ID A0A0Q5LC37_9BURK Unreviewed; 517 AA.
AC A0A0Q5LC37;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Peptidase {ECO:0000313|EMBL:KQR41342.1};
GN ORFNames=ASF94_12645 {ECO:0000313|EMBL:KQR41342.1};
OS Acidovorax sp. Leaf160.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=1736280 {ECO:0000313|EMBL:KQR41342.1, ECO:0000313|Proteomes:UP000051403};
RN [1] {ECO:0000313|EMBL:KQR41342.1, ECO:0000313|Proteomes:UP000051403}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf160 {ECO:0000313|EMBL:KQR41342.1,
RC ECO:0000313|Proteomes:UP000051403};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQR41342.1, ECO:0000313|Proteomes:UP000051403}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf160 {ECO:0000313|EMBL:KQR41342.1,
RC ECO:0000313|Proteomes:UP000051403};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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:KQR41342.1}.
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DR EMBL; LMOV01000028; KQR41342.1; -; Genomic_DNA.
DR RefSeq; WP_056669985.1; NZ_LMOV01000028.1.
DR AlphaFoldDB; A0A0Q5LC37; -.
DR STRING; 1736280.ASF94_12645; -.
DR OrthoDB; 8520726at2; -.
DR Proteomes; UP000051403; 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:UP000051403};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 310..374
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 430..507
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 84..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 163
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 193
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 266
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
SQ SEQUENCE 517 AA; 52617 MW; 0AE20E7BE7F74CE8 CRC64;
MNSILSTPRR LTLALIAAGA VGATGAGLVT NMRPGHAAVP QPVAVAAAAA PGGLPSGGVA
MPDFAQITAR NGAAVVNISV TGTTKTSLGG AGDEGDDDDD DTPAAQQRGA QGMNPNDPFY
EFFKRFGMPG GGGRMQPQRE VPMQGEGSGF IVSPDGVVLT NAHVVKGASS VTVKLTDRRE
FRAKVLGSDP KTDIAVLKID ASHLPVVQLG STQALNVGEW VLAIGSPFGF ENSVTAGVVS
AKGRALPDDS FVPFIQTDVA VNPGNSGGPL FNTRGEVVGI NSQIYSRSGG YQGVSFAIPI
EVAAKVKDQI LATGKASHAR LGVSVQEVNQ AFADSFQLDK PEGALVAGVE PGGPADKAGL
KSGDVIRSID GQPIVASGDL PAFVGQAAPG SQARMEVWRH GKKEEIVATL GDASDRKAAQ
AAAGEKGVGK GQLGLALRPL TPQERREAGV EGGLLIEQVR GPAAQAGVAP GDVLLAVNGT
PAQGLDQVRE AVSKSGKSVA LLIERDGNKI FVPVRLG
//
