ID I3IIE3_9BACT Unreviewed; 526 AA.
AC I3IIE3;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Protease {ECO:0000313|EMBL:GAB61488.1};
GN ORFNames=KSU1_B0631 {ECO:0000313|EMBL:GAB61488.1};
OS Candidatus Jettenia caeni.
OC Bacteria; Planctomycetota; Candidatus Brocadiia; Candidatus Brocadiales;
OC Candidatus Brocadiaceae; Candidatus Jettenia.
OX NCBI_TaxID=247490 {ECO:0000313|EMBL:GAB61488.1, ECO:0000313|Proteomes:UP000002985};
RN [1] {ECO:0000313|EMBL:GAB61488.1, 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 -!- 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:GAB61488.1}.
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DR EMBL; BAFH01000002; GAB61488.1; -; Genomic_DNA.
DR AlphaFoldDB; I3IIE3; -.
DR STRING; 247490.KSU1_B0631; -.
DR MEROPS; S01.453; -.
DR eggNOG; COG0265; Bacteria.
DR OrthoDB; 248175at2; -.
DR Proteomes; UP000002985; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00987; PDZ_serine_protease; 2.
DR Gene3D; 2.30.42.10; -; 2.
DR Gene3D; 2.40.10.120; -; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR011782; Pept_S1C_Do.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR001940; Peptidase_S1C.
DR NCBIfam; TIGR02037; degP_htrA_DO; 1.
DR PANTHER; PTHR22939; SERINE PROTEASE FAMILY S1C HTRA-RELATED; 1.
DR PANTHER; PTHR22939:SF129; SERINE PROTEASE HTRA2, MITOCHONDRIAL; 1.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF13180; PDZ_2; 1.
DR Pfam; PF13365; Trypsin_2; 1.
DR PRINTS; PR00834; PROTEASES2C.
DR SMART; SM00228; PDZ; 2.
DR SUPFAM; SSF50156; PDZ domain-like; 2.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50106; PDZ; 2.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:GAB61488.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002985};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 309..400
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 424..491
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 80..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..96
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..112
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 161
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 191
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 265
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
SQ SEQUENCE 526 AA; 57444 MW; B27574BB6CB77F29 CRC64;
MGNKLGKFYL RPLFVVAFSL CFGIGMYLSY GAVVCAANKQ THEADADALA TAVHLEHVFQ
NVVNQVKPAV VSITSVKTFK HSQQQRQRQM PNDRFHSPSP RSEPDQEDEG DPFRQFRDFF
GDDFFDRFFK PRFPEGDFKI QGLGSGVIID SEKGYIITNN HVVEDADELK VTLGDKREFD
GKVIGTDPQT DIAVVKIEGD NLPLAKLGDS DTIQVGQWAI AIGNPFGLSQ TVSIGVISAT
GRANVGVAQY EDMIQTDAAI NPGNSGGPLV SIRGEVMGIN TAIFTRSGGY QGIGFAIPVN
MVKIVMKDLI EKGKVTRGWL GVVIQDIDPA LAKSFNVTVT EGVLVSDVQE NSPAQEAGLE
RGDIITEYEG KPIRDVNHLR NTVAQTEVGK KVKMKVLRDG KEKELSIKIG EQPAELFAIG
PGGTPPLEKE QKELGMTVQN LTKEIAKNLG IEDESGVIVS NIQPGSPAGM SDIREGDIIK
EVNRKKISNV TEFKKALNEA DKEKGILMLV KRGEFSRYVI IKIKGK
//
