CLFA_STAAR
ID CLFA_STAAR Reviewed; 1029 AA.
AC Q6GIK4;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 100.
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=SAR0842;
OS Staphylococcus aureus (strain MRSA252).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282458;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRSA252;
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; BX571856; CAG39851.1; -; Genomic_DNA.
DR RefSeq; WP_001056313.1; NC_002952.2.
DR AlphaFoldDB; Q6GIK4; -.
DR SMR; Q6GIK4; -.
DR KEGG; sar:SAR0842; -.
DR HOGENOM; CLU_010159_0_0_9; -.
DR OMA; ATEWTTK; -.
DR OrthoDB; 495681at2; -.
DR PRO; PR:Q6GIK4; -.
DR Proteomes; UP000000596; 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..995
FT /note="Clumping factor A"
FT /id="PRO_0000041998"
FT PROPEP 996..1029
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT /id="PRO_0000041999"
FT REGION 37..200
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 529..1000
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 992..996
FT /note="LPXTG sorting signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT COMPBIAS 552..566
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 567..648
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 649..955
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 956..982
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 995
FT /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
SQ SEQUENCE 1029 AA; 106716 MW; 025E13C6A4C4F020 CRC64;
MNMKKQEKHA IRKKSIGVAS VLVGTLIGFG LLSSKEADAS ENSMTQTENT SNESKSNDPS
SVNAAPKTDN TNVSDSNTTT NTNSDETNVA QNPAQQETTQ SASTNATTEE TPVTGEVTTT
ATNQANTPAT TQSSNTNAEE SVNQTSNETT SNDTNTVSSV NSPQNSTNAE NVSTTQDIST
EATPSNNESA PQSTDASNKD VVNQAVNTSA PRMRAFSLAA VAADAPAAGK DITNQLTNVT
VGIDSGDTVY PHQAGYVKLN YGFSVPNEAV QGDTFKITVP KELNLNGVTS TAKVPPIMAG
DQVLANGVID SDGNVIYTFT DYVNTKDDVK ATLTMPAYID PENVTKTGNV TLATGIGSTT
ANKTVLVDYE KYGKFYNLSI KGTIDQIDKT NNTYRQTIYV NPSGDNVIAP VLTGNLKPNT
DSNALIDAQN TSIKVYKVDN ASDLSESYYV NPDNFEDVTD SVNITFPNPN QYKVEFNTPD
DQITTPYIVV VNGHIDPNSK GDLALRSTLY GYNSNIIWRS MSWDNEVAFN NGSGSGDGID
KPVVPEQPDE PGEIEPIPED SDSDPGSDSG SDSGSDSNSD SGSDSGSDST SDSGSDSASD
SDSASDSDSA SDSDSASDSD SASDSDSASD SDSASDSDST SDSDSTSDSD SASDSDSDSD
SDSDSDSDSD SDSDSDSDSD SDSDSDSDSD SDSDSDSDSD SDSDSESDSD SDSDSDSDSD
SDSDSDSDSV SDSDSDSDSD SESDSDSDSD SDSDSDSDSE SDSDSDSDSD SDSDSDSDSD
SDSDSDSDSD SDSDSDSDSD SDSDSDSDSD SDSDSESDSD SDSDSDSDSD SDSDSDSDSD
SDSDLDSDSD SDSDSDSDSD SDSDSDSDSD SDSDLDSDSD SDSDSDSDSD SASDSDSDSD
SDSDSESDSD SDSDSDSDSD SASDSDSDSD SASDSDSDST SDTGSDNDSD SESDSNSDSD
SGSNNNVVPP NSPKSGTNAS NKNEAKESKE PLPDTGSEDE ANTSLIWGLL ASLGSLLLFR
RKKENKDKK
