GenomeNet

Database: UniProt
Entry: A0A0U3QEH9_9ACTN
LinkDB: A0A0U3QEH9_9ACTN
Original site: A0A0U3QEH9_9ACTN 
ID   A0A0U3QEH9_9ACTN        Unreviewed;       597 AA.
AC   A0A0U3QEH9;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=Neutral metalloproteinase {ECO:0000256|RuleBase:RU366073};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU366073};
GN   ORFNames=AS200_40875 {ECO:0000313|EMBL:ALV37725.1};
OS   Streptomyces sp. CdTB01.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1725411 {ECO:0000313|EMBL:ALV37725.1, ECO:0000313|Proteomes:UP000068029};
RN   [1] {ECO:0000313|EMBL:ALV37725.1, ECO:0000313|Proteomes:UP000068029}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CdTB01 {ECO:0000313|EMBL:ALV37725.1,
RC   ECO:0000313|Proteomes:UP000068029};
RA   Tian Y., Zhou G., Yang H., Lu X.;
RT   "Complete genome sequence of the Streptomyces sp. strain CdTB01, a
RT   bacterium tolerant to cadmium.";
RL   Submitted (DEC-2015) 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP013743; ALV37725.1; -; Genomic_DNA.
DR   RefSeq; WP_058927305.1; NZ_CP013743.1.
DR   AlphaFoldDB; A0A0U3QEH9; -.
DR   STRING; 1725411.AS200_40875; -.
DR   KEGG; scx:AS200_40875; -.
DR   OrthoDB; 291295at2; -.
DR   Proteomes; UP000068029; Chromosome.
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   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   Cell projection {ECO:0000313|EMBL:ALV37725.1};
KW   Cilium {ECO:0000313|EMBL:ALV37725.1};
KW   Flagellum {ECO:0000313|EMBL:ALV37725.1};
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:UP000068029};
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..28
FT                   /evidence="ECO:0000256|RuleBase:RU366073"
FT   CHAIN           29..597
FT                   /note="Neutral metalloproteinase"
FT                   /evidence="ECO:0000256|RuleBase:RU366073"
FT                   /id="PRO_5023076965"
FT   DOMAIN          68..107
FT                   /note="FTP"
FT                   /evidence="ECO:0000259|Pfam:PF07504"
FT   DOMAIN          249..400
FT                   /note="Peptidase M4"
FT                   /evidence="ECO:0000259|Pfam:PF01447"
FT   DOMAIN          419..587
FT                   /note="Peptidase M4 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02868"
FT   ACT_SITE        394
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT   ACT_SITE        490
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ   SEQUENCE   597 AA;  62414 MW;  8F76D86EBAC9DF08 CRC64;
     MRRPHIRSVA VAVAVTTAAT GLAGTAFAGP DTGTHATAAD ASASAVVKAA ESAAFAHASA
     TGVSHGDGLQ AQDVMIDPEG ARHVRFTRTH QGLPVLGGDL VVHLTRQLSY AGVTRAADHA
     VKAAPASGAK LSAAEAEQKA ASVAKGDAGP AELVVDARDG ASALAYRVSV SDSTTTQGAG
     SRTVVVDAVS GKVRSNLPDN DEFLSPKLLD TLRERGETSA PVTGTGARSA GLLAGSAAAA
     TRYPVTANGT GKSLFVGKVP LKTTQTARTT FQLKDPTRYG SETRDAKGSY TESFGSGTKI
     TTKNDVFGNG ATTSRNSAAA DAQYGITKTL DFYKKTFGRK GIANNSKPAK AMVHWGKKVA
     NAFWDSDCGC MLYGDGDGDM FKKPLVALDV TGHELTHGVV DATAKLEPTR MDGQGNQYGE
     PGSLNESLAD IFASNVEFAT NNATDKPDYL IGEKMGLAQK FLRRLDHPSL DKLEGTIDYW
     APEVYDAEVH AGSGVSSHAY YLLAEGSGQK TIGGVKYDSP TFDGSTVKGI GRTKATAIYY
     RALTRYMVST TDFHDARVAT LKAAQDLYGA NSVEYRTVDQ SWAAVNVTEA NTPADRH
//
DBGET integrated database retrieval system