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Database: UniProt
Entry: A0A5C5W2B9_9BACT
LinkDB: A0A5C5W2B9_9BACT
Original site: A0A5C5W2B9_9BACT 
ID   A0A5C5W2B9_9BACT        Unreviewed;       954 AA.
AC   A0A5C5W2B9;
DT   13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2019, sequence version 1.
DT   27-MAR-2024, entry version 12.
DE   SubName: Full=Peptidase M16 inactive domain protein {ECO:0000313|EMBL:TWT44229.1};
DE   Flags: Precursor;
GN   ORFNames=RAS1_06390 {ECO:0000313|EMBL:TWT44229.1};
OS   Phycisphaerae bacterium RAS1.
OC   Bacteria; Planctomycetota; Phycisphaerae.
OX   NCBI_TaxID=2528034 {ECO:0000313|EMBL:TWT44229.1, ECO:0000313|Proteomes:UP000316082};
RN   [1] {ECO:0000313|EMBL:TWT44229.1, ECO:0000313|Proteomes:UP000316082}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RAS1 {ECO:0000313|EMBL:TWT44229.1,
RC   ECO:0000313|Proteomes:UP000316082};
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   -!- 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:TWT44229.1}.
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DR   EMBL; SMLU01000001; TWT44229.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5C5W2B9; -.
DR   OrthoDB; 9811314at2; -.
DR   Proteomes; UP000316082; Unassembled WGS sequence.
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; 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; PTHR43690:SF18; INSULIN-DEGRADING ENZYME-RELATED; 1.
DR   PANTHER; PTHR43690; NARDILYSIN; 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:0000256|ARBA:ARBA00022801};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000316082};
KW   Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..954
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5022942572"
FT   DOMAIN          48..170
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          208..385
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          702..885
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   REGION          595..618
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   954 AA;  103605 MW;  1D2111A80BE9240E CRC64;
     MNRPLRIARS GAISLCLALL SLPIAVAQTL PTDPSLVTGE LDNGLRYIVR RHAEPPGRAT
     VWIHFHTGSL NETDAQRGIA HYLEHMAFNG SENFPPGSVV PFFQSLGMTF GRDQNAFTSF
     EQTTYQLSLP DAKPETIAKG LTFFSDVAAG LALSAKEIDA ERQIIQEERR RGLSGRQRVS
     NYVLERLAPG SLYGVRLPIG TEETINSVNE KDFRDYYGKW YGASNATLMV VADADPAEVT
     QAISAKFAGL AKKPRPAPQA VNVRPYEKSV AIVASDAEVK SEDVRITKIG PPRPPTTSVP
     QYREDLVARL ATMAMNARLG DKVARGGTSY QNARVSLGND PGIMYSAEMS ARAASGKWQN
     ALEEAALELQ RARAFGFTQR EFEDATKEII SGAERAVETE STIPAGALIG RLNGAVTSEE
     PTLSPQQRLD LVKKLLPTIT REEVSKCFAD EFNPTAVAFI ATLPAGDNVP TEATLLEIGT
     KALAVRPTAE AEIAHATELM AGKPITGQVK EGAEHVESTV WSGWLSNNVR VHHRFMDQRK
     NEVSFNISLV GGELLETADT RGITQAAQVG WSRAATQKLS STDIRELMTG KKVDVRGGGG
     FGGGGRRGRG GGMGGPGGGD GISLNISGNP DEIETGLQLA YLLLTEPKIE QAAFDQFKTA
     TRERLEEAKL NPMMLGMQTV MAAPYPDDEV RTRPLTVEQV DKLTLAAAQA WLEKLIQTSP
     IEVVVIGDMP RERALQLAAQ YLGALPARER ISPESYASLR KLKRPAGPRV IEKTLATPTE
     QAFVLSGFYG CDETNRTDVR ALNMASRILS TRMVKEVREE AQLVYSISAS SRAASTYPGF
     GVFSAAAPTE PTKAGPLVEK LAEMFATFAK NGPTDEEMDV ARKQMAKTFE DQMREPGYWS
     GRLNQLTFRG ISLDDILSEP AAYQSMTAAQ VRDVFGKYYS KENSIVVKVV PTGK
//
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