EBPS_STAAS
ID EBPS_STAAS Reviewed; 486 AA.
AC Q6G983;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=Elastin-binding protein EbpS;
GN Name=ebpS; OrderedLocusNames=SAS1421;
OS Staphylococcus aureus (strain MSSA476).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282459;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSSA476;
RX PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT for the rapid evolution of virulence and drug resistance.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
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; BX571857; CAG43198.1; -; Genomic_DNA.
DR RefSeq; WP_000069296.1; NC_002953.3.
DR AlphaFoldDB; Q6G983; -.
DR SMR; Q6G983; -.
DR KEGG; sas:SAS1421; -.
DR HOGENOM; CLU_043950_0_0_9; -.
DR OMA; HHDRDKE; -.
DR PRO; PR:Q6G983; -.
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_0000271735"
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..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 243..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; 53240 MW; 8859F271713E7218 CRC64;
MSNNFKDDFE KNRQSIDTNS HQDHTEDVEK DQSELEHQDT IENTEQQFPP RNAQRRKRRR
DLATNHNKQV HNESQTSEDN VQNEAGTIDD RQVESSHSTE SQEPSHQDST PQHEEEYYNK
NAFAMDKSHP EPIEDNDKHE TIKEAENNTE HSTVSDKSEA EQSQQPKPYF ATGANQANTS
KDKHDDVTVK QDKDESKDHH SGKKGAAIGA GTAGVAGAAG AMGVSKAKKH SNDAQNKSNS
DKSNNSTEDK VSQDKSKDHH NGKKGAAIGA GTAGLAGGAA SKSASAASKP HASNNASQNH
DEHDNHDRDK ERKKGGMAKV LLPLIAAVLI IGALAIFGGM ALNNHNNGTK ENKIANTNKN
NADESKDKDT SKDASKDKSK STDSDKSKED QDKATKDESD NDQNNANQAN NQAQNNQNQQ
QANQNQQQQQ QRQGGGQRHT VNGQENLYRI AIQYYGSGSP ENVEKIRRAN GLSGNNIRNG
QQIVIP
