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Database: UniProt
Entry: A0A1H5JDQ7_9ACTN
LinkDB: A0A1H5JDQ7_9ACTN
Original site: A0A1H5JDQ7_9ACTN 
ID   A0A1H5JDQ7_9ACTN        Unreviewed;       551 AA.
AC   A0A1H5JDQ7;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=Neutral metalloproteinase {ECO:0000256|RuleBase:RU366073};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU366073};
GN   ORFNames=SAMN05216489_06885 {ECO:0000313|EMBL:SEE50683.1};
OS   Streptomyces sp. 3213.3.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1855348 {ECO:0000313|EMBL:SEE50683.1, ECO:0000313|Proteomes:UP000198754};
RN   [1] {ECO:0000313|EMBL:SEE50683.1, ECO:0000313|Proteomes:UP000198754}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3213 {ECO:0000313|EMBL:SEE50683.1,
RC   ECO:0000313|Proteomes:UP000198754};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FNTK01000001; SEE50683.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H5JDQ7; -.
DR   STRING; 1855348.SAMN05216489_06885; -.
DR   Proteomes; UP000198754; 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; 3.10.450.40; -; 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   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.
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   Reference proteome {ECO:0000313|Proteomes:UP000198754};
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..551
FT                   /note="Neutral metalloproteinase"
FT                   /evidence="ECO:0000256|RuleBase:RU366073"
FT                   /id="PRO_5023144174"
FT   DOMAIN          82..128
FT                   /note="FTP"
FT                   /evidence="ECO:0000259|Pfam:PF07504"
FT   DOMAIN          223..372
FT                   /note="Peptidase M4"
FT                   /evidence="ECO:0000259|Pfam:PF01447"
FT   DOMAIN          376..550
FT                   /note="Peptidase M4 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02868"
FT   ACT_SITE        366
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT   ACT_SITE        453
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ   SEQUENCE   551 AA;  56672 MW;  4EC25339B13BD2F1 CRC64;
     MTPLYARHKR TTLAIATAVA AGALLATGVT TGASAQPATG KAAPLAAAPQ LLSNAARTAL
     VKEKQADAAE TATQIGLGTK EKLVVKDVVK DVDGTVHTRY ERTYAGLPVL GGDLVVHTSP
     AGKTEGVTKA HSAAIKVATV TPKITVAKAE KQALTAAKAA GSDKTAADGA RKVIWAGGAT
     PVLAYETVVG GLQDDGTPNQ LHVITDAATG KKLFEYQGIE NATGTGKTLY SGTVSLTTTL
     SGTTYSLTDA SRGSHKTYNL KHGTSGTGTL FTNTTNTWGT GAASSSSTDV TAAADAAYGA
     QETWDFYKDT FGRSGIKNNG VGAYSRVHYG SSYVNAFWDD SCFCMTYGDG SGNTHPLTSL
     DVAGHEMSHG VTANTAGLNY SGESGGLNEA TSDIFGTGVE FYANNSSDPG DYLIGEKIDI
     NGDGSPLRYM DQPSKDGGSA NYWSSSVGNL DVHYSSGVAN HFFYLLSEGS GAKTINGVSY
     NSPTYNGSTV TGIGRAKALQ IWYKALTTYF TSTTKYAGAR TGTLSAAAAL YGSGSTEYNA
     VAAAWSAVNV S
//
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