ID A0A0B0ELG1_9BACT Unreviewed; 501 AA.
AC A0A0B0ELG1;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Protease {ECO:0000313|EMBL:KHE93857.1};
GN ORFNames=SCABRO_00414 {ECO:0000313|EMBL:KHE93857.1};
OS Candidatus Scalindua brodae.
OC Bacteria; Planctomycetota; Candidatus Brocadiia; Candidatus Brocadiales;
OC Candidatus Scalinduaceae; Scalindua.
OX NCBI_TaxID=237368 {ECO:0000313|EMBL:KHE93857.1, ECO:0000313|Proteomes:UP000030652};
RN [1] {ECO:0000313|EMBL:KHE93857.1, ECO:0000313|Proteomes:UP000030652}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RU1 {ECO:0000313|EMBL:KHE93857.1};
RA Speth D.R., Russ L., Kartal B., Op den Camp H.J., Dutilh B.E., Jetten M.S.;
RT "Draft genome of anammox bacterium scalindua brodae, obtained using
RT differential coverage binning of sequence data from two enrichment
RT reactors.";
RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
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:KHE93857.1}.
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DR EMBL; JRYO01000033; KHE93857.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B0ELG1; -.
DR PATRIC; fig|237368.3.peg.452; -.
DR eggNOG; COG0265; Bacteria.
DR Proteomes; UP000030652; 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:KHE93857.1};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..34
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 35..501
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002055161"
FT DOMAIN 292..383
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 399..467
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 73..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..114
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 144
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 174
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 248
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
SQ SEQUENCE 501 AA; 54193 MW; 0A4EDCBF0F1F8592 CRC64;
MYSKRQNIKK YFLPFIVSLF ALSLILGYTG NAKAATSARE LEQSLTRVSE DVKLSVVSIT
TVKVFKHPAT GGYHGDQYGR GRGDQYGRGH GGSRRDRRGG PFDDFFDKFT PKAPPKGEFK
TQSLGSGVIV KIDGETGYIL TNNHVVADTD ELKVRLSDKR EFDAEIVGTD EQTDLAVIKI
EGKNLIAATM GDSEILRQGQ WAIAIGNPFG LTQTVSVGVV SAIGRSGVGI ANYENFIQTD
AAINPGNSGG PLVNIDGEVI GINTAIFTRS GGYQGIGFAI PVNMAKAVLR DLIDKGKVTR
GWLGVAIQNM DESLAEQFGV EVTEGVLISD VQDGSPAKEA GFERGDIVIG YDNKEISDVD
HLRHIVAQTE VGKKIKVKVL RKEKETILTV KIGEQPSDLF ALGKSSIGND LGISVQDLTE
ELAKSFEFEG ETGVVVTAVE PGSSAAQADV KEGDLIKEVN REKINNLVEF TDALKRTAKG
KDILFLLRRG MHTRFVIIKS K
//
