EBPS_STAAU
ID EBPS_STAAU Reviewed; 486 AA.
AC Q53630; Q9R5R5; Q9R5R6;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=Elastin-binding protein EbpS;
GN Name=ebpS;
OS Staphylococcus aureus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1280;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 60-71 AND 126-144,
RP AND FUNCTION.
RC STRAIN=ATCC 12598 / Cowan 1 / DSM 20372 / NCIMB 11787 / NCTC 8530;
RX PubMed=8663124; DOI=10.1074/jbc.271.26.15803;
RA Park P.W., Rosenbloom J., Abrams W.R., Rosenbloom J., Mecham R.P.;
RT "Molecular cloning and expression of the gene for elastin-binding protein
RT (ebpS) in Staphylococcus aureus.";
RL J. Biol. Chem. 271:15803-15809(1996).
RN [2]
RP SEQUENCE REVISION.
RC STRAIN=ATCC 12598 / Cowan 1 / DSM 20372 / NCIMB 11787 / NCTC 8530;
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 PROTEIN SEQUENCE OF 2-19, AND FUNCTION.
RC STRAIN=8095, ATCC 10832 / Wood 46, and
RC ATCC 12598 / Cowan 1 / DSM 20372 / NCIMB 11787 / NCTC 8530;
RX PubMed=1744133; DOI=10.1016/s0021-9258(18)54510-5;
RA Park P.W., Roberts D.D., Grosso L.E., Parks W.C., Rosenbloom J.,
RA Abrams W.R., Mecham R.P.;
RT "Binding of elastin to Staphylococcus aureus.";
RL J. Biol. Chem. 266:23399-23406(1991).
RN [4]
RP FUNCTION, ELASTIN-BINDING DOMAIN, AND MUTAGENESIS OF ASP-23.
RC STRAIN=ATCC 12598 / Cowan 1 / DSM 20372 / NCIMB 11787 / NCTC 8530;
RX PubMed=9915819; DOI=10.1074/jbc.274.5.2845;
RA Park P.W., Broekelmann T.J., Mecham B.R., Mecham R.P.;
RT "Characterization of the elastin binding domain in the cell-surface 25-kDa
RT elastin-binding protein of Staphylococcus aureus (EbpS).";
RL J. Biol. Chem. 274:2845-2850(1999).
RN [5]
RP FUNCTION.
RC STRAIN=ATCC 12598 / Cowan 1 / DSM 20372 / NCIMB 11787 / NCTC 8530, Newman,
RC and P1;
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:15234962, ECO:0000269|PubMed:1744133,
CC ECO:0000269|PubMed:8663124, ECO:0000269|PubMed:9915819}.
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.
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DR EMBL; U48826; AAC44135.2; -; Genomic_DNA.
DR RefSeq; WP_000069298.1; NZ_WKIW01000001.1.
DR AlphaFoldDB; Q53630; -.
DR SMR; Q53630; -.
DR PRO; PR:Q53630; -.
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; Direct protein sequencing; Membrane; Transmembrane;
KW Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1744133"
FT CHAIN 2..486
FT /note="Elastin-binding protein EbpS"
FT /id="PRO_0000271731"
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 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 98..116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..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 247..264
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..297
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..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"
FT MUTAGEN 23
FT /note="D->N: Abolishes binding to elastin."
FT /evidence="ECO:0000269|PubMed:9915819"
FT CONFLICT 15
FT /note="S -> Q (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 16
FT /note="I -> S (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 486 AA; 53080 MW; 62904CF86C1F56B8 CRC64;
MSNNFKDDFE KNRQSIDTNS HQDHTEDVEK DQSELEHQDT IENTEQQFPP RNAQRRKRRR
DLATNHNKQV HNESQTSEDN VQNEAGTIDD RQVESSHSTE SQEPSHQDST PQHEEGYYNK
NAFAMDKSHP EPIEDNDKHE TIKEAENNTE HSTVSDKSEA EQSQQPKPYF ATGANQANTS
KDKHDDVTVK QDKDESKDHH SGKKGAAIGA GTAGVAGAAG AMGVSKAKKH SNDAQNKSNS
GKVNNSTEDK ASEDKSKEHH NGKKGAAIGA GTAGLAGGAA SNSASAASKP HASNNASQNN
DEHDHHDRDK ERKKGGMAKV LLPLIAAVLI IGALAIFGGM ALNNHNNGTK ENKIANTNKN
NADESKDKDT SKDASKDKSK STDSDKSKDD QDKATKDESD NDQNNANQAN NQAQNNQNQQ
QANQNQQQQQ QRQGGGQRHT VNGQENLYRI AIQYYGSGSP ENVEKIRRAN GLSGNNIRNG
QQIVIP
