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Database: UniProt
Entry: A0A518LGN4_9BACT
LinkDB: A0A518LGN4_9BACT
Original site: A0A518LGN4_9BACT 
ID   A0A518LGN4_9BACT        Unreviewed;       957 AA.
AC   A0A518LGN4;
DT   16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2019, sequence version 1.
DT   24-JAN-2024, entry version 12.
DE   SubName: Full=Protease 3 {ECO:0000313|EMBL:QDV89218.1};
DE            EC=3.4.24.55 {ECO:0000313|EMBL:QDV89218.1};
DE   Flags: Precursor;
GN   Name=ptrA_1 {ECO:0000313|EMBL:QDV89218.1};
GN   ORFNames=RAS2_02820 {ECO:0000313|EMBL:QDV89218.1};
OS   Phycisphaerae bacterium RAS2.
OC   Bacteria; Planctomycetota; Phycisphaerae.
OX   NCBI_TaxID=2528035 {ECO:0000313|EMBL:QDV89218.1, ECO:0000313|Proteomes:UP000320198};
RN   [1] {ECO:0000313|EMBL:QDV89218.1, ECO:0000313|Proteomes:UP000320198}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RAS2 {ECO:0000313|EMBL:QDV89218.1,
RC   ECO:0000313|Proteomes:UP000320198};
RA   Wiegand S., Jogler M., Boedeker C., Pinto D., Vollmers J., Rivas-Marin E.,
RA   Kohn T., Peeters S.H., Heuer A., Rast P., Oberbeckmann S., Bunk B.,
RA   Jeske O., Meyerdierks A., Storesund J.E., Kallscheuer N., Luecker S.,
RA   Lage O.M., Pohl T., Merkel B.J., Hornburger P., Mueller R.-W., Bruemmer F.,
RA   Labrenz M., Spormann A.M., Op den Camp H., Overmann J., Amann R.,
RA   Jetten M.S.M., Mascher T., Medema M.H., Devos D.P., Kaster A.-K.,
RA   Ovreas L., Rohde M., Galperin M.Y., Jogler C.;
RT   "Deep-cultivation of Planctomycetes and their phenomic and genomic
RT   characterization uncovers novel biology.";
RL   Submitted (FEB-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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DR   EMBL; CP036352; QDV89218.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A518LGN4; -.
DR   Proteomes; UP000320198; Chromosome.
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; 4.
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; METALLOPROTEASE; 1.
DR   PANTHER; PTHR11851:SF49; MITOCHONDRIAL-PROCESSING PEPTIDASE SUBUNIT ALPHA; 1.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 2.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
DR   PROSITE; PS00143; INSULINASE; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:QDV89218.1};
KW   Protease {ECO:0000313|EMBL:QDV89218.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000320198};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           30..957
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5021888936"
FT   DOMAIN          53..198
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          208..382
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          676..854
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   REGION          567..588
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          918..957
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        918..939
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        940..957
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   957 AA;  105806 MW;  42EA92007771D32B CRC64;
     MKSSTTSWRP VCIAGVAICF LSTTAVLHAA GDAKKIRSVE GITEYALDNG MKVLLFPDES
     KPTVTVNITY FVGSRHEGYG ETGMAHLLEH MVFKGTPKFP QVWKSLQDHG ASFNGTTWYD
     RTNYFETLAA TEENLNFALE LEADRMINSF IAEKDLKSEF SVVRNEFEMG ENDPVSILSE
     RITSAAYLWH NYGKSTIGSR EDIERVPIQR LQDFYKKFYQ PDNAMLVVAG KFDEAATLKK
     IEKLYGGIAR PDRKLEPTYT VEPTQDDERF VTLRRVGDIQ AVGCVYHICS GSHPDMAAVD
     VMADILDATQ TGRLYKALIE TEKATSVRSS AYSLCEPGHL EIMAEVRQNK SLDDVRETML
     AVLDDLANQD ISDAEVERAR NSYAKQFTRL INDSGRVGVQ LSEYAAMGDW RLMFWHRDQV
     AKVTPADVKR VAALYLRPSN RTVGMFIPTK DPVRTTVPPP PDVLAMLKDY KGQQAVVQGE
     SLPPEPSAIE ARTQREDLPG GLKLAMIPKK TRGQKISATI TLRYGSEEDF KGRIDAVGMI
     ASMLDKGTAK HSRRELADEL DRIKTSIGIG GGGGRGRMGR GAGGGETGAM SISVETERKH
     FAEAMALLRE MLREPTFPEK EFDKLKKQAM ASLESQLSEP MVLAMNEMMR RMNPYEPSDV
     RYVPTPAEQL QRLQAVTLED IKSAYKELLG ASYGEVSIVG DIDASEARTI VADTFKGWKS
     PRPFERIARE FKETQPDTVA INTPDKQNAL IAMAMNLPIK DDDADFAALK LGNFILGQSS
     NSRILNRLRQ KEGLSYGAGS MLNASALDRA GMFGVYGICA PQNAEKAIAC AREELDKLLK
     KGVTAEELED ARKGYLEQVK VQLSADGGIA GMLANDLYLG RTMKFRAEEL AKIEKLTLDE
     VNAALRKHID PSKLVEIRAG DFKVTPKPDA SKDTAASEDD DSGNEGSESE SSDDENS
//
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