ID   A0A1H9XDA9_9ACTN        Unreviewed;       799 AA.
AC   A0A1H9XDA9;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Zn-dependent metalloprotease {ECO:0000313|EMBL:SES43643.1};
GN   ORFNames=SAMN04487983_105426 {ECO:0000313|EMBL:SES43643.1};
OS   Streptomyces sp. yr375.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1761906 {ECO:0000313|EMBL:SES43643.1, ECO:0000313|Proteomes:UP000198568};
RN   [1] {ECO:0000313|EMBL:SES43643.1, ECO:0000313|Proteomes:UP000198568}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YR375 {ECO:0000313|EMBL:SES43643.1,
RC   ECO:0000313|Proteomes:UP000198568};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase M4 family.
CC       {ECO:0000256|ARBA:ARBA00009388}.
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DR   EMBL; FOFF01000054; SES43643.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H9XDA9; -.
DR   STRING; 1761906.SAMN04487983_105426; -.
DR   OrthoDB; 291295at2; -.
DR   Proteomes; UP000198568; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProt.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProt.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd09597; M4_TLP; 1.
DR   Gene3D; 3.10.170.10; -; 1.
DR   Gene3D; 3.10.450.40; -; 1.
DR   Gene3D; 3.10.450.490; -; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR   InterPro; IPR015919; Cadherin-like_sf.
DR   InterPro; IPR011096; FTP_domain.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR023612; Peptidase_M4.
DR   InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR   InterPro; IPR001570; Peptidase_M4_C_domain.
DR   InterPro; IPR013856; Peptidase_M4_domain.
DR   PANTHER; PTHR33794; BACILLOLYSIN; 1.
DR   PANTHER; PTHR33794:SF1; BACILLOLYSIN; 1.
DR   Pfam; PF07504; FTP; 1.
DR   Pfam; PF05345; He_PIG; 1.
DR   Pfam; PF01447; Peptidase_M4; 1.
DR   Pfam; PF02868; Peptidase_M4_C; 1.
DR   PRINTS; PR00730; THERMOLYSIN.
DR   SUPFAM; SSF49313; Cadherin-like; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW   ECO:0000313|EMBL:SES43643.1};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:SES43643.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198568};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   SIGNAL          1..33
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           34..799
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011560077"
FT   DOMAIN          82..118
FT                   /note="FTP"
FT                   /evidence="ECO:0000259|Pfam:PF07504"
FT   DOMAIN          225..372
FT                   /note="Peptidase M4"
FT                   /evidence="ECO:0000259|Pfam:PF01447"
FT   DOMAIN          375..549
FT                   /note="Peptidase M4 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02868"
FT   ACT_SITE        365
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT   ACT_SITE        452
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ   SEQUENCE   799 AA;  81633 MW;  689BACDF8D87E824 CRC64;
     MRPNPRKRTT VGAALLSSAA LLALGVQTVP ATALPAAPHP GPLRTGSLPA DLTPAQRTTL
     IKSAEARTTQ TADTLGLGAQ EKLVVKDVVK DNDGTVHTRY ERTYAGLPVL GGDLVVHTPP
     ASVAAGTVST TFNNNRRTVS VRSTTATYSK TAAESKALTA AKALDAKDPA AQSARKVIWA
     GEGTPKLAWE TVVSGLQDDG TPSKLHVITD AATGAKLSQY EGVETGTGNT QYSGTVSLST
     TLSGSTYQLY DTTRGGHKTY SLNNATSGTG TLMTDSDDVW GTGAGSNTQT AGADAAYGAQ
     ETWDFYKNTF GRSGIKNDGV AAYSRVHYSS AYVNAFWDDD CFCMTYGDGS GSTHALTSLD
     VAGHEMSHGV TSNTAGLDYT GESGGLNEAT SDIFGTGVEF YANNSSDVGD YLIGEKIDIN
     GDGTPLRYMD EPDKDGGSAD SWYSGVGNLD VHYSSGPANH MFYLLSEGSG SKTINGVTYN
     SPTSDGVAVA GIGRAAALQI WYKALTTYMT SSTNYAGART AALSAAAALY GSSSAQYAGV
     GNAFAGINVG SHITVPSTGV TVTNPGSQTA TVGTAVSLQL SASSTNSGTL TYAASGLPTG
     LSISSTGLIS GTPTTAGTYS TTVTVTDSTG ATGTAAFTWT VGSTGGGSCT VTQLLGNNGF
     ESGNTTWTAS SGVITNSSSQ AARTGSYKAW LDGYGSTHTD TLSQSVTIPS GCTNTTFTFY
     LHVDTAETST STQYDKLTVT AGSTTLATYS NLNAASGYVQ KSLSLGSYAG STVALKFSGV
     EDSSLQTSFV IDDTAVTTG
//