ID A0A133XK45_9RHOO Unreviewed; 483 AA.
AC A0A133XK45;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Peptidase {ECO:0000313|EMBL:KXB31309.1};
GN ORFNames=AT959_06405 {ECO:0000313|EMBL:KXB31309.1};
OS Dechloromonas denitrificans.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Azonexaceae;
OC Dechloromonas.
OX NCBI_TaxID=281362 {ECO:0000313|EMBL:KXB31309.1, ECO:0000313|Proteomes:UP000070186};
RN [1] {ECO:0000313|EMBL:KXB31309.1, ECO:0000313|Proteomes:UP000070186}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-841 {ECO:0000313|EMBL:KXB31309.1,
RC ECO:0000313|Proteomes:UP000070186};
RA Yoon S., Nissen S., Park D., Sanford R.A., Loeffler F.E.;
RT "Nitrous oxide reduction kinetics distinguish bacteria harboring typical
RT versus atypical NosZ.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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:KXB31309.1}.
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DR EMBL; LODL01000013; KXB31309.1; -; Genomic_DNA.
DR RefSeq; WP_066881826.1; NZ_LODL01000013.1.
DR AlphaFoldDB; A0A133XK45; -.
DR STRING; 281362.AT959_06405; -.
DR Proteomes; UP000070186; 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 Reference proteome {ECO:0000313|Proteomes:UP000070186};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..483
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039076831"
FT DOMAIN 278..369
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 388..473
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT ACT_SITE 131
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 161
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 234
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
SQ SEQUENCE 483 AA; 49633 MW; 5A207F0BFECDA2FC CRC64;
MKAMKMTVAA MAVAAAIGGA YSFGHLQALP SAQAAGSVTS AAPATPAVIA APAALPDMRS
IIAANAPAVV NISITGTRKT AATLPQLDPD DPLYQFFRRF GGQMPQESTP TRGQGSGFIV
GADGTILTNA HVVEEASEVT VKLNDKREFK ARVLGADKAS DVAVLKIDAK NLPTVRVGTS
LQTQVGEWVL AIGSPFGFES SASAGIVSAK SRTLPDGSYV PFIQTDVAVN PGNSGGPLFN
MNGEVIGINS QIYSRSGGYQ GLSFAIPIEV AMNVEHQIIS TGKVQRGKLG VSIQEVNQAL
ADSFGLAKPA GALVSSVEKG SPAAKAGLEP GDVILGVDGK TLNSAGDLPA TVALKKPGES
TRLQIWRKGG THDIDVKIGS FNEEKLASAE TPSADKGRLG VAVRPLTPDE KRQAEVNGGL
LIEQAGGAAA RAGIRPGDII LSVNGQPIDS VDQLRGIIAK SGKKAAILLE RGNARLFVPV
DLG
//
