SPG2_STRSG
ID SPG2_STRSG Reviewed; 593 AA.
AC P19909;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 25-MAY-2022, entry version 157.
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].
RC STRAIN=G148;
RX PubMed=3665928; DOI=10.1111/j.1432-1033.1987.tb13423.x;
RA Olsson A., Eliasson M., Guss B., Nilsson B., Hellman U., Lindberg M.,
RA Uhlen M.;
RT "Structure and evolution of the repetitive gene encoding streptococcal
RT protein G.";
RL Eur. J. Biochem. 168:319-324(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=GX7805;
RX PubMed=3658689; DOI=10.1093/nar/15.17.7210;
RA Filpula D., Alexander P., Fahnestock S.R.;
RT "Nucleotide sequence of the protein G gene from Streptococcus GX7805, and
RT comparison to previously reported sequences.";
RL Nucleic Acids Res. 15:7210-7210(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 114-593.
RC STRAIN=G148;
RX PubMed=3017704; DOI=10.1002/j.1460-2075.1986.tb04398.x;
RA Guss B., Eliasson M., Olsson A., Uhlen M., Frej A.-K., Joernvall H.,
RA Flock J.-I., Lindberg M.;
RT "Structure of the IgG-binding regions of streptococcal protein G.";
RL EMBO J. 5:1567-1575(1986).
RN [4]
RP STRUCTURE BY NMR OF 371-427.
RC STRAIN=G148;
RX PubMed=9628485; DOI=10.1038/nsb0698-470;
RA Malakauskas S.M., Mayo S.L.;
RT "Design, structure and stability of a hyperthermophilic protein variant.";
RL Nat. Struct. Biol. 5:470-475(1998).
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; X06173; CAA29540.1; -; Genomic_DNA.
DR EMBL; Y00428; CAA68489.1; -; Genomic_DNA.
DR EMBL; X04015; CAA27638.1; -; Genomic_DNA.
DR PIR; S00128; S00128.
DR PDB; 1FCC; X-ray; 3.20 A; C/D=372-427.
DR PDB; 1FCL; NMR; -; A=372-427.
DR PDB; 1FD6; NMR; -; A=372-427.
DR PDB; 1GB4; NMR; -; A=372-427.
DR PDB; 1GJS; NMR; -; A=254-299.
DR PDB; 1GJT; NMR; -; A=254-299.
DR PDB; 1IBX; NMR; -; B=-.
DR PDB; 1P7E; NMR; -; A=444-497.
DR PDB; 1P7F; NMR; -; A=444-497.
DR PDB; 1QKZ; X-ray; 1.95 A; A=368-430.
DR PDB; 1UWX; X-ray; 2.20 A; A/B=368-430.
DR PDB; 1ZXH; NMR; -; A=453-495.
DR PDB; 2GI9; X-ray; 1.14 A; A=303-357.
DR PDB; 2I2Y; NMR; -; A=304-357.
DR PDB; 2I38; NMR; -; A=304-357.
DR PDB; 2IGG; NMR; -; A=367-430.
DR PDB; 2JSV; NMR; -; X=303-357.
DR PDB; 2JU6; NMR; -; X=304-357.
DR PDB; 2KHU; NMR; -; A=304-357.
DR PDB; 2KHW; NMR; -; A=304-357.
DR PDB; 2KN4; NMR; -; A=304-357.
DR PDB; 2KQ4; NMR; -; X=303-357.
DR PDB; 2KWD; NMR; -; A/B/C/D/E=304-357.
DR PDB; 2LUM; NMR; -; A=444-497.
DR PDB; 2N9K; NMR; -; A=303-357.
DR PDB; 2N9L; NMR; -; A=303-357.
DR PDB; 2OED; NMR; -; A=444-497.
DR PDB; 2ON8; X-ray; 1.35 A; A=373-427.
DR PDB; 2ONQ; X-ray; 1.70 A; A=375-427.
DR PDB; 2QMT; X-ray; 1.05 A; A=303-357.
DR PDB; 3FIL; X-ray; 0.88 A; A/B=303-357.
DR PDB; 3UI3; X-ray; 2.80 A; A/B=304-357.
DR PDB; 3V3X; X-ray; 2.00 A; A/B/C/D=304-357.
DR PDB; 4OZA; X-ray; 2.20 A; A=302-357.
DR PDB; 4OZB; X-ray; 1.80 A; A/B=302-357.
DR PDB; 4OZC; X-ray; 2.30 A; A=302-357.
DR PDB; 4WH4; X-ray; 2.20 A; A/B=304-357.
DR PDB; 5BMG; X-ray; 2.20 A; A/B/C/D/E/F/G/H=304-357.
DR PDB; 5BMH; X-ray; 1.60 A; A=304-357.
DR PDB; 5BMI; X-ray; 2.50 A; A=304-357.
DR PDB; 5HFY; X-ray; 1.95 A; A/B=302-357.
DR PDB; 5HG2; X-ray; 1.80 A; A/B/C/D=302-357.
DR PDB; 5HI1; X-ray; 2.15 A; A/B/C/D/E/F/G/H=302-357.
DR PDB; 5LDE; X-ray; 3.38 A; A/B=304-356.
DR PDB; 5UB0; NMR; -; A=373-427.
DR PDB; 5UBS; NMR; -; A=373-427.
DR PDB; 5UCE; NMR; -; A=373-427.
DR PDB; 5UCF; NMR; -; A=373-427.
DR PDB; 6C9O; X-ray; 1.20 A; A/B=304-357.
DR PDB; 6CHE; X-ray; 1.10 A; A=304-357.
DR PDB; 6CPZ; X-ray; 1.12 A; A/B=304-357.
DR PDB; 6CTE; X-ray; 1.20 A; A/B=304-357.
DR PDB; 6HKA; NMR; -; A=304-357.
DR PDB; 6HPJ; NMR; -; B=304-357.
DR PDB; 6KMC; X-ray; 1.84 A; A/B=302-357.
DR PDB; 6NJF; NMR; -; A=373-427.
DR PDB; 6NL6; X-ray; 1.40 A; A/B/C/D=303-357.
DR PDB; 6NL7; X-ray; 1.40 A; A/B/C/D=303-357.
DR PDB; 6NL8; X-ray; 1.50 A; A=303-357.
DR PDB; 6NL9; X-ray; 1.70 A; A/B/C/D=303-357.
DR PDB; 6NLA; X-ray; 1.34 A; A=303-357.
DR PDB; 6NLB; X-ray; 2.30 A; A/B/C/D=303-357.
DR PDB; 6O41; X-ray; 2.46 A; M/N/O=437-497.
DR PDB; 6OC7; X-ray; 1.30 A; C=438-497.
DR PDB; 6U8C; X-ray; 2.61 A; A/B=368-430.
DR PDB; 6UUH; X-ray; 2.70 A; E/F=437-497.
DR PDB; 6UYG; X-ray; 3.38 A; G=437-497.
DR PDB; 6W00; X-ray; 1.85 A; G=440-497.
DR PDB; 6WFW; X-ray; 2.09 A; G=439-497.
DR PDB; 7DA8; X-ray; 2.40 A; A=303-357.
DR PDBsum; 1FCC; -.
DR PDBsum; 1FCL; -.
DR PDBsum; 1FD6; -.
DR PDBsum; 1GB4; -.
DR PDBsum; 1GJS; -.
DR PDBsum; 1GJT; -.
DR PDBsum; 1IBX; -.
DR PDBsum; 1P7E; -.
DR PDBsum; 1P7F; -.
DR PDBsum; 1QKZ; -.
DR PDBsum; 1UWX; -.
DR PDBsum; 1ZXH; -.
DR PDBsum; 2GI9; -.
DR PDBsum; 2I2Y; -.
DR PDBsum; 2I38; -.
DR PDBsum; 2IGG; -.
DR PDBsum; 2JSV; -.
DR PDBsum; 2JU6; -.
DR PDBsum; 2KHU; -.
DR PDBsum; 2KHW; -.
DR PDBsum; 2KN4; -.
DR PDBsum; 2KQ4; -.
DR PDBsum; 2KWD; -.
DR PDBsum; 2LUM; -.
DR PDBsum; 2N9K; -.
DR PDBsum; 2N9L; -.
DR PDBsum; 2OED; -.
DR PDBsum; 2ON8; -.
DR PDBsum; 2ONQ; -.
DR PDBsum; 2QMT; -.
DR PDBsum; 3FIL; -.
DR PDBsum; 3UI3; -.
DR PDBsum; 3V3X; -.
DR PDBsum; 4OZA; -.
DR PDBsum; 4OZB; -.
DR PDBsum; 4OZC; -.
DR PDBsum; 4WH4; -.
DR PDBsum; 5BMG; -.
DR PDBsum; 5BMH; -.
DR PDBsum; 5BMI; -.
DR PDBsum; 5HFY; -.
DR PDBsum; 5HG2; -.
DR PDBsum; 5HI1; -.
DR PDBsum; 5LDE; -.
DR PDBsum; 5UB0; -.
DR PDBsum; 5UBS; -.
DR PDBsum; 5UCE; -.
DR PDBsum; 5UCF; -.
DR PDBsum; 6C9O; -.
DR PDBsum; 6CHE; -.
DR PDBsum; 6CPZ; -.
DR PDBsum; 6CTE; -.
DR PDBsum; 6HKA; -.
DR PDBsum; 6HPJ; -.
DR PDBsum; 6KMC; -.
DR PDBsum; 6NJF; -.
DR PDBsum; 6NL6; -.
DR PDBsum; 6NL7; -.
DR PDBsum; 6NL8; -.
DR PDBsum; 6NL9; -.
DR PDBsum; 6NLA; -.
DR PDBsum; 6NLB; -.
DR PDBsum; 6O41; -.
DR PDBsum; 6OC7; -.
DR PDBsum; 6U8C; -.
DR PDBsum; 6UUH; -.
DR PDBsum; 6UYG; -.
DR PDBsum; 6W00; -.
DR PDBsum; 6WFW; -.
DR PDBsum; 7DA8; -.
DR AlphaFoldDB; P19909; -.
DR BMRB; P19909; -.
DR SMR; P19909; -.
DR MINT; P19909; -.
DR DrugBank; DB04464; N-Formylmethionine.
DR EvolutionaryTrace; P19909; -.
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; 3.
DR Pfam; PF00746; Gram_pos_anchor; 1.
DR Pfam; PF01378; IgG_binding_B; 3.
DR PRINTS; PR00015; GPOSANCHOR.
DR SUPFAM; SSF46997; SSF46997; 3.
DR TIGRFAMs; TIGR01168; YSIRK_signal; 1.
DR PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell wall; IgG-binding protein; Peptidoglycan-anchor; Repeat;
KW Secreted; Signal.
FT SIGNAL 1..33
FT CHAIN 34..562
FT /note="Immunoglobulin G-binding protein G"
FT /id="PRO_0000005659"
FT PROPEP 563..593
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT /id="PRO_0000005660"
FT REPEAT 104..140
FT /note="1-1"
FT REPEAT 179..215
FT /note="1-2"
FT REPEAT 254..290
FT /note="1-3"
FT REPEAT 303..357
FT /note="2-1"
FT REPEAT 373..427
FT /note="2-2"
FT REGION 104..290
FT /note="3 X 37 AA repeats"
FT REGION 303..427
FT /note="2 X 55 AA repeats"
FT REGION 503..567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 531..555
FT /note="5 X 5 AA repeats of [DE]-D-A-K-K"
FT MOTIF 559..563
FT /note="LPXTG sorting signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT COMPBIAS 529..558
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 562
FT /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT HELIX 251..268
FT /evidence="ECO:0007829|PDB:1GJS"
FT HELIX 272..279
FT /evidence="ECO:0007829|PDB:1GJS"
FT HELIX 284..296
FT /evidence="ECO:0007829|PDB:1GJS"
FT STRAND 303..309
FT /evidence="ECO:0007829|PDB:3FIL"
FT STRAND 311..313
FT /evidence="ECO:0007829|PDB:2I2Y"
FT STRAND 314..320
FT /evidence="ECO:0007829|PDB:3FIL"
FT STRAND 321..323
FT /evidence="ECO:0007829|PDB:1FCL"
FT HELIX 324..337
FT /evidence="ECO:0007829|PDB:3FIL"
FT STRAND 343..347
FT /evidence="ECO:0007829|PDB:3FIL"
FT HELIX 348..350
FT /evidence="ECO:0007829|PDB:3FIL"
FT STRAND 352..356
FT /evidence="ECO:0007829|PDB:3FIL"
FT STRAND 373..379
FT /evidence="ECO:0007829|PDB:2ON8"
FT STRAND 384..390
FT /evidence="ECO:0007829|PDB:2ON8"
FT HELIX 394..407
FT /evidence="ECO:0007829|PDB:2ON8"
FT STRAND 413..417
FT /evidence="ECO:0007829|PDB:2ON8"
FT TURN 418..421
FT /evidence="ECO:0007829|PDB:2ON8"
FT STRAND 422..426
FT /evidence="ECO:0007829|PDB:2ON8"
FT STRAND 442..449
FT /evidence="ECO:0007829|PDB:6OC7"
FT STRAND 451..463
FT /evidence="ECO:0007829|PDB:6OC7"
FT HELIX 464..477
FT /evidence="ECO:0007829|PDB:6OC7"
FT STRAND 483..487
FT /evidence="ECO:0007829|PDB:6OC7"
FT TURN 488..491
FT /evidence="ECO:0007829|PDB:6OC7"
FT STRAND 492..496
FT /evidence="ECO:0007829|PDB:6OC7"
SQ SEQUENCE 593 AA; 63292 MW; 048BAA760D5B2920 CRC64;
MEKEKKVKYF LRKSAFGLAS VSAAFLVGST VFAVDSPIED TPIIRNGGEL TNLLGNSETT
LALRNEESAT ADLTAAAVAD TVAAAAAENA GAAAWEAAAA ADALAKAKAD ALKEFNKYGV
SDYYKNLINN AKTVEGVKDL QAQVVESAKK ARISEATDGL SDFLKSQTPA EDTVKSIELA
EAKVLANREL DKYGVSDYHK NLINNAKTVE GVKDLQAQVV ESAKKARISE ATDGLSDFLK
SQTPAEDTVK SIELAEAKVL ANRELDKYGV SDYYKNLINN AKTVEGVKAL IDEILAALPK
TDTYKLILNG KTLKGETTTE AVDAATAEKV FKQYANDNGV DGEWTYDDAT KTFTVTEKPE
VIDASELTPA VTTYKLVING KTLKGETTTE AVDAATAEKV FKQYANDNGV DGEWTYDDAT
KTFTVTEKPE VIDASELTPA VTTYKLVING KTLKGETTTK AVDAETAEKA FKQYANDNGV
DGVWTYDDAT KTFTVTEMVT EVPGDAPTEP EKPEASIPLV PLTPATPIAK DDAKKDDTKK
EDAKKPEAKK EDAKKAETLP TTGEGSNPFF TAAALAVMAG AGALAVASKR KED
