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Protein

Clumping factor A

Gene

clfA

Organism
Staphylococcus aureus (strain NCTC 8325)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Cell surface-associated protein implicated in virulence. Promotes bacterial attachment exclusively to the gamma-chain of human fibrinogen. Induces formation of bacterial clumps, which diminish the ability of group IIA phospholipase A2 to cause bacterial phospholipid hydrolysis and killing. Significantly decreases macrophage phagocytosis possibly thanks to the clumps, clumped bacteria being too large to be phagocytosed. Dominant factor responsible for human platelet aggregation, which may be an important mechanism for initiating infective endocarditis. Enhances spleen cell proliferative response in vitro, contributing significantly to the immunostimulatory activity of S.aureus.1 Publication

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Virulence

Enzyme and pathway databases

BioCyciSAUR93061:GIWJ-779-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Clumping factor A
Alternative name(s):
Fibrinogen receptor A
Fibrinogen-binding protein A
Gene namesi
Name:clfA
Ordered Locus Names:SAOUHSC_00812
OrganismiStaphylococcus aureus (strain NCTC 8325)
Taxonomic identifieri93061 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus
Proteomesi
  • UP000008816 Componenti: Chromosome

Subcellular locationi

  • Secretedcell wall PROSITE-ProRule annotation; Peptidoglycan-anchor PROSITE-ProRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell wall, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi525 – 5251N → A: 2-fold reduction in clumping titer compared to wild-type. 1 Publication
Mutagenesisi526 – 5272EV → AS: More than 1000-fold reduction in clumping titer compared to wild-type. No binding to soluble Fg. Dramatic reduction of ability to adhere to immobilized Fg.
Mutagenesisi526 – 5261E → A: 32-fold reduction in clumping titer compared to wild-type. Reduced ability to bind to soluble Fg and to adhere to immobilized Fg. 1 Publication
Mutagenesisi527 – 5271V → S: 16- to 32-fold reduction in clumping titer compared to wild-type. activity. Reduced ability to bind to soluble Fg and to adhere to immobilized Fg. 1 Publication
Mutagenesisi528 – 5281A → V: 2-fold reduction in clumping titer compared to wild-type; when associated with A-532. 1 Publication
Mutagenesisi532 – 5321G → A: 2-fold reduction in clumping titer compared to wild-type; when associated with V-528. 1 Publication
Mutagenesisi537 – 5371D → A: 2-fold reduction in clumping titer compared to wild-type. 1 Publication
Mutagenesisi546 – 5461E → A: 2-fold reduction in clumping titer compared to wild-type. 1 Publication
Mutagenesisi559 – 5591E → A: 2-fold reduction in clumping titer compared to wild-type. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3939Sequence analysisAdd
BLAST
Chaini40 – 893854Clumping factor APRO_0000249324Add
BLAST
Propeptidei894 – 92734Removed by sortasePROSITE-ProRule annotationPRO_0000249325Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei893 – 8931Pentaglycyl murein peptidoglycan amidated threoninePROSITE-ProRule annotation

Keywords - PTMi

Peptidoglycan-anchor

Interactioni

Protein-protein interaction databases

STRINGi93061.SAOUHSC_00812.

Structurei

Secondary structure

1
927
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi233 – 2353Combined sources
Beta strandi237 – 2448Combined sources
Beta strandi247 – 2493Combined sources
Beta strandi257 – 2659Combined sources
Beta strandi274 – 2785Combined sources
Beta strandi283 – 2853Combined sources
Beta strandi305 – 3095Combined sources
Beta strandi315 – 3195Combined sources
Helixi322 – 3254Combined sources
Beta strandi326 – 33914Combined sources
Turni341 – 3433Combined sources
Beta strandi346 – 35611Combined sources
Beta strandi359 – 3679Combined sources
Beta strandi373 – 3753Combined sources
Beta strandi378 – 38811Combined sources
Turni389 – 3924Combined sources
Beta strandi393 – 4019Combined sources
Beta strandi407 – 41610Combined sources
Turni428 – 4303Combined sources
Beta strandi432 – 4376Combined sources
Helixi441 – 4433Combined sources
Helixi459 – 4613Combined sources
Beta strandi462 – 4687Combined sources
Beta strandi471 – 4755Combined sources
Beta strandi481 – 4833Combined sources
Beta strandi487 – 4959Combined sources
Beta strandi505 – 5128Combined sources
Beta strandi518 – 53013Combined sources
Beta strandi533 – 5408Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2VR3X-ray1.95A/B229-545[»]
ProteinModelPortaliQ2G015.
SMRiQ2G015. Positions 229-559.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ2G015.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni40 – 542503Ligand binding A regionAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi890 – 8945LPXTG sorting signalPROSITE-ProRule annotation

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi68 – 183116Thr-richAdd
BLAST
Compositional biasi546 – 56520Pro-richAdd
BLAST
Compositional biasi560 – 856297Asp/Ser-richAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4106HV3. Bacteria.
ENOG410Y59N. LUCA.
KOiK14201.
OMAiQTENTSN.

Family and domain databases

Gene3Di2.60.40.1280. 1 hit.
2.60.40.1290. 1 hit.
InterProiIPR011266. Adhesin_Fg-bd_dom_2.
IPR008966. Adhesion_dom.
IPR011252. Fibrogen-bd_dom1.
IPR019948. Gram-positive_anchor.
IPR005877. YSIRK_signal_dom.
[Graphical view]
PfamiPF00746. Gram_pos_anchor. 1 hit.
PF10425. SdrG_C_C. 1 hit.
PF04650. YSIRK_signal. 1 hit.
[Graphical view]
SUPFAMiSSF49401. SSF49401. 2 hits.
TIGRFAMsiTIGR01168. YSIRK_signal. 1 hit.
PROSITEiPS50847. GRAM_POS_ANCHORING. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q2G015-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNMKKKEKHA IRKKSIGVAS VLVGTLIGFG LLSSKEADAS ENSVTQSDSA
60 70 80 90 100
SNESKSNDSS SVSAAPKTDD TNVSDTKTSS NTNNGETSVA QNPAQQETTQ
110 120 130 140 150
SSSTNATTEE TPVTGEATTT TTNQANTPAT TQSSNTNAEE LVNQTSNETT
160 170 180 190 200
SNDTNTVSSV NSPQNSTNAE NVSTTQDTST EATPSNNESA PQSTDASNKD
210 220 230 240 250
VVNQAVNTSA PRMRAFSLAA VAADAPVAGT DITNQLTNVT VGIDSGTTVY
260 270 280 290 300
PHQAGYVKLN YGFSVPNSAV KGDTFKITVP KELNLNGVTS TAKVPPIMAG
310 320 330 340 350
DQVLANGVID SDGNVIYTFT DYVNTKDDVK ATLTMPAYID PENVKKTGNV
360 370 380 390 400
TLATGIGSTT ANKTVLVDYE KYGKFYNLSI KGTIDQIDKT NNTYRQTIYV
410 420 430 440 450
NPSGDNVIAP VLTGNLKPNT DSNALIDQQN TSIKVYKVDN AADLSESYFV
460 470 480 490 500
NPENFEDVTN SVNITFPNPN QYKVEFNTPD DQITTPYIVV VNGHIDPNSK
510 520 530 540 550
GDLALRSTLY GYNSNIIWRS MSWDNEVAFN NGSGSGDGID KPVVPEQPDE
560 570 580 590 600
PGEIEPIPED SDSDPGSDSG SDSNSDSGSD SGSDSTSDSG SDSASDSDSA
610 620 630 640 650
SDSDSASDSD SASDSDSASD SDSDNDSDSD SDSDSDSDSD SDSDSDSDSD
660 670 680 690 700
SDSDSDSDSD SDSDSDSDSD SDSDSDSDSD SDSDSDSDSD SDSDSDSDSD
710 720 730 740 750
SDSDSDSDSD SDSDSDSDSD SDSDSDSDSD SDSDSDSDSD SDSDSDSDSD
760 770 780 790 800
SDSDSDSDSD SDSDSDSASD SDSDSDSDSD SDSDSDSDSD SDSDSDSDSD
810 820 830 840 850
SDSDSDSESD SDSDSDSDSD SDSDSDSDSD SASDSDSGSD SDSSSDSDSE
860 870 880 890 900
SDSNSDSESV SNNNVVPPNS PKNGTNASNK NEAKDSKEPL PDTGSEDEAN
910 920
TSLIWGLLAS IGSLLLFRRK KENKDKK
Length:927
Mass (Da):96,448
Last modified:March 21, 2006 - v1
Checksum:iB429AEB92AEFCABB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000253 Genomic DNA. Translation: ABD29940.1.
RefSeqiYP_499368.1. NC_007795.1.

Genome annotation databases

EnsemblBacteriaiABD29940; ABD29940; SAOUHSC_00812.
GeneIDi3919375.
KEGGisao:SAOUHSC_00812.
PATRICi19579150. VBIStaAur99865_0734.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000253 Genomic DNA. Translation: ABD29940.1.
RefSeqiYP_499368.1. NC_007795.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2VR3X-ray1.95A/B229-545[»]
ProteinModelPortaliQ2G015.
SMRiQ2G015. Positions 229-559.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi93061.SAOUHSC_00812.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABD29940; ABD29940; SAOUHSC_00812.
GeneIDi3919375.
KEGGisao:SAOUHSC_00812.
PATRICi19579150. VBIStaAur99865_0734.

Phylogenomic databases

eggNOGiENOG4106HV3. Bacteria.
ENOG410Y59N. LUCA.
KOiK14201.
OMAiQTENTSN.

Enzyme and pathway databases

BioCyciSAUR93061:GIWJ-779-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ2G015.

Family and domain databases

Gene3Di2.60.40.1280. 1 hit.
2.60.40.1290. 1 hit.
InterProiIPR011266. Adhesin_Fg-bd_dom_2.
IPR008966. Adhesion_dom.
IPR011252. Fibrogen-bd_dom1.
IPR019948. Gram-positive_anchor.
IPR005877. YSIRK_signal_dom.
[Graphical view]
PfamiPF00746. Gram_pos_anchor. 1 hit.
PF10425. SdrG_C_C. 1 hit.
PF04650. YSIRK_signal. 1 hit.
[Graphical view]
SUPFAMiSSF49401. SSF49401. 2 hits.
TIGRFAMsiTIGR01168. YSIRK_signal. 1 hit.
PROSITEiPS50847. GRAM_POS_ANCHORING. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCLFA_STAA8
AccessioniPrimary (citable) accession number: Q2G015
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: March 21, 2006
Last modified: September 7, 2016
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.