ID M5_STRP5 Reviewed; 492 AA.
AC P02977;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 2.
DT 08-NOV-2023, entry version 101.
DE RecName: Full=M protein, serotype 5;
DE Flags: Precursor;
GN Name=emm5; Synonyms=smp5;
OS Streptococcus pyogenes serotype M5.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=301449;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3281944; DOI=10.1016/s0021-9258(18)60617-9;
RA Miller L., Gray L., Beachey E., Kehoe M.;
RT "Antigenic variation among group A streptococcal M proteins. Nucleotide
RT sequence of the serotype 5 M protein gene and its relationship with genes
RT encoding types 6 and 24 M proteins.";
RL J. Biol. Chem. 263:5668-5673(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 30-89.
RX PubMed=7891551; DOI=10.1111/j.1365-2958.1994.tb01301.x;
RA Whatmore A.M., Kapur V., Sullivan D.J., Musser J.M., Kehoe M.A.;
RT "Non-congruent relationships between variation in emm gene sequences and
RT the population genetic structure of group A streptococci.";
RL Mol. Microbiol. 14:619-631(1994).
RN [3]
RP PROTEIN SEQUENCE OF 43-212 AND 238-250.
RX PubMed=6368549; DOI=10.1016/s0021-9258(17)43150-4;
RA Manjula B.N., Acharya A.S., Mische S.M., Fairwell T., Fischetti V.A.;
RT "The complete amino acid sequence of a biologically active 197-residue
RT fragment of M protein isolated from type 5 group A streptococci.";
RL J. Biol. Chem. 259:3686-3693(1984).
CC -!- FUNCTION: This protein is one of the different antigenic serotypes of
CC protein M. Protein M is closely associated with virulence of the
CC bacterium and can render the organism resistant to phagocytosis.
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; M20374; AAA26976.1; -; Genomic_DNA.
DR PIR; A03501; MMSOMP.
DR PIR; A28616; A28616.
DR PDB; 2KK9; NMR; -; A=300-354.
DR PDBsum; 2KK9; -.
DR AlphaFoldDB; P02977; -.
DR SMR; P02977; -.
DR EvolutionaryTrace; P02977; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0006909; P:phagocytosis; IEA:UniProtKB-KW.
DR Gene3D; 6.10.250.460; -; 3.
DR InterPro; IPR019931; LPXTG_anchor.
DR InterPro; IPR019950; M_anchor.
DR InterPro; IPR003345; M_repeat.
DR InterPro; IPR005877; YSIRK_signal_dom.
DR NCBIfam; TIGR01167; LPXTG_anchor; 1.
DR NCBIfam; NF033777; M_group_A_cterm; 1.
DR NCBIfam; TIGR01168; YSIRK_signal; 1.
DR Pfam; PF00746; Gram_pos_anchor; 1.
DR Pfam; PF02370; M; 2.
DR PRINTS; PR00015; GPOSANCHOR.
DR PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
DR PROSITE; PS52028; SMCR; 3.
DR PROSITE; PS52030; SMDRR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell wall; Coiled coil; Direct protein sequencing;
KW Peptidoglycan-anchor; Phagocytosis; Repeat; Secreted; Signal; Virulence.
FT SIGNAL 1..42
FT /evidence="ECO:0000269|PubMed:6368549"
FT CHAIN 43..461
FT /note="M protein, serotype 5"
FT /id="PRO_0000005615"
FT PROPEP 462..492
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT /id="PRO_0000005616"
FT REPEAT 69..75
FT /note="1"
FT REPEAT 76..82
FT /note="2"
FT REPEAT 83..89
FT /note="3"
FT REPEAT 90..96
FT /note="4"
FT REPEAT 97..103
FT /note="5"
FT REPEAT 251..285
FT /note="C 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01372"
FT REPEAT 286..320
FT /note="C 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01372"
FT REPEAT 321..355
FT /note="C 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01372"
FT REPEAT 388..393
FT /note="D 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01374"
FT REPEAT 394..399
FT /note="D 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01374"
FT REPEAT 402..407
FT /note="D 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01374"
FT REPEAT 409..414
FT /note="D 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01374"
FT REGION 69..103
FT /note="5 X 7 AA tandem repeats of L-K-T-K-N-E-G"
FT REGION 71..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 235..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 408..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 458..462
FT /note="LPXTG sorting signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT COMPBIAS 71..123
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..354
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..464
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 461
FT /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT CONFLICT 43
FT /note="A -> T (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 50
FT /note="N -> S (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 102
FT /note="K -> SNLERKTAELTSEK (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 208
FT /note="I -> L (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 304..307
FT /evidence="ECO:0007829|PDB:2KK9"
FT HELIX 311..332
FT /evidence="ECO:0007829|PDB:2KK9"
FT STRAND 334..340
FT /evidence="ECO:0007829|PDB:2KK9"
FT STRAND 343..345
FT /evidence="ECO:0007829|PDB:2KK9"
FT TURN 346..349
FT /evidence="ECO:0007829|PDB:2KK9"
SQ SEQUENCE 492 AA; 55085 MW; 873779B6CBD55E27 CRC64;
MARENTNKHY WLRKLKKGTA SVAVALSVLG AGLVVNTNEV SAAVTRGTIN DPQRAKEALD
KYELENHDLK TKNEGLKTEN EGLKTENEGL KTENEGLKTE KKEHEAENDK LKQQRDTLST
QKETLEREVQ NTQYNNETLK IKNGDLTKEL NKTRQELANK QQESKENEKA LNELLEKTVK
DKIAKEQENK ETIGTLKKIL DETVKDKIAK EQENKETIGT LKKILDETVK DKLAKEQKSK
QNIGALKQEL AKKDEANKIS DASRKGLRRD LDASREAKKQ LEAEHQKLEE QNKISEASRK
GLRRDLDASR EAKKQLEAEQ QKLEEQNKIS EASRKGLRRD LDASREAKKQ VEKALEEANS
KLAALEKLNK ELEESKKLTE KEKAELQAKL EAEAKALKEQ LAKQAEELAK LRAGKASDSQ
TPDTKPGNKA VPGKGQAPQA GTKPNQNKAP MKETKRQLPS TGETANPFFT AAALTVMATA
GVAAVVKRKE EN
//
