ID A0A0S9NG99_9BURK Unreviewed; 341 AA.
AC A0A0S9NG99;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Signal protein PDZ {ECO:0000313|EMBL:KQP44259.1};
GN ORFNames=ASF44_28510 {ECO:0000313|EMBL:KQP44259.1};
OS Pseudorhodoferax sp. Leaf274.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae.
OX NCBI_TaxID=1736318 {ECO:0000313|EMBL:KQP44259.1, ECO:0000313|Proteomes:UP000051759};
RN [1] {ECO:0000313|EMBL:KQP44259.1, ECO:0000313|Proteomes:UP000051759}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf274 {ECO:0000313|EMBL:KQP44259.1,
RC ECO:0000313|Proteomes:UP000051759};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQP44259.1, ECO:0000313|Proteomes:UP000051759}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf274 {ECO:0000313|EMBL:KQP44259.1,
RC ECO:0000313|Proteomes:UP000051759};
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 -!- SIMILARITY: Belongs to the peptidase S1C family.
CC {ECO:0000256|ARBA:ARBA00010541}.
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:KQP44259.1}.
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DR EMBL; LMNA01000008; KQP44259.1; -; Genomic_DNA.
DR RefSeq; WP_056899569.1; NZ_LMNA01000008.1.
DR AlphaFoldDB; A0A0S9NG99; -.
DR STRING; 1736318.ASF44_28510; -.
DR OrthoDB; 8678832at2; -.
DR Proteomes; UP000051759; 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; cd00989; PDZ_metalloprotease; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001940; Peptidase_S1C.
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; PF13365; Trypsin_2; 1.
DR PRINTS; PR00834; PROTEASES2C.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000051759};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..341
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006654230"
FT DOMAIN 231..296
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 341 AA; 35942 MW; 49D45A5437A51AFB CRC64;
MRTIRSACLV LALALAPAFG PLRSIAATPS PIQQTIDAMS RAHAAVVGVQ VLASEDAPSA
ETLGRQRRGS GVVIGADGLI LTIGYLMLEA EHIQILTQDG RQLPAQAVAY DLATGFGLLR
PLLPLRGVAA VPLGSHPELE PGTVLMTAIG GEGGDVAMTQ LVAKRAFSGY WEYFIDTALF
TSPPIANHSG APLFNQKGEL VGIGSLLVMD ALGTGRQWPG NMFVPVDLLK PILAEMRSTG
STRLSKRPWL GVNSVEQSGR VQVARVSKAS PASVAGLQPG DVVLAVDGTK VTTLEGFYKK
LWDRADAQAE VQLTVLQGAD VKTLTVKPVD RMSTLRKPKG I
//
