PAM_STRPY
ID PAM_STRPY Reviewed; 388 AA.
AC P49054;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=Plasminogen-binding group A streptococcal M-like protein PAM;
DE Flags: Precursor; Fragment;
GN Name=pam; Synonyms=emm;
OS Streptococcus pyogenes.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1314;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 32-41.
RC STRAIN=AP53 / Serotype M53;
RX PubMed=8244975; DOI=10.1016/s0021-9258(19)74408-1;
RA Berge A., Sjoebring U.;
RT "PAM, a novel plasminogen-binding protein from Streptococcus pyogenes.";
RL J. Biol. Chem. 268:25417-25424(1993).
RN [2]
RP CHARACTERIZATION OF PLASMINOGEN BINDING, AND MUTAGENESIS.
RC STRAIN=AP53 / Serotype M53;
RX PubMed=8748039; DOI=10.1111/j.1365-2958.1995.mmi_18030569.x;
RA Carlsson Wistedt A., Ringdahl U., Mueller-Esterl W., Sjoebring U.;
RT "Identification of a plasminogen-binding motif in PAM, a bacterial surface
RT protein.";
RL Mol. Microbiol. 18:569-578(1995).
CC -!- FUNCTION: Binds to human plasminogen (and plasmin) via its kringle
CC repeats. Also binds to albumin, immunoglobulin G and fibrinogen. Could
CC provide the bacteria with a mechanism for invasion, as streptococcal-
CC bound plasmin could permit tissue penetration.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|PROSITE-
CC ProRule:PRU00477}; Peptidoglycan-anchor {ECO:0000255|PROSITE-
CC ProRule:PRU00477}.
CC -!- MISCELLANEOUS: PAM has more than one binding site for plasminogen; it
CC is thought that each of the a-repeats can bind one plasminogen
CC molecule.
CC -!- SIMILARITY: Belongs to the M protein family. {ECO:0000305}.
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DR EMBL; Z22219; CAA80222.1; -; Genomic_DNA.
DR PIR; A49545; A49545.
DR PDB; 1I5K; X-ray; 2.70 A; C/D=85-113.
DR PDB; 2DOH; X-ray; 2.30 A; C=85-113.
DR PDB; 2DOI; X-ray; 3.10 A; B/C=85-113.
DR PDB; 6OG4; X-ray; 1.70 A; C=76-150.
DR PDB; 6OKW; NMR; -; A=85-133.
DR PDB; 6OKX; NMR; -; A=85-133.
DR PDB; 6OKY; NMR; -; A=85-133.
DR PDB; 6OQ9; NMR; -; A=85-133.
DR PDB; 6OQJ; NMR; -; B=85-133.
DR PDB; 6OQK; NMR; -; B=85-133.
DR PDBsum; 1I5K; -.
DR PDBsum; 2DOH; -.
DR PDBsum; 2DOI; -.
DR PDBsum; 6OG4; -.
DR PDBsum; 6OKW; -.
DR PDBsum; 6OKX; -.
DR PDBsum; 6OKY; -.
DR PDBsum; 6OQ9; -.
DR PDBsum; 6OQJ; -.
DR PDBsum; 6OQK; -.
DR AlphaFoldDB; P49054; -.
DR BMRB; P49054; -.
DR SMR; P49054; -.
DR EvolutionaryTrace; P49054; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0031639; P:plasminogen activation; IDA:CACAO.
DR InterPro; IPR021965; Plasminogen_ligand_VEK-30.
DR InterPro; IPR005877; YSIRK_signal_dom.
DR Pfam; PF12107; VEK-30; 2.
DR TIGRFAMs; TIGR01168; YSIRK_signal; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell wall; Direct protein sequencing; Peptidoglycan-anchor;
KW Repeat; Secreted; Signal.
FT SIGNAL <1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..384
FT /note="Plasminogen-binding group A streptococcal M-like
FT protein PAM"
FT /id="PRO_0000005647"
FT PROPEP 385..>388
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT /id="PRO_0000005648"
FT REPEAT 91..103
FT /note="A-1"
FT REPEAT 104..116
FT /note="A-2"
FT REPEAT 147..153
FT /note="B-1"
FT REPEAT 154..161
FT /note="B-2"
FT REPEAT 163..204
FT /note="C-1"
FT REPEAT 205..246
FT /note="C-2"
FT REPEAT 247..278
FT /note="C-3; truncated"
FT REGION 85..113
FT /note="Able to bind plasminogen"
FT REGION 91..116
FT /note="2 X approximate tandem repeats, type a"
FT REGION 95..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 147..161
FT /note="2 X tandem repeats, type b"
FT REGION 163..278
FT /note="3 X tandem repeats, type c"
FT REGION 204..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 248..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 331..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 381..385
FT /note="LPXTG sorting signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT COMPBIAS 362..388
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 384
FT /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT MUTAGEN 82
FT /note="K->A: No change in plasminogen binding."
FT /evidence="ECO:0000269|PubMed:8748039"
FT MUTAGEN 98
FT /note="K->A: 50-fold decrease in plasminogen binding."
FT /evidence="ECO:0000269|PubMed:8748039"
FT MUTAGEN 111
FT /note="K->A: 2-fold decrease in plasminogen binding."
FT /evidence="ECO:0000269|PubMed:8748039"
FT NON_TER 1
FT NON_TER 388
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:6OKY"
FT HELIX 90..121
FT /evidence="ECO:0007829|PDB:6OG4"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:6OKX"
FT TURN 130..133
FT /evidence="ECO:0007829|PDB:6OKY"
SQ SEQUENCE 388 AA; 43629 MW; EEEC4FD962CCDB12 CRC64;
RKLKTGTASV AVALTVVGAG LASQTEVKAN RADDARNEVL RGNLVRAELW YRQIQENDQL
KLENKGLKTD LREKEEELQG LKDDVEKLTA DAELQRLKNE RHEEAELERL KSERHDHDKK
EAERKALEDK LADKQEHLNG ALRYINEKEA EAKEKEAEQK KLKEEKQISD ASRQGLRRDL
DASREAKKQV EKDLANLTAE LDKVKEEKQI SDASRQGLRR DLDASREAKK QVEKGLANLT
AELDKVKEEK QISDASRQGL RRDLDASREA KKQVEKALEE ANSKLAALEK LNKELEESKK
LTEKEKAELQ AKLEAEAKAL KEQLAKQAEE LAKLRAEKAS DSQTPDAKPG NKAVPGKGQA
PQAGTKPNQN KAPMKETKRQ LPSTGETT
