ID   EBPS_STAA3              Reviewed;         486 AA.
AC   Q2FGW1;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Elastin-binding protein EbpS;
GN   Name=ebpS; OrderedLocusNames=SAUSA300_1370;
OS   Staphylococcus aureus (strain USA300).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=367830;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=USA300;
RX   PubMed=16517273; DOI=10.1016/s0140-6736(06)68231-7;
RA   Diep B.A., Gill S.R., Chang R.F., Phan T.H., Chen J.H., Davidson M.G.,
RA   Lin F., Lin J., Carleton H.A., Mongodin E.F., Sensabaugh G.F.,
RA   Perdreau-Remington F.;
RT   "Complete genome sequence of USA300, an epidemic clone of community-
RT   acquired meticillin-resistant Staphylococcus aureus.";
RL   Lancet 367:731-739(2006).
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:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
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; CP000255; ABD21237.1; -; Genomic_DNA.
DR   RefSeq; WP_000069282.1; NZ_CP027476.1.
DR   AlphaFoldDB; Q2FGW1; -.
DR   SMR; Q2FGW1; -.
DR   EnsemblBacteria; ABD21237; ABD21237; SAUSA300_1370.
DR   KEGG; saa:SAUSA300_1370; -.
DR   HOGENOM; CLU_043950_0_0_9; -.
DR   OMA; HHDRDKE; -.
DR   PRO; PR:Q2FGW1; -.
DR   Proteomes; UP000001939; Chromosome.
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..486
FT                   /note="Elastin-binding protein EbpS"
FT                   /id="PRO_0000271740"
FT   TOPO_DOM        2..204
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        205..225
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        226..319
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        320..340
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        341..486
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          437..485
FT                   /note="LysM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT   REGION          1..314
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          14..34
FT                   /note="Elastin-binding"
FT                   /evidence="ECO:0000250"
FT   REGION          351..440
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..179
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        180..204
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        248..264
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        296..314
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        360..400
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        401..440
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   486 AA;  53221 MW;  70173FD572F47AD8 CRC64;
     MSNNFKDDFE KNRQSIDTNS HQDHTEDVEK DQSELEHQDT IENTEQQFPP RNAQRRKRRR
     DLATNHNKQV HNESQTSEDN VQNEAGTIDD RQVESSHSTE SQEPSHQDST PQHEEEYYNK
     NAFAMDKSHP EPIEDNDKHD TIKNAENNTE HSTVSDKSEA EQSQQPKPYF TTGANQSETS
     KNEHDNDSVK QDQDEPKEHH NGKKAAAIGA GTAGVAGAAG AMAASKAKKH SNDAQNKSNS
     GKANNSTEDK ASQDKSKDHH NGKKGAAIGA GTAGLAGGAA SKSASAASKP HASNNASQNH
     DEHDNHDRDK ERKKGGMAKV LLPLIAAVLI IGALAIFGGM ALNNHNNGTK ENKIANTNKN
     NADESKDKDT SKDASKDKSK STDSDKSKED QDKATKDESD NDQNNANQAN NQAQNNQNQQ
     QANQNQQQQQ QRQGGGQRHT VNGQENLYRI AIQYYGSGSP ENVEKIRRAN GLSGNNIRNG
     QQIVIP