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}.
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; 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
//