SPH_STRP1
ID SPH_STRP1 Reviewed; 376 AA.
AC P50470;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=Immunoglobulin G-binding protein H;
DE Short=IgG-binding protein H;
DE Flags: Precursor;
OS Streptococcus pyogenes serotype M1.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=301447;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 42-51.
RC STRAIN=AP1 / 40/58 / Serotype M1;
RX PubMed=2332638;
RA Gomi H., Hozumi T., Hattori S., Tagawa C., Kishimoto F., Bjoerck L.;
RT "The gene sequence and some properties of protein H. A novel IgG-binding
RT protein.";
RL J. Immunol. 144:4046-4052(1990).
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|PROSITE-
CC ProRule:PRU00477}; Peptidoglycan-anchor {ECO:0000255|PROSITE-
CC ProRule:PRU00477}.
CC -!- SIMILARITY: Belongs to the M protein family. {ECO:0000305}.
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DR EMBL; M29398; AAA26963.1; -; Genomic_DNA.
DR PIR; A43528; A43528.
DR AlphaFoldDB; P50470; -.
DR SMR; P50470; -.
DR STRING; 1314.HKU360_01834; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0019864; F:IgG binding; IEA:UniProtKB-KW.
DR InterPro; IPR019931; LPXTG_anchor.
DR InterPro; IPR019950; M_anchor.
DR InterPro; IPR003345; M_repeat.
DR InterPro; IPR005877; YSIRK_signal_dom.
DR Pfam; PF00746; Gram_pos_anchor; 1.
DR Pfam; PF02370; M; 5.
DR Pfam; PF04650; YSIRK_signal; 1.
DR PRINTS; PR00015; GPOSANCHOR.
DR TIGRFAMs; TIGR01168; YSIRK_signal; 1.
DR PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
PE 1: Evidence at protein level;
KW Cell wall; Direct protein sequencing; IgG-binding protein;
KW Peptidoglycan-anchor; Repeat; Secreted; Signal.
FT SIGNAL 1..41
FT /evidence="ECO:0000269|PubMed:2332638"
FT CHAIN 42..345
FT /note="Immunoglobulin G-binding protein H"
FT /id="PRO_0000005661"
FT PROPEP 346..376
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT /id="PRO_0000005662"
FT REPEAT 159..199
FT /note="C-1"
FT REPEAT 200..241
FT /note="C-2"
FT REPEAT 242..283
FT /note="C-3"
FT REGION 69..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 159..283
FT /note="3 X repeats, type C"
FT REGION 292..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 342..346
FT /note="LPXTG sorting signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT COMPBIAS 69..149
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..207
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..249
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..271
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..348
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 345
FT /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
SQ SEQUENCE 376 AA; 42501 MW; F3BC76EBFDDFC317 CRC64;
MTRQQTKKNY SLRKLKTGTA SVAVALTVLG AGFANQTTVK AEGAKIDWQE EYKKLDEDNA
KLVEVVETTS LENEKLKSEN EENKKNLDKL SKENQGKLEK LELDYLKKLD HEHKEHQKEQ
QEQEERQKNQ EQLERKYQRE VEKRYQEQLQ KQQQLETEKQ ISEASRKSLS RDLEASRAAK
KDLEAEHQKL EAEHQKLKED KQISDASRQG LSRDLEASRA AKKELEANHQ KLEAEHQKLK
EDKQISDASR QGLSRDLEAS RAAKKELEAN HQKLEAEAKA LKEQLAKQAE ELAKLRAGKA
SDSQTPDTKP GNKAVPGKGQ APQAGTKPNQ NKAPMKETKR QLPSTGETAN PFFTAAALTV
MATAGVAAVV KRKEEN