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 24-JAN-2024, entry version 163. 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; Bacillota; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 PDB; 8DIJ; NMR; -; A=302-357. DR PDB; 8TFR; X-ray; 2.99 A; C=437-497. 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 PDBsum; 8DIJ; -. DR PDBsum; 8TFR; -. 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 Gene3D; 3.10.20.10; -; 3. DR Gene3D; 1.10.8.40; Albumin-binding domain; 3. 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 NCBIfam; TIGR01167; LPXTG_anchor; 1. DR NCBIfam; TIGR01168; YSIRK_signal; 1. 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; Bacterial immunoglobulin/albumin-binding domains; 3. DR SUPFAM; SSF54358; Immunoglobulin-binding domains; 3. 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 //