ID   YSC6_STRGC              Reviewed;         564 AA.
AC   P42359;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Putative zinc metalloproteinase in scaA 5'region;
DE            EC=3.4.24.-;
DE   AltName: Full=ORF6;
DE   Flags: Fragment;
OS   Streptococcus gordonii (strain Challis / ATCC 35105 / BCRC 15272 / CH1 /
OS   DL1 / V288).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=467705;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 51656 / PK488;
RX   PubMed=7927711; DOI=10.1128/iai.62.10.4469-4480.1994;
RA   Kolenbrander P.E., Andersen R.N., Ganeshkumar N.;
RT   "Nucleotide sequence of the Streptococcus gordonii PK488 coaggregation
RT   adhesin gene, scaA, and ATP-binding cassette.";
RL   Infect. Immun. 62:4469-4480(1994).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the peptidase M13 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01233, ECO:0000305}.
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DR   EMBL; L11577; AAA71944.1; -; Genomic_DNA.
DR   PIR; T11548; T11548.
DR   AlphaFoldDB; P42359; -.
DR   SMR; P42359; -.
DR   STRING; 467705.SGO_1799; -.
DR   MEROPS; M13.005; -.
DR   eggNOG; COG3590; Bacteria.
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   CDD; cd08662; M13; 1.
DR   Gene3D; 1.10.1380.10; -; 1.
DR   Gene3D; 3.40.390.10; -; 1.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR000718; Peptidase_M13.
DR   InterPro; IPR018497; Peptidase_M13_C.
DR   InterPro; IPR042089; Peptidase_M13_dom_2.
DR   InterPro; IPR008753; Peptidase_M13_N.
DR   PANTHER; PTHR11733; PTHR11733; 1.
DR   Pfam; PF01431; Peptidase_M13; 1.
DR   Pfam; PF05649; Peptidase_M13_N; 1.
DR   PRINTS; PR00786; NEPRILYSIN.
DR   PROSITE; PS51885; NEPRILYSIN; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Metalloprotease; Protease; Zinc.
FT   CHAIN           1..>564
FT                   /note="Putative zinc metalloproteinase in scaA 5'region"
FT                   /id="PRO_0000078233"
FT   DOMAIN          1..>564
FT                   /note="Peptidase M13"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT   ACT_SITE        479
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01233,
FT                   ECO:0000255|PROSITE-ProRule:PRU10095"
FT   ACT_SITE        542
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT   BINDING         478
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01233,
FT                   ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         482
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01233,
FT                   ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         538
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT   NON_TER         564
SQ   SEQUENCE   564 AA;  63706 MW;  64FF4E1C0E7C877E CRC64;
     MTRLQDDFYD AINGEWAKTA VIPDDKPVTG GFMDLAEEIE DLMLSTTDKW LAGDGVPEDA
     ILQNFVAYHR LAADYDKREA AGTEPARAYI DEIRNLASFE EYASKIADFE LAGKPTYFPF
     GVAPDFMDAR INVLWADGPG TILPDTTYYA EDHPQKADLL AKWRKAQEDL LAKFDFTEEE
     IKDLLDKVLD LDAVFAQYVL SNEESSEYAK LYHPYKWDDF KALVPELPLT DIFTKLIGQE
     PDQVIVPEER FWKAAKDIYT AANWDKLHAL LILSAVRNTT PYLTDDIRVL AGAYQRALSG
     TPQAQDKKKA AYYLAQGPFN QAIGLWYAGQ KFSPEAKADV EQKVVTMIEV YKNRLAQNDW
     LTPETRDKAI VKLNVIKPYI GYPDELPERY SRKIVDENLT LFENAQKLSL IDIAYSWSKW
     NQPVDYKEWG MPAHMVNAYY NPQKNLIVFP AAILQAPFYD LHQSSSANYG GIGAVIAHEI
     SHAFDTNGAS FDENGSLNNW WTEHDYQAFT ERTQKVIDQF EGQDSYGAKV NGKLTVSENV
     ADLGGIAAAL EAAKKEADFS AEEF