CLFA_STAAS
ID CLFA_STAAS Reviewed; 928 AA.
AC Q6GB45;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 96.
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=SAS0752;
OS Staphylococcus aureus (strain MSSA476).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282459;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSSA476;
RX PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT for the rapid evolution of virulence and drug resistance.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
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; BX571857; CAG42526.1; -; Genomic_DNA.
DR RefSeq; WP_001056174.1; NC_002953.3.
DR AlphaFoldDB; Q6GB45; -.
DR SMR; Q6GB45; -.
DR KEGG; sas:SAS0752; -.
DR HOGENOM; CLU_010159_0_0_9; -.
DR OMA; ATEWTTK; -.
DR PRO; PR:Q6GB45; -.
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..894
FT /note="Clumping factor A"
FT /id="PRO_0000042000"
FT PROPEP 895..928
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT /id="PRO_0000042001"
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..899
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 891..895
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..854
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 855..881
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 894
FT /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
SQ SEQUENCE 928 AA; 96419 MW; FBE8570209E9E195 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 NSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSASDS DSDSDSDSDS
DSDSDSDSDS DSDSDSDSDS DSDSDSESDS DSESDSDSDS DSDSDSDSDS DSASDSDSGS
DSDSSSDSDS ESDSNSDSES GSNNNVVPPN SPKNGTNASN KNEAKDSKEP LPDTGSEDEA
NTSLIWGLLA SIGSLLLFRR KKENKDKK
