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Protein

Clumping factor B

Gene

clfB

Organism
Staphylococcus aureus (strain MRSA252)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Cell surface-associated protein implicated in virulence by promoting bacterial attachment to both alpha- and beta-chains of human fibrinogen and inducing the formation of bacterial clumps.By similarity

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Virulence

Names & Taxonomyi

Protein namesi
Recommended name:
Clumping factor B
Alternative name(s):
Fibrinogen receptor B
Fibrinogen-binding protein B
Gene namesi
Name:clfB
Ordered Locus Names:SAR2709
OrganismiStaphylococcus aureus (strain MRSA252)
Taxonomic identifieri282458 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus

Subcellular locationi

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

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell wall, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 44By similarityAdd BLAST44
ChainiPRO_000004201245 – 837Clumping factor BAdd BLAST793
PropeptideiPRO_0000042013838 – 873Removed by sortasePROSITE-ProRule annotationAdd BLAST36

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei837Pentaglycyl murein peptidoglycan amidated threoninePROSITE-ProRule annotation1

Post-translational modificationi

Proteolytically cleaved by aureolysin (aur). This cleavage leads to the inactivation of ClfB (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei197 – 198Cleavage; by aureolysinBy similarity2
Sitei199 – 200Cleavage; by aureolysinBy similarity2

Keywords - PTMi

Peptidoglycan-anchor

Structurei

Secondary structure

1873
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi216 – 218Combined sources3
Beta strandi219 – 227Combined sources9
Beta strandi229 – 231Combined sources3
Helixi233 – 235Combined sources3
Beta strandi239 – 249Combined sources11
Beta strandi256 – 260Combined sources5
Beta strandi265 – 269Combined sources5
Helixi274 – 276Combined sources3
Beta strandi279 – 286Combined sources8
Beta strandi292 – 299Combined sources8
Turni300 – 303Combined sources4
Beta strandi304 – 309Combined sources6
Helixi311 – 313Combined sources3
Beta strandi317 – 329Combined sources13
Turni331 – 333Combined sources3
Beta strandi336 – 341Combined sources6
Beta strandi344 – 346Combined sources3
Beta strandi349 – 351Combined sources3
Beta strandi354 – 357Combined sources4
Beta strandi373 – 381Combined sources9
Beta strandi384 – 387Combined sources4
Beta strandi389 – 397Combined sources9
Beta strandi403 – 415Combined sources13
Helixi417 – 419Combined sources3
Turni426 – 428Combined sources3
Beta strandi430 – 437Combined sources8
Helixi439 – 441Combined sources3
Beta strandi455 – 457Combined sources3
Helixi459 – 461Combined sources3
Turni463 – 465Combined sources3
Beta strandi473 – 481Combined sources9
Beta strandi485 – 493Combined sources9
Beta strandi501 – 509Combined sources9
Turni511 – 513Combined sources3
Beta strandi518 – 529Combined sources12
Beta strandi532 – 538Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4F1ZX-ray2.30A197-542[»]
4F20X-ray2.50A197-542[»]
4F24X-ray2.51A197-542[»]
4F27X-ray1.92A197-542[»]
ProteinModelPortaliQ6GDH2.
SMRiQ6GDH2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni45 – 542Ligand binding A regionBy similarityAdd BLAST498

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi272 – 276MIDAS-like motif5
Motifi834 – 838LPXTG sorting signalPROSITE-ProRule annotation5

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi543 – 586Pro-richAdd BLAST44
Compositional biasi585 – 799Asp/Ser-richAdd BLAST215

Domaini

The Asp/Ser-rich domain functions as a stalk to allow the ligand binding domain to be displayed in a functional form on the cell surface.By similarity

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

KOiK14192.

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.

Q6GDH2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKRIDYLSN KQNKYSIRRF TVGTTSVIVG ATILFGIGNH QAQASEQSND
60 70 80 90 100
TTQSSKNNAS ADSEKNNTIE TPQLNTTAND TSDISANTNS ANVDSTAKTM
110 120 130 140 150
STQTSNTTTT EPASTNETPQ PTAIKDQATA AKMQDQTVPQ EANSQVDNKT
160 170 180 190 200
TNDANNIATN SELKNPQTLD LPQSSPQTIS NAQGTSKPSV RTRAVRSLAV
210 220 230 240 250
AEPVVNAADA KGTNVNDKVT ASDFKLEKTA FDPNQSGNTF MAANFKVTGQ
260 270 280 290 300
VKSGDYFTAK LPDSVTGNGD VDYSNSNNTM PIADIKSTNG DVVAKATYDI
310 320 330 340 350
LTKTYTFVFT DYVNDKENIN GQFSLPLFTD RAKAPKSGTY DANINIADEM
360 370 380 390 400
FDNKITYNYS SPIAGIDKPN GANISSQIIG VDTASGQNTY KQTVFVNPKQ
410 420 430 440 450
RVLGNTWVYI KGYQDKIEES SGKVSATDTK LRIFEVNDTS KLSDSYYADP
460 470 480 490 500
NDSNLKEVTG EFKDKISYKY DNVASINFGD INKTYVVLVE GHYDNTGKNL
510 520 530 540 550
KTQVIQENID PATGKDYSIF GWNNENVVRY GGGSADGDSA VNPVDPTPGP
560 570 580 590 600
PVDPEPEPEP TPDPEPSPEP EPEPTPDPEP SPEPDPDSDS DSDSGSDSDS
610 620 630 640 650
GSDSDSDSDS DSDSDSDSNS DSESDSDSDS DSDSDSDSDS DSDSDSDSDS
660 670 680 690 700
DSESDSDSDS DSDSDSDSDS DSDSDSDSNS DSDSDSDSDS DSDSDSDSDS
710 720 730 740 750
DSESDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSES DSESDSDSDS
760 770 780 790 800
ESDSDSDPDS ESDSDSDSDS DSDSDSDSES DSDSESDSDS DSDSDSDSDS
810 820 830 840 850
RVTPPNNEQK APSNPKGEVN HSNKASKQHQ TDALPETGDK SENTNATLFD
860 870
AMVALLGSLL LFRKRKQDHK EKA
Length:873
Mass (Da):92,996
Last modified:July 19, 2004 - v1
Checksum:iFC2093B51A4E71EF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX571856 Genomic DNA. Translation: CAG41687.1.
RefSeqiWP_000745917.1. NC_002952.2.

Genome annotation databases

EnsemblBacteriaiCAG41687; CAG41687; SAR2709.
KEGGisar:SAR2709.
PATRICi19549132. VBIStaAur71814_2744.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX571856 Genomic DNA. Translation: CAG41687.1.
RefSeqiWP_000745917.1. NC_002952.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4F1ZX-ray2.30A197-542[»]
4F20X-ray2.50A197-542[»]
4F24X-ray2.51A197-542[»]
4F27X-ray1.92A197-542[»]
ProteinModelPortaliQ6GDH2.
SMRiQ6GDH2.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAG41687; CAG41687; SAR2709.
KEGGisar:SAR2709.
PATRICi19549132. VBIStaAur71814_2744.

Phylogenomic databases

KOiK14192.

Miscellaneous databases

PROiQ6GDH2.

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 nameiCLFB_STAAR
AccessioniPrimary (citable) accession number: Q6GDH2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 27, 2005
Last sequence update: July 19, 2004
Last modified: November 2, 2016
This is version 81 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

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.