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M24_STRPY
ID   M24_STRPY               Reviewed;         539 AA.
AC   P12379;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   25-MAY-2022, entry version 92.
DE   RecName: Full=M protein, serotype 24;
DE   Flags: Precursor;
GN   Name=emm24;
OS   Streptococcus pyogenes.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1314;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Vaughn / Serotype M24;
RX   PubMed=3276665; DOI=10.1128/jb.170.2.676-684.1988;
RA   Mouw A.R., Beachey E.H., Burdett V.;
RT   "Molecular evolution of streptococcal M protein: cloning and nucleotide
RT   sequence of the type 24 M protein gene and relation to other genes of
RT   Streptococcus pyogenes.";
RL   J. Bacteriol. 170:676-684(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 30-89.
RC   STRAIN=Serotype M24;
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).
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; M19031; AAA26874.1; -; Genomic_DNA.
DR   PIR; A28549; A28549.
DR   AlphaFoldDB; P12379; -.
DR   SMR; P12379; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0006909; P:phagocytosis; 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; 2.
DR   Pfam; PF04650; YSIRK_signal; 1.
DR   PRINTS; PR00015; GPOSANCHOR.
DR   TIGRFAMs; TIGR01168; YSIRK_signal; 1.
DR   PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
PE   3: Inferred from homology;
KW   Cell wall; Coiled coil; Peptidoglycan-anchor; Phagocytosis; Repeat;
KW   Secreted; Signal; Virulence.
FT   SIGNAL          1..42
FT                   /evidence="ECO:0000255"
FT   CHAIN           43..508
FT                   /note="M protein, serotype 24"
FT                   /id="PRO_0000005623"
FT   PROPEP          509..539
FT                   /note="Removed by sortase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT                   /id="PRO_0000005624"
FT   REPEAT          118..152
FT                   /note="A-1"
FT   REPEAT          153..187
FT                   /note="A-2"
FT   REPEAT          188..222
FT                   /note="A-3"
FT   REPEAT          223..257
FT                   /note="A-4"
FT   REPEAT          258..292
FT                   /note="A-5"
FT   REPEAT          293..301
FT                   /note="A-6; truncated"
FT   REPEAT          311..355
FT                   /note="B-1"
FT   REPEAT          356..380
FT                   /note="B-2"
FT   REPEAT          381..405
FT                   /note="B-3; truncated"
FT   REGION          118..301
FT                   /note="5.3 X 35 AA tandem repeats, A-type"
FT   REGION          297..401
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          311..405
FT                   /note="2.7 X 35 AA tandem repeats, B-type"
FT   REGION          456..511
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           505..509
FT                   /note="LPXTG sorting signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT   COMPBIAS        315..401
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        486..511
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         508
FT                   /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
SQ   SEQUENCE   539 AA;  58804 MW;  B03EDF3AC1E6E9C7 CRC64;
     MTKNNTNRHY SLRKLKTGTA SVAVALTVLG AGLVVNTNEV SAVATRSQTD TLEKVQERAD
     KFEIENNTLK LKNSDLSFNN KALKDHNDEL TEELSNAKEK LRKNDKSLSE KASKIQELEA
     RKADLEKALE GAMNFSTADS AKIKTLEAEK AALAARKADL EKALEGAMNF STADSAKIKT
     LEAEKAALEA RQAELEKALE GAMNFSTADS AKIKTLEAEK AALAARKADL EKALEGAMNF
     STADSAKIKT LEAEKAALEA RQAELEKALE GAMNFSTADS AKIKTLEAEK AALEAEKADL
     EHQSQVLNAN RQSLRRDLDA SREAKKQLEA EHQKLEEQNK ISEASRQSLR RDLDASREAK
     KQLEAEHQKL EEQNKISEAS RQSLRRDLDA SREAKKQVEK ALEEANSKLA ALEKLNKELE
     ESKKLTEKEK AELQAKLEAE AKALKEKLAK QAEELAKLRA GKASDSQTPD AKPGNKAVPG
     KGQAPQAGTK PNQNKAPMKE TKRQLPSTGE TANPFFTAAA LTVMATAGVA AVVKRKEEN
 
 
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