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Protein

Immunoglobulin G-binding protein G

Gene

spg

Organism
Streptococcus sp. group G
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Binds to the constant Fc region of IgG with high affinity.

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

IgG-binding protein

Names & Taxonomyi

Protein namesi
Recommended name:
Immunoglobulin G-binding protein G
Short name:
IgG-binding protein G
Gene namesi
Name:spg
OrganismiStreptococcus sp. group G
Taxonomic identifieri1320 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

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 – 33331 PublicationAdd
BLAST
Chaini34 – 417384Immunoglobulin G-binding protein GPRO_0000005657Add
BLAST
Propeptidei418 – 44831Removed by sortasePROSITE-ProRule annotationPRO_0000005658Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei417 – 4171Pentaglycyl murein peptidoglycan amidated threoninePROSITE-ProRule annotation

Keywords - PTMi

Peptidoglycan-anchor

Structurei

Secondary structure

1
448
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi227 – 2348Combined sources
Beta strandi239 – 24810Combined sources
Helixi249 – 26214Combined sources
Turni264 – 2663Combined sources
Beta strandi268 – 2725Combined sources
Turni273 – 2764Combined sources
Beta strandi277 – 2815Combined sources
Beta strandi297 – 3048Combined sources
Beta strandi309 – 31810Combined sources
Helixi319 – 33214Combined sources
Beta strandi338 – 3425Combined sources
Turni343 – 3464Combined sources
Beta strandi347 – 3515Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EM7X-ray2.00A228-282[»]
1GB1NMR-A228-282[»]
1IGCX-ray2.60A293-352[»]
1IGDX-ray1.10A293-352[»]
1LE3NMR-A267-282[»]
1MPENMR-A/B/C/D228-282[»]
1MVKX-ray2.50A/B/C/D/E/F/G/H/I/J/K/L228-282[»]
1PGAX-ray2.07A228-282[»]
1PGBX-ray1.92A228-282[»]
1PGXX-ray1.66A288-369[»]
1PN5NMR-A228-282[»]
1Q10NMR-A/B228-282[»]
2GB1NMR-A228-282[»]
2IGDX-ray1.10A293-352[»]
2IGHNMR-A292-352[»]
2J52NMR-A228-282[»]
2J53NMR-A228-282[»]
2K0PNMR-A228-282[»]
2KBTNMR-A228-282[»]
2KLKOther-A/B229-282[»]
2LGINMR-A229-282[»]
2MBBNMR-A229-282[»]
2N7JNMR-A299-352[»]
2NMQNMR-A298-352[»]
2PLPNMR-A228-281[»]
2RMMNMR-A/B229-282[»]
2RPVNMR-A226-282[»]
3GB1NMR-A228-282[»]
3MP9X-ray1.20A/B227-282[»]
4KGRX-ray2.00A/B/C/D/E/F/G/H227-282[»]
4KGSX-ray1.95A/B227-282[»]
4KGTX-ray2.00A/B227-282[»]
ProteinModelPortaliP06654.
SMRiP06654. Positions 95-148, 171-224, 229-282, 291-358.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06654.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati104 – 140371-1Add
BLAST
Repeati179 – 215371-2Add
BLAST
Repeati228 – 282552-1Add
BLAST
Repeati298 – 352552-2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni104 – 2151122 X 37 AA repeatsAdd
BLAST
Regioni228 – 3521252 X 55 AA repeatsAdd
BLAST
Regioni386 – 410255 X 5 AA repeats of [DE]-D-A-K-KAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi414 – 4185LPXTG sorting signalPROSITE-ProRule annotation

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi69 – 11143Ala-richAdd
BLAST

Keywords - Domaini

Repeat, Signal

Family and domain databases

InterProiIPR019948. Gram-positive_anchor.
IPR019950. Gram_pos_anchor.
IPR009063. Ig/albumin-bd.
IPR000724. IgG-bd_B.
IPR019931. LPXTG_anchor.
IPR005877. YSIRK_signal_dom.
[Graphical view]
PfamiPF00746. Gram_pos_anchor. 1 hit.
PF01378. IgG_binding_B. 2 hits.
[Graphical view]
PRINTSiPR00015. GPOSANCHOR.
SUPFAMiSSF46997. SSF46997. 2 hits.
TIGRFAMsiTIGR01167. LPXTG_anchor. 1 hit.
TIGR01168. 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.

P06654-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEKEKKVKYF LRKSAFGLAS VSAAFLVGST VFAVDSPIED TPIIRNGGEL
60 70 80 90 100
TNLLGNSETT LALRNEESAT ADLTAAAVAD TVAAAAAENA GAAAWEAAAA
110 120 130 140 150
ADALAKAKAD ALKEFNKYGV SDYYKNLINN AKTVEGIKDL QAQVVESAKK
160 170 180 190 200
ARISEATDGL SDFLKSQTPA EDTVKSIELA EAKVLANREL DKYGVSDYHK
210 220 230 240 250
NLINNAKTVE GVKELIDEIL AALPKTDTYK LILNGKTLKG ETTTEAVDAA
260 270 280 290 300
TAEKVFKQYA NDNGVDGEWT YDDATKTFTV TEKPEVIDAS ELTPAVTTYK
310 320 330 340 350
LVINGKTLKG ETTTKAVDAE TAEKAFKQYA NDNGVDGVWT YDDATKTFTV
360 370 380 390 400
TEMVTEVPGD APTEPEKPEA SIPLVPLTPA TPIAKDDAKK DDTKKEDAKK
410 420 430 440
PEAKKDDAKK AETLPTTGEG SNPFFTAAAL AVMAGAGALA VASKRKED
Length:448
Mass (Da):47,567
Last modified:January 1, 1988 - v1
Checksum:iA0759060C8F9E6CA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti43 – 442II → N AA sequence (PubMed:1985908).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M13825 Unassigned DNA. Translation: AAA03664.1.
PIRiA24496.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M13825 Unassigned DNA. Translation: AAA03664.1.
PIRiA24496.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EM7X-ray2.00A228-282[»]
1GB1NMR-A228-282[»]
1IGCX-ray2.60A293-352[»]
1IGDX-ray1.10A293-352[»]
1LE3NMR-A267-282[»]
1MPENMR-A/B/C/D228-282[»]
1MVKX-ray2.50A/B/C/D/E/F/G/H/I/J/K/L228-282[»]
1PGAX-ray2.07A228-282[»]
1PGBX-ray1.92A228-282[»]
1PGXX-ray1.66A288-369[»]
1PN5NMR-A228-282[»]
1Q10NMR-A/B228-282[»]
2GB1NMR-A228-282[»]
2IGDX-ray1.10A293-352[»]
2IGHNMR-A292-352[»]
2J52NMR-A228-282[»]
2J53NMR-A228-282[»]
2K0PNMR-A228-282[»]
2KBTNMR-A228-282[»]
2KLKOther-A/B229-282[»]
2LGINMR-A229-282[»]
2MBBNMR-A229-282[»]
2N7JNMR-A299-352[»]
2NMQNMR-A298-352[»]
2PLPNMR-A228-281[»]
2RMMNMR-A/B229-282[»]
2RPVNMR-A226-282[»]
3GB1NMR-A228-282[»]
3MP9X-ray1.20A/B227-282[»]
4KGRX-ray2.00A/B/C/D/E/F/G/H227-282[»]
4KGSX-ray1.95A/B227-282[»]
4KGTX-ray2.00A/B227-282[»]
ProteinModelPortaliP06654.
SMRiP06654. Positions 95-148, 171-224, 229-282, 291-358.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP06654.

Family and domain databases

InterProiIPR019948. Gram-positive_anchor.
IPR019950. Gram_pos_anchor.
IPR009063. Ig/albumin-bd.
IPR000724. IgG-bd_B.
IPR019931. LPXTG_anchor.
IPR005877. YSIRK_signal_dom.
[Graphical view]
PfamiPF00746. Gram_pos_anchor. 1 hit.
PF01378. IgG_binding_B. 2 hits.
[Graphical view]
PRINTSiPR00015. GPOSANCHOR.
SUPFAMiSSF46997. SSF46997. 2 hits.
TIGRFAMsiTIGR01167. LPXTG_anchor. 1 hit.
TIGR01168. YSIRK_signal. 1 hit.
PROSITEiPS50847. GRAM_POS_ANCHORING. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Gene for an immunoglobulin-binding protein from a group G streptococcus."
    Fahnestock S.R., Alexander P., Nagle J., Filpula D.
    J. Bacteriol. 167:870-880(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Streptococcal protein G. Gene structure and protein binding properties."
    Sjoebring U., Bjoerck L., Kastern W.
    J. Biol. Chem. 266:399-405(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 34-48; 62-77 AND 187-200.
  3. "Two crystal structures of the B1 immunoglobulin-binding domain of streptococcal protein G and comparison with NMR."
    Gallagher T., Alexander P., Bryan P., Gilliland G.L.
    Biochemistry 33:4721-4729(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.07 ANGSTROMS) OF 228-282.
  4. "The third IgG-binding domain from streptococcal protein G. An analysis by X-ray crystallography of the structure alone and in a complex with Fab."
    Derrick J.P., Wigley D.B.
    J. Mol. Biol. 243:906-918(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS) OF 293-351.
  5. "Crystal structure of the C2 fragment of streptococcal protein G in complex with the Fc domain of human IgG."
    Sauer-Eriksson A.E., Kleywegt G.J., Uhlen M., Jones T.A.
    Structure 3:265-278(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 297-352.
  6. Butterworth S., Lamzin V.S., Wigley D.B., Derrick J.P., Wilson K.S.
    Submitted (APR-1997) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS) OF 228-282.
  7. "A novel, highly stable fold of the immunoglobulin binding domain of streptococcal protein G."
    Gronenborn A.M., Filpula D.R., Essig N.Z., Achari A., Whitlow M., Wingfield P.T., Clore G.M.
    Science 253:657-661(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 298-351.

Entry informationi

Entry nameiSPG1_STRSG
AccessioniPrimary (citable) accession number: P06654
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: December 9, 2015
This is version 121 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, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

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.