CLFA_STAAC
ID CLFA_STAAC Reviewed; 933 AA.
AC Q5HHM8;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 99.
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=SACOL0856;
OS Staphylococcus aureus (strain COL).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93062;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COL;
RX PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA Fraser C.M.;
RT "Insights on evolution of virulence and resistance from the complete genome
RT analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT strain.";
RL J. Bacteriol. 187:2426-2438(2005).
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; CP000046; AAW36411.1; -; Genomic_DNA.
DR RefSeq; WP_001056223.1; NC_002951.2.
DR AlphaFoldDB; Q5HHM8; -.
DR SMR; Q5HHM8; -.
DR EnsemblBacteria; AAW36411; AAW36411; SACOL0856.
DR KEGG; sac:SACOL0856; -.
DR HOGENOM; CLU_010159_0_0_9; -.
DR OMA; ATEWTTK; -.
DR PRO; PR:Q5HHM8; -.
DR Proteomes; UP000000530; 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..899
FT /note="Clumping factor A"
FT /id="PRO_0000041992"
FT PROPEP 900..933
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT /id="PRO_0000041993"
FT REGION 34..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..904
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 896..900
FT /note="LPXTG sorting signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT COMPBIAS 36..200
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..614
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 615..859
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 860..886
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 899
FT /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
SQ SEQUENCE 933 AA; 96998 MW; 75326D0C44834D00 CRC64;
MNMKKKEKHA IRKKSIGVAS VLVGTLIGFG LLSSKEADAS ENSVTQSDSA SNESKSNDSS
SVSAAPKTDD TNVSDTKTSS NTNNGETSVA QNPAQQETTQ SSSTNATTEE TPVTGEATTT
TTNQANTPAT TQSSNTNAEE LVNQTSNETT SNDTNTVSSV NSPQNSTNAE NVSTTQDTST
EATPSNNESA PQSTDASNKD VVNQAVNTSA PRMRAFSLAA VAADAPAAGT DITNQLTNVT
VGIDSGTTVY PHQAGYVKLN YGFSVPNSAV KGDTFKITVP KELNLNGVTS TAKVPPIMAG
DQVLANGVID SDGNVIYTFT DYVNTKDDVK ATLTMPAYID PENVKKTGNV TLATGIGSTT
ANKTVLVDYE KYGKFYNLSI KGTIDQIDKT NNTYRQTIYV NPSGDNVIAP VLTGNLKPNT
DSNALIDQQN TSIKVYKVDN AADLSESYFV NPENFEDVTN SVNITFPNPN QYKVEFNTPD
DQITTPYIVV VNGHIDPNSK GDLALRSTLY GYNSNIIWRS MSWDNEVAFN NGSGSGDGID
KPVVPEQPDE PGEIEPIPED SDSDPGSDSG SDSNSDSGSD SGSDSTSDSG SDSASDSDSA
SDSDSASDSD SASDSDSASD SDSDNDSDSD SDSDSDSDSD SDSDSDSDSD SDSDSDSDSD
SDSDSDSDSD SDSDSDSDSD SDSDSDSDSD SDSDSDSDSD SDSDSDSDSD SDSDSDSDSD
SDSDSDSDSD SDSDSDSDSD SDSDSDSDSD SDSDSDSDSD SDSDSDSASD SDSDSDSDSD
SDSDSDSDSD SDSDSDSDSD SDSDSDSESD SDSESDSDSD SDSDSDSDSD SDSDSDSASD
SDSGSDSDSS SDSDSESDSN SDSESGSNNN VVPPNSPKNG TNASNKNEAK DSKEPLPDTG
SEDEANTSLI WGLLASIGSL LLFRRKKENK DKK
