Y1682_STRP6
ID Y1682_STRP6 Reviewed; 419 AA.
AC Q5X9U6;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Putative zinc metalloprotease M6_Spy1682;
DE EC=3.4.24.-;
GN OrderedLocusNames=M6_Spy1682;
OS Streptococcus pyogenes serotype M6 (strain ATCC BAA-946 / MGAS10394).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=286636;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-946 / MGAS10394;
RX PubMed=15272401; DOI=10.1086/422697;
RA Banks D.J., Porcella S.F., Barbian K.D., Beres S.B., Philips L.E.,
RA Voyich J.M., DeLeo F.R., Martin J.M., Somerville G.A., Musser J.M.;
RT "Progress toward characterization of the group A Streptococcus metagenome:
RT complete genome sequence of a macrolide-resistant serotype M6 strain.";
RL J. Infect. Dis. 190:727-738(2004).
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; CP000003; AAT87817.1; -; Genomic_DNA.
DR RefSeq; WP_011184987.1; NC_006086.1.
DR AlphaFoldDB; Q5X9U6; -.
DR SMR; Q5X9U6; -.
DR EnsemblBacteria; AAT87817; AAT87817; M6_Spy1682.
DR KEGG; spa:M6_Spy1682; -.
DR HOGENOM; CLU_025778_1_0_9; -.
DR OMA; QYMVGFG; -.
DR Proteomes; UP000001167; Chromosome.
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 M6_Spy1682"
FT /id="PRO_0000088470"
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; 45620 MW; 3944087416275A75 CRC64;
MLGIITFIII FGILVIVHEF GHFYFAKKSG ILVREFAIGM GPKIFSHVDQ GGTLYTLRML
PLGGYVRMAG WGDDKTEIKT GTPASLTLNE QGFVKRINLS QSKLDPTSLP MHVTGYDLED
QLSITGLVLE ETKTYKVAHD ATIVEEDGTE IRIAPLDVQY QNASIGGRLI TNFAGPMNNF
ILGIVVFILL VFLQGGMPDF SSNHVGVQEN GAAAKAGLRD NDQIVAINGY KVTSWNDLTE
AVDLATRDLG PSQTIKVTYK SHQRLKTVAV KPQKHAKTYT IGVKASLKTG FKDKLLGGLE
LAWSGAFTIL NALKGLITGF SLNKLGGPVA MYDMSNQAAQ NGLESVLSLM AMLSINLGIF
NLIPIPALDG GKILMNIIEA IRRKPIKQET EAYITLAGVA IMVVLMIAVT WNDIMRVFF