ID   CLFA_STAAN              Reviewed;         989 AA.
AC   Q99VJ4;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 118.
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=SA0742;
OS   Staphylococcus aureus (strain N315).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=158879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N315;
RX   PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA   Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA   Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA   Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA   Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA   Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA   Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA   Hiramatsu K.;
RT   "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL   Lancet 357:1225-1240(2001).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=N315;
RA   Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F.;
RT   "Shotgun proteomic analysis of total and membrane protein extracts of S.
RT   aureus strain N315.";
RL   Submitted (OCT-2007) to UniProtKB.
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, which diminish the
CC       ability of group IIA phospholipase A2 to cause bacterial phospholipid
CC       hydrolysis and killing. Significantly decreases macrophage phagocytosis
CC       possibly thanks to the clumps, clumped bacteria being too large to be
CC       phagocytosed. Dominant factor responsible for human platelet
CC       aggregation, which may be an important mechanism for initiating
CC       infective endocarditis (By similarity). {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; BA000018; BAB41975.1; -; Genomic_DNA.
DR   PIR; D89852; D89852.
DR   RefSeq; WP_001056195.1; NC_002745.2.
DR   AlphaFoldDB; Q99VJ4; -.
DR   SMR; Q99VJ4; -.
DR   ABCD; Q99VJ4; 14 sequenced antibodies.
DR   EnsemblBacteria; BAB41975; BAB41975; BAB41975.
DR   KEGG; sau:SA0742; -.
DR   HOGENOM; CLU_010159_0_0_9; -.
DR   OMA; ATEWTTK; -.
DR   PRO; PR:Q99VJ4; -.
DR   Proteomes; UP000000751; 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   1: Evidence at protein level;
KW   Cell wall; Peptidoglycan-anchor; Secreted; Signal; Virulence.
FT   SIGNAL          1..39
FT                   /evidence="ECO:0000255"
FT   CHAIN           40..955
FT                   /note="Clumping factor A"
FT                   /id="PRO_0000041996"
FT   PROPEP          956..989
FT                   /note="Removed by sortase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT                   /id="PRO_0000041997"
FT   REGION          34..205
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..960
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           952..956
FT                   /note="LPXTG sorting signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT   COMPBIAS        36..205
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        552..566
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        567..662
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        663..885
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        886..902
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        916..942
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         955
FT                   /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
SQ   SEQUENCE   989 AA;  102409 MW;  DA6E807539623467 CRC64;
     MNMKKKEKHA IRKKSIGVAS VLVGTLIGFG LLSSKEADAS ENSVTQSDSA SNESKSNDSS
     SVSAAPKTDD TNVSDTKTSS NTNNGETSVA QNPAQQETTQ SSSTNATTEE TPVTGEATTT
     TTNQANTPAT TQSSNTNAEE LVNQTSNETT SNDTNTVSSV NSPQNSTNAE NVSTTQDTST
     EATPSNNESA PQNTDASNKD VVSQAVNPST PRMRAFSLAA VAADAPAAGT DITNQLTDVK
     VTIDSGTTVY PHQAGYVKLN YGFSVPNSAV KGDTFKITVP KELNLNGVTS TAKVPPIMAG
     DQVLANGVID SDGNVIYTFT DYVDNKENVT ANITMPAYID PENVTKTGNV TLTTGIGTNT
     ASKTVLIDYE KYGQFHNLSI KGTIDQIDKT NNTYRQTIYV NPSGDNVVLP ALTGNLIPNT
     KSNALIDAKN TDIKVYRVDN ANDLSESYYV NPSDFEDVTN QVRISFPNAN QYKVEFPTDD
     DQITTPYIVV VNGHIDPAST GDLALRSTFY GYDSNFIWRS MSWDNEVAFN NGSGSGDGID
     KPVVPEQPDE PGEIEPIPED SDSDPGSDSG SDSNSDSGSD SGSDSTSDSG SDSASDSDSA
     SDSDSASDSD SASDSDSASD SDSASDSDSA SDSDSASDSD SASDSDSASD SDSASDSDSA
     SDSDSASDSD SDSDSDSDSD SDSDSDSDSD SDSDSDSDSD SDSDSDSDSD SDSDSDSDSD
     SDSDSDSDSD SDSDSDSDSD SDSDSDSDSD SDSDSDSDSD SDSDSDSDSD SDSDSDSDSD
     SDSDSDSDSD SDSDSDSDSD SDSDSDSDSD SDSDSDSDSD SASDSDSDSD SESDSDSDSD
     SDSDSDSDSD SDSDSESDSD SDSDSDSESD SDSDSDSDSD SASDSDSGSD SDSSSDSDSD
     STSDTGSDND SDSDSNSDSE SGSNNNVVPP NSPKNGTNAS NKNEAKDSKE PLPDTGSEDE
     ANTSLIWGLL ASLGSLLLFR RKKENKDKK