EBPS_STAAE
ID EBPS_STAAE Reviewed; 486 AA.
AC A6QH29;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=Elastin-binding protein EbpS;
GN Name=ebpS; OrderedLocusNames=NWMN_1389;
OS Staphylococcus aureus (strain Newman).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=426430;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Newman;
RX PubMed=17951380; DOI=10.1128/jb.01000-07;
RA Baba T., Bae T., Schneewind O., Takeuchi F., Hiramatsu K.;
RT "Genome sequence of Staphylococcus aureus strain Newman and comparative
RT analysis of staphylococcal genomes: polymorphism and evolution of two major
RT pathogenicity islands.";
RL J. Bacteriol. 190:300-310(2008).
RN [2]
RP FUNCTION IN ELASTIN BINDING, AND SUBCELLULAR LOCATION.
RX PubMed=11684686; DOI=10.1074/jbc.m107621200;
RA Downer R., Roche F.M., Park P.W., Mecham R.P., Foster T.J.;
RT "The elastin-binding protein of Staphylococcus aureus (EbpS) is expressed
RT at the cell surface as an integral membrane protein and not as a cell-wall
RT associated protein.";
RL J. Biol. Chem. 277:243-250(2002).
RN [3]
RP FUNCTION.
RX PubMed=15234962; DOI=10.1074/jbc.m402122200;
RA Roche F.M., Downer R., Keane F., Speziale P., Park P.W., Foster T.J.;
RT "The N-terminal A domain of fibronectin-binding proteins A and B promotes
RT adhesion of Staphylococcus aureus to elastin.";
RL J. Biol. Chem. 279:38433-38440(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:0000269|PubMed:11684686, ECO:0000269|PubMed:15234962}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11684686};
CC Single-pass membrane protein {ECO:0000269|PubMed:11684686}.
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; AP009351; BAF67661.1; -; Genomic_DNA.
DR RefSeq; WP_000069282.1; NZ_CP023390.1.
DR AlphaFoldDB; A6QH29; -.
DR SMR; A6QH29; -.
DR EnsemblBacteria; BAF67661; BAF67661; NWMN_1389.
DR KEGG; sae:NWMN_1389; -.
DR HOGENOM; CLU_043950_0_0_9; -.
DR OMA; HHDRDKE; -.
DR PRO; PR:A6QH29; -.
DR Proteomes; UP000006386; 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 1: Evidence at protein level;
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_0000324103"
FT TRANSMEM 320..340
FT /note="Helical"
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
