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Database: UniProt
Entry: A0A136LY80_9BACT
LinkDB: A0A136LY80_9BACT
Original site: A0A136LY80_9BACT 
ID   A0A136LY80_9BACT        Unreviewed;       425 AA.
AC   A0A136LY80;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Protease 3 {ECO:0000313|EMBL:KXK26609.1};
DE            EC=3.4.24.55 {ECO:0000313|EMBL:KXK26609.1};
GN   Name=ptrA {ECO:0000313|EMBL:KXK26609.1};
GN   ORFNames=TR69_WS6001000615 {ECO:0000313|EMBL:KXK26609.1};
OS   candidate division WS6 bacterium OLB20.
OC   Bacteria; Candidatus Dojkabacteria.
OX   NCBI_TaxID=1617426 {ECO:0000313|EMBL:KXK26609.1, ECO:0000313|Proteomes:UP000070457};
RN   [1] {ECO:0000313|EMBL:KXK26609.1, ECO:0000313|Proteomes:UP000070457}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OLB20 {ECO:0000313|EMBL:KXK26609.1};
RA   Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.;
RT   "Improved understanding of the partial-nitritation anammox process through
RT   23 genomes representing the majority of the microbial community.";
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
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:KXK26609.1}.
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DR   EMBL; JYNZ01000003; KXK26609.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A136LY80; -.
DR   STRING; 1617426.TR69_WS6001000615; -.
DR   Proteomes; UP000070457; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-EC.
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; 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.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:KXK26609.1};
KW   Protease {ECO:0000313|EMBL:KXK26609.1}.
FT   DOMAIN          14..161
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          167..342
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   425 AA;  47462 MW;  200E6D36E8D27FB1 CRC64;
     MTPLVSTLKN GLRVLRLQDK NAAGVSIVML VGVGSRHETE EQGGIAHFLE HSLFKGSKNY
     PTSKAIGMAV ELLGGSSNAF TSYDYTGYYI KVPMHTAEQA TAILADMIMY PVFDEREIEK
     ERGVIIEEIR MYNDEPRSRA SDLFNERLFQ GHPLGRDIAG TIETVSSMTP DKLRGFVARN
     YHSRNMLLIF SGNFEPDTAQ AWAEEHFSDI PAGEAVATEL FKRPDNLNEV LYHEKQLEQT
     HMVLGGFASR RTHPDRFKYQ VGNALLSYGF GSRLFQTIRD ELGLAYYISS GISSYEETGK
     FMIRLGSDAT RAKEAVTAVL RELSAVIAGD FSDEELTRAK NYLIGTMTTQ LEATDEIALW
     YGMQLMLRKE ILSYEEISSR IEAVTRDEVT EAWSSVITSD NLLLSVLGPE ISADTRDLQL
     SVGTV
//
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