ID   Y263_STRPN              Reviewed;         419 AA.
AC   Q97SR2;
DT   15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Putative zinc metalloprotease SP_0263;
DE            EC=3.4.24.-;
GN   OrderedLocusNames=SP_0263;
OS   Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=170187;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-334 / TIGR4;
RX   PubMed=11463916; DOI=10.1126/science.1061217;
RA   Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA   Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA   Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA   Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA   Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA   McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA   Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA   Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT   "Complete genome sequence of a virulent isolate of Streptococcus
RT   pneumoniae.";
RL   Science 293:498-506(2001).
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; AE005672; AAK74441.1; -; Genomic_DNA.
DR   PIR; H95030; H95030.
DR   RefSeq; WP_000900658.1; NZ_AKVY01000001.1.
DR   AlphaFoldDB; Q97SR2; -.
DR   SMR; Q97SR2; -.
DR   STRING; 170187.SP_0263; -.
DR   EnsemblBacteria; AAK74441; AAK74441; SP_0263.
DR   KEGG; spn:SP_0263; -.
DR   eggNOG; COG0750; Bacteria.
DR   OMA; QYMVGFG; -.
DR   PhylomeDB; Q97SR2; -.
DR   BioCyc; SPNE170187:G1FZB-270-MON; -.
DR   Proteomes; UP000000585; 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; IPR036034; PDZ_sf.
DR   InterPro; IPR004387; Pept_M50_Zn.
DR   InterPro; IPR008915; Peptidase_M50.
DR   PANTHER; PTHR42837; PTHR42837; 1.
DR   Pfam; PF02163; Peptidase_M50; 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 SP_0263"
FT                   /id="PRO_0000088466"
FT   TRANSMEM        169..191
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        345..367
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        388..410
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
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;  45894 MW;  07412BF2F1B41CE1 CRC64;
     MLGILTFILV FGIIVVVHEF GHFYFAKKSG ILVREFAIGM GPKIFAHIGK DGTAYTIRIL
     PLGGYVRMAG WGDDTTEIKT GTPVSLTLAD DGKVKRINLS GKKLDQTALP MQVTQFDFED
     KLFIKGLVLE EEKTFAVDHD ATVVEADGTE VRIAPLDVQY QNATIWGKLI TNFAGPMNNF
     ILGVVVFWVL IFMQGGVRDV DTNQFHIMPQ GALAKVGVPE MAQITKIGSH EVSNWESLIQ
     AVETETKDKT APTLDVTISE KGSDKQVTVT PKDSQGRYLL GVQPGVKSDF LSMFVGGFTT
     AADSALRILS ALKNLIFQPD LNKLGGPVAI FKASSDAAKN GIENILYFLA MISINIGIFN
     LIPIPALDGG KIVLNILEAI RRKPLKQEIE TYVTLAGVVI MVVLMIAVTW NDIMRLFFR