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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

Enzyme and pathway databases

BioCyciSAUR282458:GJA5-2750-MONOMER.

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)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 4444By similarityAdd
BLAST
Chaini45 – 837793Clumping factor BPRO_0000042012Add
BLAST
Propeptidei838 – 87336Removed by sortasePROSITE-ProRule annotationPRO_0000042013Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei837 – 8371Pentaglycyl murein peptidoglycan amidated threoninePROSITE-ProRule annotation

Post-translational modificationi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei197 – 1982Cleavage; by aureolysinBy similarity
Sitei199 – 2002Cleavage; by aureolysinBy similarity

Keywords - PTMi

Peptidoglycan-anchor

Structurei

Secondary structure

1
873
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi216 – 2183Combined sources
Beta strandi219 – 2279Combined sources
Beta strandi229 – 2313Combined sources
Helixi233 – 2353Combined sources
Beta strandi239 – 24911Combined sources
Beta strandi256 – 2605Combined sources
Beta strandi265 – 2695Combined sources
Helixi274 – 2763Combined sources
Beta strandi279 – 2868Combined sources
Beta strandi292 – 2998Combined sources
Turni300 – 3034Combined sources
Beta strandi304 – 3096Combined sources
Helixi311 – 3133Combined sources
Beta strandi317 – 32913Combined sources
Turni331 – 3333Combined sources
Beta strandi336 – 3416Combined sources
Beta strandi344 – 3463Combined sources
Beta strandi349 – 3513Combined sources
Beta strandi354 – 3574Combined sources
Beta strandi373 – 3819Combined sources
Beta strandi384 – 3874Combined sources
Beta strandi389 – 3979Combined sources
Beta strandi403 – 41513Combined sources
Helixi417 – 4193Combined sources
Turni426 – 4283Combined sources
Beta strandi430 – 4378Combined sources
Helixi439 – 4413Combined sources
Beta strandi455 – 4573Combined sources
Helixi459 – 4613Combined sources
Turni463 – 4653Combined sources
Beta strandi473 – 4819Combined sources
Beta strandi485 – 4939Combined sources
Beta strandi501 – 5099Combined sources
Turni511 – 5133Combined sources
Beta strandi518 – 52912Combined sources
Beta strandi532 – 5387Combined sources

3D structure databases

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

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni45 – 542498Ligand binding A regionBy similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi272 – 2765MIDAS-like motif
Motifi834 – 8385LPXTG sorting signalPROSITE-ProRule annotation

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi543 – 58644Pro-richAdd
BLAST
Compositional biasi585 – 799215Asp/Ser-richAdd
BLAST

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
EntryMethodResolution (Å)ChainPositionsPDBsum
4F1ZX-ray2.30A197-542[»]
4F20X-ray2.50A197-542[»]
4F24X-ray2.51A197-542[»]
4F27X-ray1.92A197-542[»]
ProteinModelPortaliQ6GDH2.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

KOiK14192.

Enzyme and pathway databases

BioCyciSAUR282458:GJA5-2750-MONOMER.

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: September 7, 2016
This is version 80 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.