:24936067,
FT ECO:0000305|PubMed:28246170"
FT CARBOHYD 78
FT /note="O-linked (GlcNAc...) serine"
FT /evidence="ECO:0000305|PubMed:24936067,
FT ECO:0000305|PubMed:28246170"
FT CARBOHYD 80
FT /note="O-linked (GlcNAc...) serine"
FT /evidence="ECO:0000305|PubMed:24936067,
FT ECO:0000305|PubMed:28246170"
FT CARBOHYD 82
FT /note="O-linked (GlcNAc...) serine"
FT /evidence="ECO:0000305|PubMed:24936067,
FT ECO:0000305|PubMed:28246170"
FT CARBOHYD 94
FT /note="O-linked (GlcNAc...) serine"
FT /evidence="ECO:0000305|PubMed:24936067,
FT ECO:0000305|PubMed:28246170"
FT CARBOHYD 100
FT /note="O-linked (GlcNAc...) serine"
FT /evidence="ECO:0000305|PubMed:24936067,
FT ECO:0000305|PubMed:28246170"
FT CARBOHYD 108
FT /note="O-linked (GlcNAc...) serine"
FT /evidence="ECO:0000305|PubMed:24936067,
FT ECO:0000305|PubMed:28246170"
FT CARBOHYD 110
FT /note="O-linked (GlcNAc...) serine"
FT /evidence="ECO:0000305|PubMed:24936067,
FT ECO:0000305|PubMed:28246170"
FT CARBOHYD 118
FT /note="O-linked (GlcNAc...) serine"
FT /evidence="ECO:0000305|PubMed:24936067,
FT ECO:0000305|PubMed:28246170"
FT CARBOHYD 120
FT /note="O-linked (GlcNAc...) serine"
FT /evidence="ECO:0000305|PubMed:24936067,
FT ECO:0000305|PubMed:28246170"
FT CARBOHYD 121
FT /note="O-linked (GlcNAc...) serine"
FT /evidence="ECO:0000305|PubMed:24936067,
FT ECO:0000305|PubMed:28246170"
FT MUTAGEN 165..168
FT /note="RRKR->SRKS: No longer cleaved in vitro by human
FT furin protease."
FT /evidence="ECO:0000269|PubMed:27582320"
FT MUTAGEN 230
FT /note="K->A: No change in binding of BR (187-385) to host
FT keratin 10 (KRT10)."
FT /evidence="ECO:0000269|PubMed:24430336"
FT MUTAGEN 276
FT /note="M->A: About 20% binding of BR to host KRT10."
FT /evidence="ECO:0000269|PubMed:24430336"
FT MUTAGEN 289
FT /note="V->A: About 20% binding of BR to host KRT10."
FT /evidence="ECO:0000269|PubMed:24430336"
FT MUTAGEN 293
FT /note="I->A: About 20% binding of BR to host KRT10."
FT /evidence="ECO:0000269|PubMed:24430336"
FT MUTAGEN 304
FT /note="Y->A: 50% binding of BR to host KRT10."
FT /evidence="ECO:0000269|PubMed:24430336"
FT MUTAGEN 309
FT /note="M->A: 40% binding of BR to host KRT10."
FT /evidence="ECO:0000269|PubMed:24430336"
FT MUTAGEN 316
FT /note="Y->A: About 20% binding of BR to host KRT10."
FT /evidence="ECO:0000269|PubMed:24430336"
FT MUTAGEN 318
FT /note="W->A: About 20% binding of BR to host KRT10."
FT /evidence="ECO:0000269|PubMed:24430336"
FT MUTAGEN 320
FT /note="N->A: No change in binding of BR to host KRT10."
FT /evidence="ECO:0000269|PubMed:24430336"
FT MUTAGEN 324
FT /note="M->A: About 20% binding of BR to host KRT10."
FT /evidence="ECO:0000269|PubMed:24430336"
FT MUTAGEN 328
FT /note="F->A: About 20% binding of BR to host KRT10."
FT /evidence="ECO:0000269|PubMed:24430336"
FT STRAND 208..218
FT /evidence="ECO:0007829|PDB:3ZGH"
FT TURN 219..222
FT /evidence="ECO:0007829|PDB:3ZGH"
FT STRAND 223..233
FT /evidence="ECO:0007829|PDB:3ZGH"
FT STRAND 235..247
FT /evidence="ECO:0007829|PDB:3ZGH"
FT TURN 249..251
FT /evidence="ECO:0007829|PDB:3ZGH"
FT STRAND 265..269
FT /evidence="ECO:0007829|PDB:3ZGH"
FT STRAND 277..279
FT /evidence="ECO:0007829|PDB:3ZGH"
FT STRAND 289..294
FT /evidence="ECO:0007829|PDB:3ZGH"
FT STRAND 300..307
FT /evidence="ECO:0007829|PDB:3ZGH"
FT STRAND 309..311
FT /evidence="ECO:0007829|PDB:3ZGH"
FT STRAND 313..318
FT /evidence="ECO:0007829|PDB:3ZGH"
FT STRAND 323..325
FT /evidence="ECO:0007829|PDB:3ZGH"
FT HELIX 326..329
FT /evidence="ECO:0007829|PDB:3ZGH"
FT TURN 330..332
FT /evidence="ECO:0007829|PDB:3ZGH"
FT STRAND 334..343
FT /evidence="ECO:0007829|PDB:3ZGH"
FT STRAND 350..352
FT /evidence="ECO:0007829|PDB:3ZGH"
FT STRAND 357..360
FT /evidence="ECO:0007829|PDB:3ZGI"
FT TURN 366..370
FT /evidence="ECO:0007829|PDB:3ZGH"
FT STRAND 373..375
FT /evidence="ECO:0007829|PDB:3ZGH"
SQ SEQUENCE 4776 AA; 412239 MW; C84E039E1521C17E CRC64;
MTETVEDKVS HSITGLDILK GIVAAGAVIS GTVATQTKVF TNESAVLEKT VEKTDALATN
DTVVLGTIST SNSASSTSLS ASESASTSAS ESASTSASTS ASTSASESAS TSASTSISAS
STVVGSQTAA ATEATAKKVE EDRKKPASDY VASVTNVNLQ SYAKRRKRSV DSIEQLLASI
KNAAVFSGNT IVNGAPAINA SLNIAKSETK VYTGEGVDSV YRVPIYYKLK VTNDGSKLTF
TYTVTYVNPK TNDLGNISSM RPGYSIYNSG TSTQTMLTLG SDLGKPSGVK NYITDKNGRQ
VLSYNTSTMT TQGSGYTWGN GAQMNGFFAK KGYGLTSSWT VPITGTDTSF TFTPYAARTD
RIGINYFNGG GKVVESSTTS QSLSQSKSLS VSASQSASAS ASTSASASAS TSASASASTS
ASASASTSAS VSASTSASAS ASTSASASAS TSASESASTS ASASASTSAS ASASTSASAS
ASTSASESAS TSASASASTS ASESASTSAS ASASTSASAS ASTSASGSAS TSTSASASTS
ASASASTSAS ASASISASES ASTSASESAS TSTSASASTS ASESASTSAS ASASTSASAS
ASTSASASAS TSASASTSAS ESASTSASAS ASTSASASAS TSASASASTS ASASASTSAS
VSASTSASAS ASTSASASAS TSASESASTS ASASASTSAS ASASTSASAS ASTSASASAS
TSASASASTS ASESASTSAS ASASTSASAS ASTSASASAS TSASASASTS ASASASISAS
ESASTSASAS ASTSASASAS TSASASASTS ASESASTSAS ASASTSASAS ASTSASASAS
TSASASASTS ASASASTSAS ASASTSASES ASTSASASAS TSASESASTS ASASASTSAS
ASASTSASAS ASTSASASAS TSASASASTS ASASASTSAS ASTSASESAS TSASASASTS
ASASASTSAS ASASTSASES ASTSASASAS TSASASASTS ASASASTSAS ASASTSASAS
ASISASESAS TSASASASTS ASVSASTSAS ASASTSASES ASTSASASAS TSASESASTS
ASASASTSAS ASASISASES ASTSASASAS TSASASASTS ASASASTSAS ESASTSTSAS
ASTSASESAS TSASASASTS ASASASTSAS ASASTSASAS ASTSASASTS ASESASTSAS
ASASTSASAS ASTSASASAS TSASASASTS ASASASTSAS ASASTSASAS ASTSASASAS
TSASESASTS ASASASTSAS ASASTSASAS ASTSASASAS TSASVSASTS ASESASTSAS
ASASTSASAS ASTSASESAS TSASASASTS ASESASTSAS ASASTSASAS ASTSASASAS
TSASASASTS ASASASTSAS ASASTSASAS ASTSASASAS TSASASASTS ASASASTSAS
ASASTSASAS ASTSASASAS ISASESASTS ASASASTSAS ASASTSASVS ASTSASASAS
TSASASASIS ASESASTSAS ASASTSASAS ASTSASASAS TSASASASIS ASESASTSAS
ASASTSASAS ASTSASASAS TSASASASTS ASASASTSAS ASASTSASAS ASTSASASAS
TSASASASTS ASESASTSAS ASASTSASAS ASTSASASAS TSASVSASTS ASESASTSAS
ASASTSASAS ASTSASASAS TSASESASTS ASASASTSAS ASASTSASES ASTSASASAS
TSASASASTS ASASASTSAS ASASASTSAS ASASTSASAS ASTSASASAS ISASESASTS
ASESASTSTS ASASTSASES ASTSASASAS TSASASASTS ASASASTSAS ASTSASESAS
TSASASASTS ASASASTSAS ASASTSASAS ASTSASASAS TSASVSASTS ASASASTSAS
ASASTSASES ASTSASASAS TSASASASTS ASASASTSAS ASASTSASAS ASTSASESAS
TSASASASTS ASASASTSAS ASASTSASAS ASTSASASAS ISASESASTS ASASASTSAS
ASASTSASAS ASTSASESAS TSASASASTS ASASASTSAS ASASTSASAS ASTSASASAS
TSASASASTS ASESASTSAS ASASTSASES ASTSASASAS TSASASASTS ASASASTSAS
ASASTSASAS ASTSASASAS TSASASTSAS ESASTSASAS ASTSASASAS TSASASASTS
ASESASTSAS ASASTSASAS ASTSASASAS TSASASASTS ASASASISAS ESASTSASAS
ASTSASVSAS TSASASASTS ASESASTSAS ASASTSASES ASTSASASAS TSASASASIS
ASESASTSAS ASASTSASAS ASTSASASAS TSASESASTS TSASASTSAS ESASTSASAS
ASTSASASAS TSASASASTS ASASASTSAS ASTSASESAS TSASASASTS ASASASTSAS
ASASTSASAS ASTSASASAS TSASASASTS ASASASTSAS ASASTSASAS ASTSASASAS
TSASASASTS ASESASTSAS ASASTSASAS ASTSASASAS TSASVSASTS ASESASTSAS
ASASTSASAS ASTSASASAS TSASESASTS ASASASTSAS ASASTSASES ASTSASASAS
TSASASASTS ASASASTSAS ASASASTSAS ASASTSASAS ASTSASASAS ISASESASTS
ASASASASTS ASASASTSAS ASASTSASAS ASISASESAS TSASESASTS TSASASTSAS
ESASTSASAS ASTSASASAS TSASASASTS ASASTSASES ASTSASASAS TSASASASTS
ASASASTSAS ASASTSASAS ASTSASVSAS TSASASASTS ASASASTSAS ESASTSASAS
TSASESASTS ASASASTSAS ASASTSASAS ASTSASESAS TSASASASTS ASASASTSAS
ESASTSASAS ASTSASASAS TSASASASTS ASESASTSAS ASASTSASES ASTSASASAS
TSASASASTS ASGSASTSTS ASASTSASAS ASTSASASAS ISASESASTS ASESASTSTS
ASASTSASES ASTSASASAS TSASASASTS ASASASTSAS ASTSASESAS TSASASASTS
ASASASTSAS ASASTSASAS ASTSASVSAS TSASASASTS ASASASTSAS ESASTSASAS
ASTSASASAS TSASASASTS ASASASTSAS ASASTSASES ASTSASASAS TSASASASTS
ASASASTSAS ASASTSASAS ASISASESAS TSASASASTS ASASASTSAS ASASTSASES
ASTSASASAS TSASASASTS ASASASTSAS ASASTSASAS ASTSASASAS TSASESASTS
ASASASTSAS ESASTSASAS ASTSASASAS TSASASASTS ASASASTSAS ASASTSASAS
ASTSASASTS ASESASTSAS ASASTSASAS ASTSASASAS TSASESASTS ASASASTSAS
ASASTSASAS ASTSASASAS TSASASASIS ASESASTSAS ASASTSASVS ASTSASASAS
TSASESASTS ASASASTSAS ESASTSASAS ASTSASASAS ISASESASTS ASASASTSAS
ASASTSASAS ASTSASESAS TSTSASASTS ASESASTSAS ASASTSASAS ASTSASASAS
TSASASASTS ASASTSASES ASTSASASAS TSASASASTS ASASASTSAS ASASTSASAS
ASTSASASAS TSASASASTS ASASASTSAS ESASTSASAS ASTSASASAS TSASASASTS
ASASASTSAS VSASTSASES ASTSASASAS TSASASASTS ASESASTSAS ASASTSASES
ASTSASASAS TSASASASTS ASASASTSAS ASASTSASAS ASTSASASAS TSASASASTS
ASASASTSAS ASASTSASAS ASTSASASAS TSASASASTS ASASASISAS ESASTSASAS
ASTSASASAS TSASVSASTS ASASASTSAS ASASISASES ASTSASASAS TSASASASTS
ASASASTSAS ASASISASES ASTSASASAS TSASASASTS ASASASTSAS ASASTSASAS
ASTSASASAS TSASASASTS ASASASTSAS ASASTSASES ASTSASASAS TSASASASIS
ASESASTSAS ASASTSASAS ASTSASASAS TSASESASTS TSASASTSAS ESASTSASAS
ASTSASASAS TSASASASTS ASASASTSAS ASTSASESAS TSASASASTS ASASASTSAS
ASASTSASAS ASTSASASAS TSASASASTS ASASASTSAS ASASTSASES ASTSASASAS
TSASASASTS ASASASTSAS ASASTSASVS ASTSASESAS TSASASASTS ASASASTSAS
ESASTSASAS ASTSASESAS TSASASASTS ASASASTSAS ASASTSASAS ASTSASASAS
TSASASASTS ASASASTSAS ASASTSASAS ASTSASASAS TSASASASTS ASASASTSAS
ASASISASES ASTSASASAS TSASASASTS ASVSASTSAS ASASTSASAS ASISASESAS
TSASASASTS ASASASTSAS ASASTSASAS ASISASESAS TSASASASTS ASASASTSAS
ASASTSASAS ASTSASASAS TSASASASTS ASASASTSAS ASASTSASAS ASTSASASAS
TSASASASTS ASASASTSAS ASASTSASAS ASTSVSNSAN HSNSQVGNTS GSTGKSQKEL
PNTGTESSIG SVLLGVLAAV TGIGLVAKRR KRDEEE
