EBPS_STAAC
ID EBPS_STAAC Reviewed; 486 AA.
AC Q5HFU2;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 102.
DE RecName: Full=Elastin-binding protein EbpS;
GN Name=ebpS; OrderedLocusNames=SACOL1522;
OS Staphylococcus aureus (strain COL).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93062;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COL;
RX PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA Fraser C.M.;
RT "Insights on evolution of virulence and resistance from the complete genome
RT analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT strain.";
RL J. Bacteriol. 187:2426-2438(2005).
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; CP000046; AAW36716.1; -; Genomic_DNA.
DR RefSeq; WP_000069282.1; NC_002951.2.
DR AlphaFoldDB; Q5HFU2; -.
DR SMR; Q5HFU2; -.
DR EnsemblBacteria; AAW36716; AAW36716; SACOL1522.
DR KEGG; sac:SACOL1522; -.
DR HOGENOM; CLU_043950_0_0_9; -.
DR OMA; HHDRDKE; -.
DR PRO; PR:Q5HFU2; -.
DR Proteomes; UP000000530; 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_0000271733"
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
