Y2031_STRP8
ID Y2031_STRP8 Reviewed; 419 AA.
AC Q8NZB3;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Putative zinc metalloprotease spyM18_2031;
DE EC=3.4.24.-;
GN OrderedLocusNames=spyM18_2031;
OS Streptococcus pyogenes serotype M18 (strain MGAS8232).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=186103;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGAS8232;
RX PubMed=11917108; DOI=10.1073/pnas.062526099;
RA Smoot J.C., Barbian K.D., Van Gompel J.J., Smoot L.M., Chaussee M.S.,
RA Sylva G.L., Sturdevant D.E., Ricklefs S.M., Porcella S.F., Parkins L.D.,
RA Beres S.B., Campbell D.S., Smith T.M., Zhang Q., Kapur V., Daly J.A.,
RA Veasy L.G., Musser J.M.;
RT "Genome sequence and comparative microarray analysis of serotype M18 group
RT A Streptococcus strains associated with acute rheumatic fever outbreaks.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:4668-4673(2002).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase M50B family. {ECO:0000305}.
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DR EMBL; AE009949; AAL98508.1; -; Genomic_DNA.
DR RefSeq; WP_011018245.1; NC_003485.1.
DR AlphaFoldDB; Q8NZB3; -.
DR SMR; Q8NZB3; -.
DR KEGG; spm:spyM18_2031; -.
DR HOGENOM; CLU_025778_1_0_9; -.
DR OMA; QYMVGFG; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR004387; Pept_M50_Zn.
DR InterPro; IPR008915; Peptidase_M50.
DR PANTHER; PTHR42837; PTHR42837; 1.
DR Pfam; PF13180; PDZ_2; 1.
DR Pfam; PF02163; Peptidase_M50; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR TIGRFAMs; TIGR00054; TIGR00054; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 3: Inferred from homology;
KW Cell membrane; Hydrolase; Membrane; Metal-binding; Metalloprotease;
KW Protease; Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..419
FT /note="Putative zinc metalloprotease spyM18_2031"
FT /id="PRO_0000088471"
FT TRANSMEM 169..191
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 301..323
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 343..365
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 392..411
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 175..274
FT /note="PDZ"
FT ACT_SITE 19
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 18
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 22
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ SEQUENCE 419 AA; 45719 MW; A66550CB3779548E CRC64;
MLGIITFIII FGILVIVHEF GHFYFAKKSG ILVREFAIGM GPKIFSHVDQ GGTLYTLRML
PLGGYVRMAG WGDDKTEIKT GTPASLTLNE QGFVKRINLS QSKLDPTSLP MHVTGYDLED
QLSITGLVLE ETKTYKVAHD ATIVEEDGTE IRIAPLDVQY QNASIGGRLI TNFAGPMNNF
ILGIVVFILL VFLQGGMPDF SSNHVRVQEN GAAAKAGLRD NDQIVAINGY KVTSWNDLTE
AVDLATRDLG PSQTIKVTYK SHQRLKTVAV KPQKHAKTYT IGVKASLKTG FKDKLLGGLE
LAWSGAFTIL NALKGLITGF SLNKLGGPVA MYDMSNQAAQ NGLESVLSLM AMLSINLGIF
NLIPIPALDG GKILMNIIEA IRRKPIKQET EAYITLAGVA IMVVLMIAVT WNDIMRVFF