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Protein

Clumping factor A

Gene

clfA

Organism
Staphylococcus aureus (strain Newman)
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.4 Publications

GO - Biological processi

  • cell adhesion Source: InterPro
  • pathogenesis Source: CACAO
Complete GO annotation...

Keywords - Biological processi

Virulence

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:NWMN_0756
OrganismiStaphylococcus aureus (strain Newman)
Taxonomic identifieri426430 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus
Proteomesi
  • UP000006386 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)DescriptionActionsGraphical viewLength
Mutagenesisi254A → S: Decrease in Fg-binding activity. 1 Publication1
Mutagenesisi256Y → A: Decrease in Fg-binding activity. 1 Publication1
Mutagenesisi310D → A: Decrease in gamma-chain peptide-binding activity and in the degree of inhibition induced by Ca(2+). 3-fold decrease in gamma-chain peptide binding activity and decrease in the degree of inhibition induced by Ca(2+); when associated with A-312. Dramatic decrease in gamma-chain peptide-binding activity and decrease in the degree of inhibition induced by Ca(2+); when associated with A-312; A-318 and A-321. 1 Publication1
Mutagenesisi312D → A: 3-fold decrease in gamma-chain peptide binding activity and decrease in the degree of inhibition induced by Ca(2+); when associated with A-310. Dramatic decrease in gamma-chain peptide-binding activity and decrease in the degree of inhibition induced by Ca(2+); when associated with A-310; A-318 and A-321. 1 Publication1
Mutagenesisi318T → A: Dramatic decrease in gamma-chain peptide-binding activity and decrease in the degree of inhibition induced by Ca(2+); when associated with A-310; A-312 and A-321. 1 Publication1
Mutagenesisi321D → A: Dramatic decrease in gamma-chain peptide-binding activity and decrease in the degree of inhibition induced by Ca(2+); when associated with A-310; A-312 and A-318. 1 Publication1
Mutagenesisi336P → S: Decrease in Fg-binding activity. 1 Publication1
Mutagenesisi338Y → A: No Fg-binding. 1 Publication1
Mutagenesisi387I → S: Decrease of Fg-binding activity. 1 Publication1
Mutagenesisi389K → A: Decrease of Fg-binding activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 39Sequence analysisAdd BLAST39
ChainiPRO_000004199040 – 899Clumping factor AAdd BLAST860
PropeptideiPRO_0000041991900 – 933Removed by sortasePROSITE-ProRule annotationAdd BLAST34

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei899Pentaglycyl murein peptidoglycan amidated threoninePROSITE-ProRule annotation1

Keywords - PTMi

Peptidoglycan-anchor

Expressioni

Inductioni

Expressed on cells from both exponential and stationary phases. Up-regulated by sigma-B factor during later growth stages. Sigma-B seems to have a transient enhancing effect on bacterial density in the early stages of infection that it lost during later stages of infection.2 Publications

Structurei

Secondary structure

1933
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi233 – 235Combined sources3
Beta strandi237 – 244Combined sources8
Beta strandi247 – 249Combined sources3
Beta strandi257 – 264Combined sources8
Beta strandi274 – 278Combined sources5
Beta strandi283 – 289Combined sources7
Beta strandi297 – 299Combined sources3
Beta strandi302 – 309Combined sources8
Beta strandi315 – 319Combined sources5
Helixi322 – 325Combined sources4
Beta strandi330 – 339Combined sources10
Turni341 – 343Combined sources3
Beta strandi346 – 356Combined sources11
Beta strandi359 – 367Combined sources9
Beta strandi373 – 375Combined sources3
Beta strandi378 – 382Combined sources5
Beta strandi386 – 388Combined sources3
Turni389 – 392Combined sources4
Beta strandi393 – 400Combined sources8
Beta strandi407 – 416Combined sources10
Turni428 – 430Combined sources3
Beta strandi432 – 439Combined sources8
Helixi441 – 443Combined sources3
Helixi452 – 454Combined sources3
Beta strandi455 – 457Combined sources3
Helixi459 – 461Combined sources3
Beta strandi462 – 468Combined sources7
Beta strandi471 – 475Combined sources5
Beta strandi481 – 483Combined sources3
Beta strandi487 – 495Combined sources9
Beta strandi503 – 512Combined sources10
Beta strandi519 – 527Combined sources9
Beta strandi537 – 543Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1N67X-ray1.90A221-559[»]
ProteinModelPortaliQ53653.
SMRiQ53653.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ53653.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni40 – 542Ligand binding A regionAdd BLAST503

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi896 – 900LPXTG sorting signalPROSITE-ProRule annotation5

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi68 – 183Thr-richAdd BLAST116
Compositional biasi546 – 565Pro-richAdd BLAST20
Compositional biasi560 – 865Asp/Ser-richAdd BLAST306

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000022927.
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.

Q53653-1 [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
FNDTNTVSSV NSPQNSTNAE NVSTTQDTST EATPSNNESA PQSTDASNKD
210 220 230 240 250
VVNQAVNTSA PRMRAFSLAA VAADAPAAGT 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 SDSESDSDSD SDSDSDSDSD SDSDSDSASD SDSGSDSDSS
860 870 880 890 900
SDSDSESDSN SDSESGSNNN VVPPNSPKNG TNASNKNEAK DSKEPLPDTG
910 920 930
SEDEANTSLI WGLLASIGSL LLFRRKKENK DKK
Length:933
Mass (Da):97,058
Last modified:November 1, 1996 - v1
Checksum:iEB51A6DE2FF759F4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z18852 Genomic DNA. Translation: CAA79304.1.
AP009351 Genomic DNA. Translation: BAF67028.1.
PIRiS41539.
RefSeqiWP_001056178.1. NC_009641.1.

Genome annotation databases

EnsemblBacteriaiBAF67028; BAF67028; NWMN_0756.
KEGGisae:NWMN_0756.
PATRICi19584983. VBIStaAur133992_0818.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z18852 Genomic DNA. Translation: CAA79304.1.
AP009351 Genomic DNA. Translation: BAF67028.1.
PIRiS41539.
RefSeqiWP_001056178.1. NC_009641.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1N67X-ray1.90A221-559[»]
ProteinModelPortaliQ53653.
SMRiQ53653.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAF67028; BAF67028; NWMN_0756.
KEGGisae:NWMN_0756.
PATRICi19584983. VBIStaAur133992_0818.

Phylogenomic databases

HOGENOMiHOG000022927.
KOiK14201.
OMAiQTENTSN.

Miscellaneous databases

EvolutionaryTraceiQ53653.

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_STAAE
AccessioniPrimary (citable) accession number: Q53653
Secondary accession number(s): A6QF96
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 27, 2005
Last sequence update: November 1, 1996
Last modified: November 2, 2016
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Fg-binding activity is regulated by the divalent cations Ca2+ and Mn2+.

Keywords - Technical termi

3D-structure, Complete 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.