GenomeNet

Database: UniProt
Entry: A0A0U3PNY1_9ACTN
LinkDB: A0A0U3PNY1_9ACTN
Original site: A0A0U3PNY1_9ACTN 
ID   A0A0U3PNY1_9ACTN        Unreviewed;       673 AA.
AC   A0A0U3PNY1;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=Neutral metalloproteinase {ECO:0000256|RuleBase:RU366073};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU366073};
GN   ORFNames=AS200_16245 {ECO:0000313|EMBL:ALV33413.1};
OS   Streptomyces sp. CdTB01.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1725411 {ECO:0000313|EMBL:ALV33413.1, ECO:0000313|Proteomes:UP000068029};
RN   [1] {ECO:0000313|EMBL:ALV33413.1, ECO:0000313|Proteomes:UP000068029}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CdTB01 {ECO:0000313|EMBL:ALV33413.1,
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; ALV33413.1; -; Genomic_DNA.
DR   RefSeq; WP_058923078.1; NZ_CP013743.1.
DR   AlphaFoldDB; A0A0U3PNY1; -.
DR   STRING; 1725411.AS200_16245; -.
DR   KEGG; scx:AS200_16245; -.
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:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
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; 1.10.390.10; Neutral Protease Domain 2; 1.
DR   InterPro; IPR011096; FTP_domain.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR002884; P_dom.
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; PF01483; P_proprotein; 1.
DR   Pfam; PF01447; Peptidase_M4; 1.
DR   Pfam; PF02868; Peptidase_M4_C; 1.
DR   PRINTS; PR00730; THERMOLYSIN.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   PROSITE; PS51829; P_HOMO_B; 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   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..34
FT                   /evidence="ECO:0000256|RuleBase:RU366073"
FT   CHAIN           35..673
FT                   /note="Neutral metalloproteinase"
FT                   /evidence="ECO:0000256|RuleBase:RU366073"
FT                   /id="PRO_5023109920"
FT   DOMAIN          555..673
FT                   /note="P/Homo B"
FT                   /evidence="ECO:0000259|PROSITE:PS51829"
FT   ACT_SITE        363
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT   ACT_SITE        450
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ   SEQUENCE   673 AA;  69892 MW;  345C7D3E4CCED4DC CRC64;
     MRSSSSRRRT SHTLAIAGVT ALLAAAVQTG AASAAPEQTS AKGNPAHAAV KLSPSQRAEL
     LRDADTARSQ TARDIGLGAK EKLVARDVVK DADGTLHTRY ERTYAGLPVL GGDLVVDTAK
     SGATQRVIKA TNAAIKVSDV TPDITRAAAE KQAVSRAKAL GGTKAGADSA RKVIWAASGK
     PVLAYETVIG GFQDDGTPNQ LHVITDATTG KKLYEYQGIE NATGTGNTQY SGTVSLTTTQ
     SGSNYNLTDG DRGNHKTYNL NHGTSGTGTL FSQTSNTWGN GTTSNAATAG ADAHYGAAVT
     WDFYKNTFGR SGIKNNGVGA YSRVHYGNSY VNAFWDDSCF CMTYGDGSGN ADPLTSLDVA
     GHEMSHGVTS NTAGLNYSGE SGGLNEATSD IFGTGVEFYA ANSSDVGDYL IGEKIDINGD
     GTPLRYMDKP SKDGASKDSW YSGLGGLDVH YSSGPANHFF YLLSEGSGAK VINGVSYNSP
     TADGLPVTGI GRDKALQIWY RALTTKFTST TNYASARTGT LAAAGELYGT TSAEYKAVQD
     AWAGVAVGSR SGGGGGTGTS YESTTAVSIP DNGPAVTSSI TVSGRTGNAP SNLQVTPNIT
     HTWRGDLVID LIGPSGTAYR LKNFSSSDSA DNVTDTYTVN ASTESANGTW KLRVQDQAAQ
     DVGTINSWKL TFP
//
DBGET integrated database retrieval system