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Protein

Clumping factor B

Gene

clfB

Organism
Staphylococcus aureus (strain N315)
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:SA2423
OrganismiStaphylococcus aureus (strain N315)
Taxonomic identifieri158879 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus
Proteomesi
  • UP000000751 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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 44Sequence analysisAdd BLAST44
ChainiPRO_000004201045 – 841Clumping factor BAdd BLAST797
PropeptideiPRO_0000042011842 – 877Removed by sortasePROSITE-ProRule annotationAdd BLAST36

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei841Pentaglycyl 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

1877
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 – 247Combined sources9
Beta strandi256 – 260Combined sources5
Beta strandi265 – 268Combined sources4
Turni274 – 278Combined sources5
Beta strandi279 – 286Combined sources8
Beta strandi292 – 299Combined sources8
Turni300 – 303Combined sources4
Beta strandi304 – 309Combined sources6
Helixi311 – 313Combined sources3
Beta strandi320 – 329Combined sources10
Turni331 – 333Combined sources3
Beta strandi336 – 341Combined sources6
Beta strandi344 – 348Combined sources5
Beta strandi354 – 357Combined sources4
Beta strandi374 – 381Combined sources8
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
Helixi460 – 462Combined sources3
Beta strandi465 – 467Combined sources3
Beta strandi473 – 481Combined sources9
Beta strandi485 – 493Combined sources9
Beta strandi500 – 509Combined sources10
Turni511 – 513Combined sources3
Beta strandi518 – 526Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3ASWX-ray2.60A212-531[»]
3AT0X-ray2.50A212-541[»]
3AU0X-ray2.45A203-541[»]
ProteinModelPortaliQ7A382.
SMRiQ7A382.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ7A382.

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
Motifi838 – 842LPXTG sorting signalPROSITE-ProRule annotation5

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi543 – 584Pro-richAdd BLAST42
Compositional biasi581 – 803Asp/Ser-richAdd BLAST223

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.
OMAiEREIMST.

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.

Q7A382-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKRIDYLSN KQNKYSIRRF TVGTTSVIVG ATILFGIGNH QAQASEQSND
60 70 80 90 100
TTQSSKNNAS ADSEKNNMIE TPQLNTTAND TSDISANTNS ANVDSTTKPM
110 120 130 140 150
STQTSNTTTT EPASTNETPQ PTAIKNQATA AKMQDQTVPQ EANSQVDNKT
160 170 180 190 200
TNDANSIATN SELKNSQTLD LPQSSPQTIS NAQGTSKPSV RTRAVRSLAV
210 220 230 240 250
AEPVVNAADA KGTNVNDKVT ASNFKLEKTT FDPNQSGNTF MAANFTVTDK
260 270 280 290 300
VKSGDYFTAK LPDSLTGNGD VDYSNSNNTM PIADIKSTNG DVVAKATYDI
310 320 330 340 350
LTKTYTFVFT DYVNNKENIN GQFSLPLFTD RAKAPKSGTY DANINIADEM
360 370 380 390 400
FNNKITYNYS SPIAGIDKPN GANISSQIIG VDTASGQNTY KQTVFVNPKQ
410 420 430 440 450
RVLGNTWVYI KGYQDKIEES SGKVSATDTK LRIFEVNDTS KLSDSYYADP
460 470 480 490 500
NDSNLKEVTD QFKNRIYYEH PNVASIKFGD ITKTYVVLVE GHYDNTGKNL
510 520 530 540 550
KTQVIQENVD PVTNRDYSIF GWNNENVVRY GGGSADGDSA VNPKDPTPGP
560 570 580 590 600
PVDPEPSPDP EPEPTPDPEP SPDPEPEPSP DPDPDSDSDS DSGSDSDSGS
610 620 630 640 650
DSDSESDSDS DSDSDSDSDS DSESDSDSES DSDSDSDSDS DSDSDSESDS
660 670 680 690 700
DSDSDSDSDS DSDSESDSDS ESDSESDSDS DSDSDSDSDS DSDSDSDSDS
710 720 730 740 750
DSDSDSDSDS DSESDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS
760 770 780 790 800
DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS
810 820 830 840 850
DSDSRVTPPN NEQKAPSNPK GEVNHSNKVS KQHKTDALPE TGDKSENTNA
860 870
TLFGAMMALL GSLLLFRKRK QDHKEKA
Length:877
Mass (Da):93,651
Last modified:July 5, 2004 - v1
Checksum:iF0EF0A57AFDB357F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000018 Genomic DNA. Translation: BAB43728.1.
PIRiF90070.
RefSeqiWP_000745891.1. NC_002745.2.

Genome annotation databases

EnsemblBacteriaiBAB43728; BAB43728; BAB43728.
KEGGisau:SA2423.
PATRICi19577414. VBIStaAur116463_2625.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000018 Genomic DNA. Translation: BAB43728.1.
PIRiF90070.
RefSeqiWP_000745891.1. NC_002745.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3ASWX-ray2.60A212-531[»]
3AT0X-ray2.50A212-541[»]
3AU0X-ray2.45A203-541[»]
ProteinModelPortaliQ7A382.
SMRiQ7A382.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAB43728; BAB43728; BAB43728.
KEGGisau:SA2423.
PATRICi19577414. VBIStaAur116463_2625.

Phylogenomic databases

KOiK14192.
OMAiEREIMST.

Miscellaneous databases

EvolutionaryTraceiQ7A382.
PROiQ7A382.

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_STAAN
AccessioniPrimary (citable) accession number: Q7A382
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 27, 2005
Last sequence update: July 5, 2004
Last modified: November 2, 2016
This is version 89 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

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.