ID   CLFA_STAAW              Reviewed;         946 AA.
AC   Q8NXJ1;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 108.
DE   RecName: Full=Clumping factor A;
DE   AltName: Full=Fibrinogen receptor A;
DE   AltName: Full=Fibrinogen-binding protein A;
DE   Flags: Precursor;
GN   Name=clfA; OrderedLocusNames=MW0764;
OS   Staphylococcus aureus (strain MW2).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=196620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MW2;
RX   PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA   Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA   Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT   "Genome and virulence determinants of high virulence community-acquired
RT   MRSA.";
RL   Lancet 359:1819-1827(2002).
CC   -!- FUNCTION: Cell surface-associated protein implicated in virulence.
CC       Promotes bacterial attachment exclusively to the gamma-chain of human
CC       fibrinogen. Induces formation of bacterial clumps (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|PROSITE-
CC       ProRule:PRU00477}; Peptidoglycan-anchor {ECO:0000255|PROSITE-
CC       ProRule:PRU00477}. Note=Anchored to the cell wall by sortase A (By
CC       similarity). {ECO:0000250|UniProtKB:Q2G015}.
CC   -!- SIMILARITY: Belongs to the serine-aspartate repeat-containing protein
CC       (SDr) family. {ECO:0000305}.
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DR   EMBL; BA000033; BAB94629.1; -; Genomic_DNA.
DR   RefSeq; WP_001056172.1; NC_003923.1.
DR   AlphaFoldDB; Q8NXJ1; -.
DR   SMR; Q8NXJ1; -.
DR   EnsemblBacteria; BAB94629; BAB94629; BAB94629.
DR   KEGG; sam:MW0764; -.
DR   HOGENOM; CLU_010159_0_0_9; -.
DR   OMA; ATEWTTK; -.
DR   PRO; PR:Q8NXJ1; -.
DR   Proteomes; UP000000418; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR   Gene3D; 2.60.40.1280; -; 1.
DR   InterPro; IPR011266; Adhesin_Fg-bd_dom_2.
DR   InterPro; IPR008966; Adhesion_dom_sf.
DR   InterPro; IPR011252; Fibrogen-bd_dom1.
DR   InterPro; IPR019931; LPXTG_anchor.
DR   InterPro; IPR041171; SDR_Ig.
DR   InterPro; IPR005877; YSIRK_signal_dom.
DR   Pfam; PF17961; Big_8; 1.
DR   Pfam; PF00746; Gram_pos_anchor; 1.
DR   Pfam; PF10425; SdrG_C_C; 1.
DR   Pfam; PF04650; YSIRK_signal; 1.
DR   SUPFAM; SSF49401; SSF49401; 2.
DR   TIGRFAMs; TIGR01168; YSIRK_signal; 1.
DR   PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
PE   3: Inferred from homology;
KW   Cell wall; Peptidoglycan-anchor; Secreted; Signal; Virulence.
FT   SIGNAL          1..39
FT                   /evidence="ECO:0000255"
FT   CHAIN           40..912
FT                   /note="Clumping factor A"
FT                   /id="PRO_0000042002"
FT   PROPEP          913..946
FT                   /note="Removed by sortase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT                   /id="PRO_0000042003"
FT   REGION          34..199
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          40..542
FT                   /note="Ligand binding A region"
FT                   /evidence="ECO:0000250"
FT   REGION          528..917
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           9..20
FT                   /note="YSIRK-G/S signaling motif"
FT                   /evidence="ECO:0000250|UniProtKB:Q2G015"
FT   MOTIF           909..913
FT                   /note="LPXTG sorting signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT   COMPBIAS        36..199
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        551..565
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        566..637
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        638..872
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        873..899
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         912
FT                   /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
SQ   SEQUENCE   946 AA;  98238 MW;  EFFB838793201173 CRC64;
     MNMKKKEKHA IRKKSIGVAS VLVGTLIGFG LLSSKEADAS ENSVTQSDSA SNESKSNDSS
     SVSAAPKTDD TNVSDTKTSS NTNNGETSVA QNPAQQETTQ SALTNATTEE TPVTGEATTA
     TNQANTPATT QSSNTNAEEL VNQTSNETTS NDTNTVSSVN SPQNSTNAEN VSTTQDTSTE
     ATPSNNESAP QSTDASNKDV VNQAVNTSAP RMRAFSLSAV AADAPAAGKD ITNQLTNVTV
     GIDSGDTVYP HQAGYVKLNY GFSVPNSAVK GDTFKITVPK ELNLNGVTST AKVPPIMAGD
     QVLANGVIDS DGNVIYTFTD YVDTKENVTA NITMPAYIDP ENVTKTGNVT LTTGIGSTTA
     NKTVLVDYEK YGKFYNLSIK GTIDQIDKTN NTYRQTIYVN PSGDNVIAPV LTGNLKPNTD
     SNALIDQQNT SIKVYKVDNA ADLSESYFVN PENFEDVTNS VNITFPNPNQ YKVEFNTPDD
     QITTPYIVVV NGHIDPNSKG DLALRSTLYG YDSRFVWRSM SWDNEVAFNN GSGSGDGIDK
     PVVPEQPDEP GEIEPIPEDS DSDPGSDSGS DSNSDSGSDS GSDSTSDSGS DSASDSDSAS
     DSDSASDSDS ASDSDSASDS DSASDSDSAS DSDSASDSDS ASDSDSDNDS DSDSDSDSDS
     DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS
     DSDSDSDSDS DSDSDSDSDS DSDSDSDSNS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS
     DSDSASDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSESDSDS ESDSDSDSDS
     DSDSDSDSDS ASDSDSGSDS DSSSDSDSES DSNSDSESGS NNNVVPPNSP KNGTNASNKN
     EAKDSKEPLP DTGSEDEANT SLIWGLLASI GSLLLFRRKK ENKDKK