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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

Enzyme and pathway databases

BioCyciSAUR426430:GIXC-776-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: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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi254 – 2541A → S: Decrease in Fg-binding activity. 1 Publication
Mutagenesisi256 – 2561Y → A: Decrease in Fg-binding activity. 1 Publication
Mutagenesisi310 – 3101D → 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 Publication
Mutagenesisi312 – 3121D → 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 Publication
Mutagenesisi318 – 3181T → 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 Publication
Mutagenesisi321 – 3211D → 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 Publication
Mutagenesisi336 – 3361P → S: Decrease in Fg-binding activity. 1 Publication
Mutagenesisi338 – 3381Y → A: No Fg-binding. 1 Publication
Mutagenesisi387 – 3871I → S: Decrease of Fg-binding activity. 1 Publication
Mutagenesisi389 – 3891K → A: Decrease of Fg-binding activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3939Sequence analysisAdd
BLAST
Chaini40 – 899860Clumping factor APRO_0000041990Add
BLAST
Propeptidei900 – 93334Removed by sortasePROSITE-ProRule annotationPRO_0000041991Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei899 – 8991Pentaglycyl murein peptidoglycan amidated threoninePROSITE-ProRule annotation

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

1
933
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 – 2648Combined sources
Beta strandi274 – 2785Combined sources
Beta strandi283 – 2897Combined sources
Beta strandi297 – 2993Combined sources
Beta strandi302 – 3098Combined sources
Beta strandi315 – 3195Combined sources
Helixi322 – 3254Combined sources
Beta strandi330 – 33910Combined sources
Turni341 – 3433Combined sources
Beta strandi346 – 35611Combined sources
Beta strandi359 – 3679Combined sources
Beta strandi373 – 3753Combined sources
Beta strandi378 – 3825Combined sources
Beta strandi386 – 3883Combined sources
Turni389 – 3924Combined sources
Beta strandi393 – 4008Combined sources
Beta strandi407 – 41610Combined sources
Turni428 – 4303Combined sources
Beta strandi432 – 4398Combined sources
Helixi441 – 4433Combined sources
Helixi452 – 4543Combined sources
Beta strandi455 – 4573Combined sources
Helixi459 – 4613Combined sources
Beta strandi462 – 4687Combined sources
Beta strandi471 – 4755Combined sources
Beta strandi481 – 4833Combined sources
Beta strandi487 – 4959Combined sources
Beta strandi503 – 51210Combined sources
Beta strandi519 – 5279Combined sources
Beta strandi537 – 5437Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1N67X-ray1.90A221-559[»]
ProteinModelPortaliQ53653.
SMRiQ53653. Positions 229-559.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ53653.

Family & Domainsi

Region

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

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi896 – 9005LPXTG sorting signalPROSITE-ProRule annotation

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi68 – 183116Thr-richAdd
BLAST
Compositional biasi546 – 56520Pro-richAdd
BLAST
Compositional biasi560 – 865306Asp/Ser-richAdd
BLAST

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
EntryMethodResolution (Å)ChainPositionsPDBsum
1N67X-ray1.90A221-559[»]
ProteinModelPortaliQ53653.
SMRiQ53653. Positions 229-559.
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.

Enzyme and pathway databases

BioCyciSAUR426430:GIXC-776-MONOMER.

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: September 7, 2016
This is version 108 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.