SPG1_STRSG
ID SPG1_STRSG Reviewed; 448 AA.
AC P06654;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Immunoglobulin G-binding protein G;
DE Short=IgG-binding protein G;
DE Flags: Precursor;
GN Name=spg;
OS Streptococcus sp. group G.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1320;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3745123; DOI=10.1128/jb.167.3.870-880.1986;
RA Fahnestock S.R., Alexander P., Nagle J., Filpula D.;
RT "Gene for an immunoglobulin-binding protein from a group G streptococcus.";
RL J. Bacteriol. 167:870-880(1986).
RN [2]
RP PROTEIN SEQUENCE OF 34-48; 62-77 AND 187-200.
RX PubMed=1985908; DOI=10.1016/s0021-9258(18)52448-0;
RA Sjoebring U., Bjoerck L., Kastern W.;
RT "Streptococcal protein G. Gene structure and protein binding properties.";
RL J. Biol. Chem. 266:399-405(1991).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.07 ANGSTROMS) OF 228-282.
RX PubMed=8161530; DOI=10.1021/bi00181a032;
RA Gallagher T., Alexander P., Bryan P., Gilliland G.L.;
RT "Two crystal structures of the B1 immunoglobulin-binding domain of
RT streptococcal protein G and comparison with NMR.";
RL Biochemistry 33:4721-4729(1994).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS) OF 293-351.
RX PubMed=7966308; DOI=10.1006/jmbi.1994.1691;
RA Derrick J.P., Wigley D.B.;
RT "The third IgG-binding domain from streptococcal protein G. An analysis by
RT X-ray crystallography of the structure alone and in a complex with Fab.";
RL J. Mol. Biol. 243:906-918(1994).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 297-352.
RX PubMed=7788293; DOI=10.1016/s0969-2126(01)00157-5;
RA Sauer-Eriksson A.E., Kleywegt G.J., Uhlen M., Jones T.A.;
RT "Crystal structure of the C2 fragment of streptococcal protein G in complex
RT with the Fc domain of human IgG.";
RL Structure 3:265-278(1995).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS) OF 228-282.
RA Butterworth S., Lamzin V.S., Wigley D.B., Derrick J.P., Wilson K.S.;
RL Submitted (APR-1997) to the PDB data bank.
RN [7]
RP STRUCTURE BY NMR OF 298-351.
RX PubMed=1871600; DOI=10.1126/science.1871600;
RA Gronenborn A.M., Filpula D.R., Essig N.Z., Achari A., Whitlow M.,
RA Wingfield P.T., Clore G.M.;
RT "A novel, highly stable fold of the immunoglobulin binding domain of
RT streptococcal protein G.";
RL Science 253:657-661(1991).
CC -!- FUNCTION: Binds to the constant Fc region of IgG with high affinity.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|PROSITE-
CC ProRule:PRU00477}; Peptidoglycan-anchor {ECO:0000255|PROSITE-
CC ProRule:PRU00477}.
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DR EMBL; M13825; AAA03664.1; -; Unassigned_DNA.
DR PIR; A24496; A24496.
DR PDB; 1EM7; X-ray; 2.00 A; A=228-282.
DR PDB; 1GB1; NMR; -; A=228-282.
DR PDB; 1IGC; X-ray; 2.60 A; A=293-352.
DR PDB; 1IGD; X-ray; 1.10 A; A=293-352.
DR PDB; 1LE3; NMR; -; A=267-282.
DR PDB; 1MPE; NMR; -; A/B/C/D=228-282.
DR PDB; 1MVK; X-ray; 2.50 A; A/B/C/D/E/F/G/H/I/J/K/L=228-282.
DR PDB; 1PGA; X-ray; 2.07 A; A=228-282.
DR PDB; 1PGB; X-ray; 1.92 A; A=228-282.
DR PDB; 1PGX; X-ray; 1.66 A; A=288-369.
DR PDB; 1PN5; NMR; -; A=228-282.
DR PDB; 1Q10; NMR; -; A/B=228-282.
DR PDB; 2GB1; NMR; -; A=228-282.
DR PDB; 2IGD; X-ray; 1.10 A; A=293-352.
DR PDB; 2IGH; NMR; -; A=292-352.
DR PDB; 2J52; NMR; -; A=228-282.
DR PDB; 2J53; NMR; -; A=228-282.
DR PDB; 2K0P; NMR; -; A=228-282.
DR PDB; 2KBT; NMR; -; A=228-282.
DR PDB; 2KLK; Other; -; A/B=229-282.
DR PDB; 2LGI; NMR; -; A=229-282.
DR PDB; 2MBB; NMR; -; A=229-282.
DR PDB; 2N7J; NMR; -; A=299-352.
DR PDB; 2NMQ; NMR; -; A=298-352.
DR PDB; 2PLP; NMR; -; A=228-281.
DR PDB; 2RMM; NMR; -; A/B=229-282.
DR PDB; 2RPV; NMR; -; A=226-282.
DR PDB; 3GB1; NMR; -; A=228-282.
DR PDB; 3MP9; X-ray; 1.20 A; A/B=227-282.
DR PDB; 4KGR; X-ray; 2.00 A; A/B/C/D/E/F/G/H=227-282.
DR PDB; 4KGS; X-ray; 1.95 A; A/B=227-282.
DR PDB; 4KGT; X-ray; 2.00 A; A/B=227-282.
DR PDB; 6CNE; X-ray; 1.20 A; A/B=229-282.
DR PDB; 6L91; X-ray; 1.84 A; A=227-282.
DR PDB; 6L9B; X-ray; 1.95 A; A=227-282.
DR PDB; 6L9D; X-ray; 1.73 A; A=227-282.
DR PDB; 6LJI; X-ray; 1.84 A; A/B=227-282.
DR PDB; 6V9I; EM; 5.20 A; C=229-282.
DR PDB; 7RXC; EM; 3.20 A; B=295-352.
DR PDB; 7RXD; EM; 3.60 A; B=295-352.
DR PDBsum; 1EM7; -.
DR PDBsum; 1GB1; -.
DR PDBsum; 1IGC; -.
DR PDBsum; 1IGD; -.
DR PDBsum; 1LE3; -.
DR PDBsum; 1MPE; -.
DR PDBsum; 1MVK; -.
DR PDBsum; 1PGA; -.
DR PDBsum; 1PGB; -.
DR PDBsum; 1PGX; -.
DR PDBsum; 1PN5; -.
DR PDBsum; 1Q10; -.
DR PDBsum; 2GB1; -.
DR PDBsum; 2IGD; -.
DR PDBsum; 2IGH; -.
DR PDBsum; 2J52; -.
DR PDBsum; 2J53; -.
DR PDBsum; 2K0P; -.
DR PDBsum; 2KBT; -.
DR PDBsum; 2KLK; -.
DR PDBsum; 2LGI; -.
DR PDBsum; 2MBB; -.
DR PDBsum; 2N7J; -.
DR PDBsum; 2NMQ; -.
DR PDBsum; 2PLP; -.
DR PDBsum; 2RMM; -.
DR PDBsum; 2RPV; -.
DR PDBsum; 3GB1; -.
DR PDBsum; 3MP9; -.
DR PDBsum; 4KGR; -.
DR PDBsum; 4KGS; -.
DR PDBsum; 4KGT; -.
DR PDBsum; 6CNE; -.
DR PDBsum; 6L91; -.
DR PDBsum; 6L9B; -.
DR PDBsum; 6L9D; -.
DR PDBsum; 6LJI; -.
DR PDBsum; 6V9I; -.
DR PDBsum; 7RXC; -.
DR PDBsum; 7RXD; -.
DR AlphaFoldDB; P06654; -.
DR BMRB; P06654; -.
DR SMR; P06654; -.
DR PRIDE; P06654; -.
DR EvolutionaryTrace; P06654; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0019864; F:IgG binding; IEA:UniProtKB-KW.
DR InterPro; IPR035152; GA-like.
DR InterPro; IPR009063; Ig/albumin-bd_sf.
DR InterPro; IPR000724; IgG-bd_B.
DR InterPro; IPR019931; LPXTG_anchor.
DR InterPro; IPR019950; M_anchor.
DR InterPro; IPR005877; YSIRK_signal_dom.
DR Pfam; PF17573; GA-like; 2.
DR Pfam; PF00746; Gram_pos_anchor; 1.
DR Pfam; PF01378; IgG_binding_B; 2.
DR PRINTS; PR00015; GPOSANCHOR.
DR SUPFAM; SSF46997; SSF46997; 2.
DR TIGRFAMs; TIGR01168; YSIRK_signal; 1.
DR PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell wall; Direct protein sequencing; IgG-binding protein;
KW Peptidoglycan-anchor; Repeat; Secreted; Signal.
FT SIGNAL 1..33
FT /evidence="ECO:0000269|PubMed:1985908"
FT CHAIN 34..417
FT /note="Immunoglobulin G-binding protein G"
FT /id="PRO_0000005657"
FT PROPEP 418..448
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT /id="PRO_0000005658"
FT REPEAT 104..140
FT /note="1-1"
FT REPEAT 179..215
FT /note="1-2"
FT REPEAT 228..282
FT /note="2-1"
FT REPEAT 298..352
FT /note="2-2"
FT REGION 104..215
FT /note="2 X 37 AA repeats"
FT REGION 228..352
FT /note="2 X 55 AA repeats"
FT REGION 358..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 386..410
FT /note="5 X 5 AA repeats of [DE]-D-A-K-K"
FT MOTIF 414..418
FT /note="LPXTG sorting signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT COMPBIAS 384..413
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 417
FT /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT CONFLICT 43..44
FT /note="II -> N (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 227..234
FT /evidence="ECO:0007829|PDB:3MP9"
FT STRAND 239..248
FT /evidence="ECO:0007829|PDB:3MP9"
FT HELIX 249..262
FT /evidence="ECO:0007829|PDB:3MP9"
FT TURN 264..266
FT /evidence="ECO:0007829|PDB:1Q10"
FT STRAND 268..272
FT /evidence="ECO:0007829|PDB:3MP9"
FT TURN 273..276
FT /evidence="ECO:0007829|PDB:3MP9"
FT STRAND 277..281
FT /evidence="ECO:0007829|PDB:3MP9"
FT STRAND 297..304
FT /evidence="ECO:0007829|PDB:1IGD"
FT STRAND 309..318
FT /evidence="ECO:0007829|PDB:1IGD"
FT HELIX 319..332
FT /evidence="ECO:0007829|PDB:1IGD"
FT STRAND 338..342
FT /evidence="ECO:0007829|PDB:1IGD"
FT TURN 343..346
FT /evidence="ECO:0007829|PDB:1IGD"
FT STRAND 347..351
FT /evidence="ECO:0007829|PDB:1IGD"
SQ SEQUENCE 448 AA; 47567 MW; A0759060C8F9E6CA CRC64;
MEKEKKVKYF LRKSAFGLAS VSAAFLVGST VFAVDSPIED TPIIRNGGEL TNLLGNSETT
LALRNEESAT ADLTAAAVAD TVAAAAAENA GAAAWEAAAA ADALAKAKAD ALKEFNKYGV
SDYYKNLINN AKTVEGIKDL QAQVVESAKK ARISEATDGL SDFLKSQTPA EDTVKSIELA
EAKVLANREL DKYGVSDYHK NLINNAKTVE GVKELIDEIL AALPKTDTYK LILNGKTLKG
ETTTEAVDAA TAEKVFKQYA NDNGVDGEWT YDDATKTFTV TEKPEVIDAS ELTPAVTTYK
LVINGKTLKG ETTTKAVDAE TAEKAFKQYA NDNGVDGVWT YDDATKTFTV TEMVTEVPGD
APTEPEKPEA SIPLVPLTPA TPIAKDDAKK DDTKKEDAKK PEAKKDDAKK AETLPTTGEG
SNPFFTAAAL AVMAGAGALA VASKRKED
