ID   EMP_STAAE               Reviewed;         340 AA.
AC   A6QF98; P81684; Q9K2Q1; Q9L3L5;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 59.
DE   RecName: Full=Extracellular matrix protein-binding protein emp;
DE   Flags: Precursor;
GN   Name=ssp; OrderedLocusNames=NWMN_0758;
OS   Staphylococcus aureus (strain Newman).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=426430;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 27-63, BINDING
RP   ACTIVITY, AND SUBCELLULAR LOCATION.
RX   PubMed=11698365; DOI=10.1128/jb.183.23.6778-6786.2001;
RA   Hussain M.S., Becker K., von Eiff C., Schrenzel J., Peters G., Herrmann M.;
RT   "Identification and characterization of a novel 38.5-kilodalton cell
RT   surface protein of Staphylococcus aureus with extended-spectrum binding
RT   activity for extracellular matrix and plasma proteins.";
RL   J. Bacteriol. 183:6778-6786(2001).
RN   [2]
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   [3]
RP   INDUCTION.
RX   PubMed=15941988; DOI=10.1099/mic.0.27902-0;
RA   Harraghy N., Kormanec J., Wolz C., Homerova D., Goerke C., Ohlsen K.,
RA   Qazi S., Hill P., Herrmann M.;
RT   "Sae is essential for expression of the staphylococcal adhesins Eap and
RT   Emp.";
RL   Microbiology 151:1789-1800(2005).
CC   -!- FUNCTION: Adhesin that binds to the host cell extracellular matrix
CC       proteins fibronectin, fibrinogen, collagen, and vitronectin.
CC   -!- SUBCELLULAR LOCATION: Cell surface {ECO:0000269|PubMed:11698365}.
CC   -!- INDUCTION: Expressed in the stationary growth phase. Regulated by Sae,
CC       which is essential for emp transcription. Repressed in the presence of
CC       glucose as a result of a pH-mediated decrease in expression of sae.
CC       Also under control of both Agr and SarA. {ECO:0000269|PubMed:15941988}.
CC   -!- MISCELLANEOUS: Strain Newman has emp expression enhanced compared with
CC       NCTC 8325 derivatives.
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DR   EMBL; AJ271347; CAB67709.1; -; Genomic_DNA.
DR   EMBL; AP009351; BAF67030.1; -; Genomic_DNA.
DR   RefSeq; WP_000728056.1; NZ_CP023390.1.
DR   AlphaFoldDB; A6QF98; -.
DR   EnsemblBacteria; BAF67030; BAF67030; NWMN_0758.
DR   KEGG; sae:NWMN_0758; -.
DR   HOGENOM; CLU_078520_0_0_9; -.
DR   OMA; MINHYFA; -.
DR   Proteomes; UP000006386; Chromosome.
DR   GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..340
FT                   /note="Extracellular matrix protein-binding protein emp"
FT                   /id="PRO_0000324104"
SQ   SEQUENCE   340 AA;  38485 MW;  BDC25A6F79C5E42A CRC64;
     MKKKLLVLTM STLFATQIMN SNHAKASVTE SVDKKFVVPE SGINKIIPAY DEFKNSPKVN
     VSNLTDNKNF VASEDKLNKI ADSSAASKIV DKNFVVPESK LGNIVPEYKE INNRVNVATN
     NPASQQVDKH FVAKGPEVNR FITQNKVNHH FITTQTHYKK VITSYKSTHV HKHVNHAKDS
     INKHFIVKPS ESPRYTHPSQ SLIIKHHFAV PGYHAHKFVT PGHASIKINH FCVVPQINSF
     KVIPPYGHNS HRMHVPSFQN NTTATHQNAK VNKAYDYKYF YSYKVVKGVK KYFSFSQSNG
     YKIGKPSLNI KNVNYQYAVP SYSPTHYVPE FKGSLPAPRV