ID   EBPS_STAAB              Reviewed;         483 AA.
AC   Q2YY76;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Elastin-binding protein EbpS;
GN   Name=ebpS; OrderedLocusNames=SAB1343c;
OS   Staphylococcus aureus (strain bovine RF122 / ET3-1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=273036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=bovine RF122 / ET3-1;
RX   PubMed=17971880; DOI=10.1371/journal.pone.0001120;
RA   Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V.;
RT   "Molecular correlates of host specialization in Staphylococcus aureus.";
RL   PLoS ONE 2:E1120-E1120(2007).
CC   -!- FUNCTION: Promotes binding of soluble elastin peptides and tropoelastin
CC       to S.aureus cells although it is not able to promote bacterial
CC       adherence to immobilized elastin and, therefore, is not a microbial
CC       surface component recognizing adhesive matrix molecule (MSCRAMM).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- DOMAIN: The elastin-binding domain is located between residues 13-33 at
CC       the surface-exposed N-terminus, whereas the C-terminus, containing the
CC       LysM peptidoglycan-binding domain, is not exposed on the surface of
CC       intact cells and presumably remains buried within the peptidoglycan.
CC       The presence of the TNSHQD sequence, corresponding to residues 18-23,
CC       is essential for EbpS activity but not sufficient, additional flanking
CC       amino acids in the amino- or carboxy-terminal are required for elastin
CC       recognition (By similarity). {ECO:0000250}.
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DR   EMBL; AJ938182; CAI81032.1; -; Genomic_DNA.
DR   RefSeq; WP_000069313.1; NC_007622.1.
DR   AlphaFoldDB; Q2YY76; -.
DR   SMR; Q2YY76; -.
DR   KEGG; sab:SAB1343c; -.
DR   HOGENOM; CLU_043950_0_0_9; -.
DR   OMA; HHDRDKE; -.
DR   PRO; PR:Q2YY76; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   CDD; cd00118; LysM; 1.
DR   Gene3D; 3.10.350.10; -; 1.
DR   InterPro; IPR018392; LysM_dom.
DR   InterPro; IPR036779; LysM_dom_sf.
DR   Pfam; PF01476; LysM; 1.
DR   SMART; SM00257; LysM; 1.
DR   SUPFAM; SSF54106; SSF54106; 1.
DR   PROSITE; PS51782; LYSM; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Membrane; Transmembrane; Transmembrane helix.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..483
FT                   /note="Elastin-binding protein EbpS"
FT                   /id="PRO_0000271732"
FT   TRANSMEM        317..337
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          434..482
FT                   /note="LysM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT   REGION          1..311
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          14..34
FT                   /note="Elastin-binding"
FT                   /evidence="ECO:0000250"
FT   REGION          348..437
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..41
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        68..89
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        107..157
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        158..178
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        179..204
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        245..261
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        293..311
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        357..397
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        398..437
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   483 AA;  52976 MW;  0F83201A1C52BFA5 CRC64;
     MSNNFKDDFE KNRQSIDTNS HQDHTEEVEK DQSELEHQDT IENTEQQFPP RNAQRRKRRR
     DLATNHNKQV HNESQTSEDN VQNEAGTIDD HQVESSHSTE SQEPSHQDST PQHEEEYYNK
     NAFAMDKSHP EPIEDNDKHE TVKDAENNTE HSTVSDKSEA EQSQQPKPYF ATGANQANTS
     KDKHDDVTVK QYKDESKDHH SGKKGAAIGA GTAGVAGAMA ASKAKKHSND AQNKSNSGKA
     NNSTEDKASQ DKSKEHHNGK KGAAIGAGTA GLAGGAASKS ASAASKPHAS NNASQNHDEH
     DHHDRDKERK KGGMAKVLLP LIAAVLIIGA LAIFGGMALN NHNNGTKENK IANTNKNNAD
     ESKDKDTSKD ASKDKSKSTD SDKSKEDQDK ATKDESDNDQ NNANQANNQA QNNQNQQQAN
     QNQQQQQQRQ GGGQRHTVNG QENLYRIAIQ YYGSGSPENV EKIRRANGLS GNNIRNGQQI
     VIP