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Database: UniProt
Entry: D6EEH2_STRLI
LinkDB: D6EEH2_STRLI
Original site: D6EEH2_STRLI 
ID   D6EEH2_STRLI            Unreviewed;       547 AA.
AC   D6EEH2;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   24-JAN-2024, entry version 62.
DE   RecName: Full=Neutral metalloproteinase {ECO:0000256|RuleBase:RU366073};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU366073};
GN   ORFNames=SSPG_05058 {ECO:0000313|EMBL:EFD69418.2};
OS   Streptomyces lividans TK24.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=457428 {ECO:0000313|EMBL:EFD69418.2};
RN   [1] {ECO:0000313|EMBL:EFD69418.2}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TK24 {ECO:0000313|EMBL:EFD69418.2};
RG   The Broad Institute Genome Sequencing Platform;
RG   Broad Institute Microbial Sequencing Center;
RA   Fischbach M., Godfrey P., Ward D., Young S., Kodira C.D., Zeng Q.,
RA   Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., Chen Z., Engels R.,
RA   Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D.I.,
RA   Hepburn T.A., Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D.,
RA   Pearson M., Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C.,
RA   Sykes S.N., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA   Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA   Galagan J., Nusbaum C., Birren B.;
RT   "The genome sequence of Streptomyces lividans strain TK24.";
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Extracellular zinc metalloprotease.
CC       {ECO:0000256|RuleBase:RU366073}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU366073};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|RuleBase:RU366073}.
CC   -!- SIMILARITY: Belongs to the peptidase M4 family.
CC       {ECO:0000256|ARBA:ARBA00009388, ECO:0000256|RuleBase:RU366073}.
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DR   EMBL; GG657756; EFD69418.2; -; Genomic_DNA.
DR   RefSeq; WP_003976330.1; NZ_GG657756.1.
DR   AlphaFoldDB; D6EEH2; -.
DR   SMR; D6EEH2; -.
DR   MEROPS; M04.017; -.
DR   HOGENOM; CLU_008590_5_1_11; -.
DR   Proteomes; UP000002769; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd09597; M4_TLP; 1.
DR   Gene3D; 3.10.170.10; -; 1.
DR   Gene3D; 3.10.450.490; -; 1.
DR   Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR   InterPro; IPR011096; FTP_domain.
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   InterPro; IPR006311; TAT_signal.
DR   PANTHER; PTHR33794; BACILLOLYSIN; 1.
DR   PANTHER; PTHR33794:SF1; BACILLOLYSIN; 1.
DR   Pfam; PF07504; FTP; 1.
DR   Pfam; PF01447; Peptidase_M4; 1.
DR   Pfam; PF02868; Peptidase_M4_C; 1.
DR   PRINTS; PR00730; THERMOLYSIN.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU366073};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW   ECO:0000256|RuleBase:RU366073};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU366073};
KW   Secreted {ECO:0000256|RuleBase:RU366073};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU366073};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU366073}.
FT   SIGNAL          1..35
FT                   /evidence="ECO:0000256|RuleBase:RU366073"
FT   CHAIN           36..547
FT                   /note="Neutral metalloproteinase"
FT                   /evidence="ECO:0000256|RuleBase:RU366073"
FT                   /id="PRO_5031677990"
FT   DOMAIN          67..108
FT                   /note="FTP"
FT                   /evidence="ECO:0000259|Pfam:PF07504"
FT   DOMAIN          211..368
FT                   /note="Peptidase M4"
FT                   /evidence="ECO:0000259|Pfam:PF01447"
FT   DOMAIN          371..546
FT                   /note="Peptidase M4 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02868"
FT   ACT_SITE        361
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT   ACT_SITE        449
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ   SEQUENCE   547 AA;  56812 MW;  C9A7380AE53D3F0A CRC64;
     MSRIPHVRGS RLALAGTAAT TATLLIAALA PGAAAAGRPT PATALDHAAA ALSEHAAALG
     LTDDQDTEVR DVIVDGDGTQ HVRYDRTYRE LPVLGGDFVV HLAPDGDFRG ADRATDTPLS
     LPTVVPKLSA PKAADLASNA LRAANPGELL KKLTARPELV VDALHGTPRL AWRTDAAALD
     SLGNPVARTV LTDAGTGARI DAWDTVESAS GDGKSLYGGT VPLETTPSGS SYRLEDPTRG
     GTYTGDAENR TDLCLLTVCL VRAPATPFTD ADNHWGTGAA DDRASAAVDA QYGTDATWDY
     YEDVHGRRGI AGDGKGSYNR VHYGTRYNNA FWDDGCFCMT YGDGDGSAFG PLVSLDVAGH
     EMSHGVTSKT AALTYSGEPG GLNEATSDIF GALVEWHADN SADPGDYLIG EKVVRDGFGR
     NALRYLDRPS RDGSSADCWS TSLGDLDVHY SSGVANHFAY LLAEGSGART VGGVAYDSPT
     CDGSTVSGIG RDKLGDIWYR ALTVYMTSST DYAGARAATL SAAGDLYGTG STEYAAVGAA
     WSAVSVG
//
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