ARP4_STRPY
ID ARP4_STRPY Reviewed; 386 AA.
AC P13050;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=IgA receptor;
DE Flags: Precursor;
GN Name=arp4;
OS Streptococcus pyogenes.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1314;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=AW43 / Serotype M60;
RX PubMed=2691841; DOI=10.1111/j.1365-2958.1989.tb00261.x;
RA Frithz E., Heden L.-O., Lindahl G.;
RT "Extensive sequence homology between IgA receptor and M proteins in
RT Streptococcus pyogenes.";
RL Mol. Microbiol. 3:1111-1119(1989).
CC -!- FUNCTION: Binds IgA of both subclasses, and also binds polyclonal IgG
CC weakly.
CC -!- INTERACTION:
CC P13050; P04003: C4BPA; Xeno; NbExp=5; IntAct=EBI-978341, EBI-978348;
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; X15198; CAA33269.1; -; Genomic_DNA.
DR PIR; S05568; S05568.
DR AlphaFoldDB; P13050; -.
DR SMR; P13050; -.
DR IntAct; P13050; 1.
DR GO; GO:0005576; C:extracellular region; 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; 3.
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; Peptidoglycan-anchor; Receptor; Repeat; Secreted; Signal.
FT SIGNAL 1..41
FT CHAIN 42..356
FT /note="IgA receptor"
FT /id="PRO_0000005591"
FT PROPEP 357..386
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT /id="PRO_0000005592"
FT REPEAT 153..187
FT /note="C-1"
FT REPEAT 188..229
FT /note="C-2"
FT REPEAT 230..271
FT /note="C-3"
FT REGION 42..152
FT /note="IgA-binding"
FT /evidence="ECO:0000255"
FT REGION 79..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 153..271
FT /note="3 X tandem repeats"
FT REGION 233..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 323..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 353..357
FT /note="LPXTG sorting signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT COMPBIAS 79..170
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..221
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..360
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 356
FT /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
SQ SEQUENCE 386 AA; 43837 MW; C5FBDCDBB97BA0B8 CRC64;
MARKDTNKQY SLRKLKTGTA SVAVAVAVLG AGFANQTEVK AAEIKKPQAD SAWNWPKEYN
ALLKENEELK VEREKYLSYA DDKEKDPQYR ALMGENQDLR KREGQYQDKI EELEKERKEK
QERQEQLERQ YQIEADKHYQ EQQKKHQQEQ QQLEAEKQKL AKDKQISDAS RQGLSRDLEA
SRAAKKELEA EHQKLKEEKQ ISDASRQGLS RDLEASREAK KKVEADLAAL TAEHQKLKED
KQISDASRQG LSRDLEASRE AKKKVEADLA EANSKLQALE KLNKELEEGK KLSEKEKAEL
QARLEAEAKA LKEQLAKQAE ELAKLKGNQT PNAKVAPQAN RSRSAMTQQK RTLPSTGETA
NPFFTAAAAT VMVSAGMLAL KRKEEN