ID A0A136PSE3_9ACTN Unreviewed; 452 AA.
AC A0A136PSE3;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Zinc protease {ECO:0000313|EMBL:KXK61338.1};
GN ORFNames=AWW66_14030 {ECO:0000313|EMBL:KXK61338.1};
OS Micromonospora rosaria.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=47874 {ECO:0000313|EMBL:KXK61338.1, ECO:0000313|Proteomes:UP000070620};
RN [1] {ECO:0000313|EMBL:KXK61338.1, ECO:0000313|Proteomes:UP000070620}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 803 {ECO:0000313|EMBL:KXK61338.1,
RC ECO:0000313|Proteomes:UP000070620};
RA Yang H., He X., Zhu D.;
RT "Whole genome sequence and analysis of Micromonospora rosaria DSM 803,
RT which can produce antibacterial substance rosamicin.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KXK61338.1}.
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DR EMBL; LRQV01000043; KXK61338.1; -; Genomic_DNA.
DR RefSeq; WP_067365388.1; NZ_LRQV01000043.1.
DR AlphaFoldDB; A0A136PSE3; -.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000070620; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 2.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR001431; Pept_M16_Zn_BS.
DR InterPro; IPR007863; Peptidase_M16_C.
DR PANTHER; PTHR11851:SF149; GH01077P; 1.
DR PANTHER; PTHR11851; METALLOPROTEASE; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
DR PROSITE; PS00143; INSULINASE; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:KXK61338.1};
KW Protease {ECO:0000313|EMBL:KXK61338.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000070620}.
FT DOMAIN 44..191
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 198..376
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 241..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 452 AA; 48772 MW; 352BEF0068A60019 CRC64;
MSRAPRSSSP ADRREVTPRA ATRTLSEDPL GGTVRRTVLP SGLRVLTEAI PTTRSVSFGV
WVAVGSRDET GTQSGAAHFL EHLLFKGTHK RTALDISAQI EAVGGETNAF TTKEYTCYYA
RVLDEDLPLA IDVMCDLVAD SVLAAADVET ERGVILEEIA MHDDEPGDEV HDLFVRAVYG
DHPLGRLISG TEETVTPMTR RQIHHFYRRR YTPPQIVVAA AGNLDHAAVL RLVRQALRGT
PLDTERAAPA PPRPRTPGVR TRPAATVVEP KETEQAHVIL GCPGIDRLDE RRFALGVLNN
VLGGGMSSRL FQEIRERRGL AYSVYSYASQ YADSGLFAVY AGCAPGKLDE VLTLTRAELG
RVAADGLTEA EVARGKGMSK GSFVLGLEDT GSRMSRLAKG ELLYGTLMPV DELLARVDAV
TVDEVNALAA ELLARPMSLA VVGPFGADDF TG
//
