ID A0A1F4JMV9_9BURK Unreviewed; 497 AA.
AC A0A1F4JMV9;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Peptidase {ECO:0000313|EMBL:OGB23621.1};
GN ORFNames=A3I66_24200 {ECO:0000313|EMBL:OGB23621.1};
OS Burkholderiales bacterium RIFCSPLOWO2_02_FULL_57_36.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales.
OX NCBI_TaxID=1797562 {ECO:0000313|EMBL:OGB23621.1, ECO:0000313|Proteomes:UP000176765};
RN [1] {ECO:0000313|EMBL:OGB23621.1, ECO:0000313|Proteomes:UP000176765}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
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:OGB23621.1}.
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DR EMBL; MESE01000091; OGB23621.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F4JMV9; -.
DR STRING; 1797562.A3I66_24200; -.
DR Proteomes; UP000176765; Unassembled WGS sequence.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
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; IPR041489; PDZ_6.
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; PF13180; PDZ_2; 1.
DR Pfam; PF17820; PDZ_6; 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};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..497
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038443159"
FT DOMAIN 292..383
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 398..487
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT ACT_SITE 145
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 175
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 497 AA; 51005 MW; CC39472EB97FD18D CRC64;
MTMKLKSLSL ALIAAGVVAT GAANAVGWNP IGWFDKKQTT SQTSAVQNSA PGTAAPASAP
IGPVTAPNYR AIVEQYGPAV VGINTQGVAK TAARGAPDAI PDEMRRFFRG MPGFNGQMPR
NEAPTRGVGS GFIISKDGLI LTNAHVVDEA DEVTVKLSDR REYRAKVLGS DPATDVAVLK
IDAKDLPVVS LGHPSGIGVG DYVLAIGSPF GFEQSATAGI VSAKGRSLPG DGYVPFIQTD
VAVNPGNSGG PLFDTGGNVV GINSQIYSRS GGYQGVSFAI PIDVALRVKD QIVTTGKVSH
ARLGVSIQEL DQSLAESFKL QQPNGALVSS VMPGSAAAKA GIESGDVILS FNSQPIGRSG
DLPAMVGAAK PGDKTTLEVW RAGKKIEVPV VLAEAKEQLA ANDADDGVRQ GRLGVAVRPL
TGEEKAAANV ASGVVVEQSG GRAARAGIEA GDIIVSVNGT PVKSVEQLQA FVSKANKHLA
LLIQRDGSKI FVPVPLG
//
