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Database: UniProt
Entry: I3II94_9BACT
LinkDB: I3II94_9BACT
Original site: I3II94_9BACT 
ID   I3II94_9BACT            Unreviewed;       886 AA.
AC   I3II94;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   SubName: Full=Putative peptidase {ECO:0000313|EMBL:GAB61439.1};
GN   ORFNames=KSU1_B0582 {ECO:0000313|EMBL:GAB61439.1};
OS   Candidatus Jettenia caeni.
OC   Bacteria; Planctomycetota; Candidatus Brocadiia; Candidatus Brocadiales;
OC   Candidatus Brocadiaceae; Candidatus Jettenia.
OX   NCBI_TaxID=247490 {ECO:0000313|EMBL:GAB61439.1, ECO:0000313|Proteomes:UP000002985};
RN   [1] {ECO:0000313|EMBL:GAB61439.1, ECO:0000313|Proteomes:UP000002985}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=22673575; DOI=10.1016/j.febslet.2012.04.041;
RA   Hira D., Toh H., Migita C.T., Okubo H., Nishiyama T., Hattori M.,
RA   Furukawa K., Fujii T.;
RT   "Anammox organism KSU-1 expresses a NirK-type copper-containing nitrite
RT   reductase instead of a NirS-type with cytochrome cd1.";
RL   FEBS Lett. 586:1658-1663(2012).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC   -!- SIMILARITY: Belongs to the peptidase M36 family.
CC       {ECO:0000256|ARBA:ARBA00006006}.
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:GAB61439.1}.
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DR   EMBL; BAFH01000002; GAB61439.1; -; Genomic_DNA.
DR   AlphaFoldDB; I3II94; -.
DR   STRING; 247490.KSU1_B0582; -.
DR   eggNOG; COG3227; Bacteria.
DR   eggNOG; COG4935; Bacteria.
DR   Proteomes; UP000002985; Unassembled WGS sequence.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.10.170.10; -; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR   Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR002884; P_dom.
DR   InterPro; IPR001842; Peptidase_M36.
DR   InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR   PANTHER; PTHR33478; EXTRACELLULAR METALLOPROTEINASE MEP; 1.
DR   PANTHER; PTHR33478:SF1; EXTRACELLULAR METALLOPROTEINASE MEP; 1.
DR   Pfam; PF01483; P_proprotein; 2.
DR   Pfam; PF02128; Peptidase_M36; 1.
DR   PRINTS; PR00999; FUNGALYSIN.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 2.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   PROSITE; PS51829; P_HOMO_B; 2.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002985};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   DOMAIN          630..757
FT                   /note="P/Homo B"
FT                   /evidence="ECO:0000259|PROSITE:PS51829"
FT   DOMAIN          760..886
FT                   /note="P/Homo B"
FT                   /evidence="ECO:0000259|PROSITE:PS51829"
SQ   SEQUENCE   886 AA;  95383 MW;  DDCC1DF326B34FC7 CRC64;
     MSREIDRRNF SVNKVTPARE AELKSRASEI SDRLPGSQRI RIKRFDTTTG NPAVITSEDG
     PAETGNYIQR ALDHVRNISK ALGLTATQPN EFVADPHIQR ASSGAVAVHL QQQYKGISIF
     QAAETVRFAP DGRLEETVGS SVAVDHDREV IPKLSVQEAV LKTAQHVATP DRDEYKMTDQ
     FGEPLTPKSV DLSGFVPKII AILSDKADQP AVFEPGPFGD KIKAALIWFP LDGGLRLAWE
     VIITMPNYEG QYRTMADAET GEILYCKQLV QSVKARGNVY HVDGGSARQM THFPSPLTDY
     GLPLPNFPFN FPDDWVEVNA TIGNSVYAHL GDTGSAVQGV VQDGVLTFNP ADSKGDDQKV
     LNIFYYNCYM HDFFYLLGFR EGDGNFQHNN LGRGGVATDR VDARAHSGAV WGTANMYTPI
     DGSNPVMNMG LVTSTDRHTA FDSSVVFHEF MHGVTNRLVG GPMNVSALEA PQSSGMGEGW
     GDYIACTINN TTVVGAWVVK KAGGIRGFPY DSNFPDTFAD VGKGRYTEEH NIGEIWCATI
     MEMNRKIGAV LAVQLVVDAL KLSPANPSFL DMRDSILAAL DKKHAAGQLS SGEHSTAKNG
     IWSVFAKFGM GPNAKSHGAS LSGIVADFKT PSDTTGQNIR VETEPNIAIP DNNSSGLTSI
     LTISQAGKIK RLVISINIEH TYIGDLKVSL TTPGNGTAVL HNRTGASADN LVKSYTSEDT
     SDLASLIGAQ TQGNWVLKVA DLAGQDVGTL RSWGIEIDLE AASQVIRGEA APALTIPDNN
     PAGAQSVIGI TQSGVAKGIK VSVDITHTYI GDLRVELVAP SGQQVILHNR TGGSKDNLIT
     TYDSISASSL AALIGQQIEG NWILRPTDMA GQDIGKLNKW SLEFTL
//
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