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}.
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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
//