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
//