pepQ_1 protein (Xanthomonas fragariae) - STRING interaction network

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pepQ_1

Xaa-Pro dipeptidase; Splits dipeptides with a prolyl residue in the C-terminal position. (442 aa)

Predicted Functional Partners:

map

0.567

BER92_03555

0.548

plsB

0.543

pepN

0.537

AOD16482.1

0.423

AOD16452.1

0.407

Your Current Organism:

Xanthomonas fragariae

NCBI taxonomy Id: 48664
Other names: ATCC 33239, CCUG 23372, CFBP 2157, DSM 3587, ICMP 5715, LMG 708, LMG:708, VKM B-2165, X. fragariae

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
AOD16452.1	pepN	BER92_01665	BER92_02725	Peptidase S9; Derived by automated computational analysis using gene prediction method: Protein Homology.	Aminopeptidase; Derived by automated computational analysis using gene prediction method: Protein Homology.	0.634
AOD16452.1	pepQ_1	BER92_01665	BER92_03545	Peptidase S9; Derived by automated computational analysis using gene prediction method: Protein Homology.	Xaa-Pro dipeptidase; Splits dipeptides with a prolyl residue in the C-terminal position.	0.407
AOD16482.1	BER92_03555	BER92_03565	BER92_03555	Non-canonical purine NTP pyrophosphatase, RdgB/HAM1 family; Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions. Belongs to the HAM1 NTPase family.	Pilus assembly protein PilZ; Incomplete; partial on complete genome; missing start; Derived by automated computational analysis using gene prediction method: Protein Homology.	0.658
AOD16482.1	pepQ_1	BER92_03565	BER92_03545	Non-canonical purine NTP pyrophosphatase, RdgB/HAM1 family; Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions. Belongs to the HAM1 NTPase family.	Xaa-Pro dipeptidase; Splits dipeptides with a prolyl residue in the C-terminal position.	0.423
BER92_03555	AOD16482.1	BER92_03555	BER92_03565	Pilus assembly protein PilZ; Incomplete; partial on complete genome; missing start; Derived by automated computational analysis using gene prediction method: Protein Homology.	Non-canonical purine NTP pyrophosphatase, RdgB/HAM1 family; Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions. Belongs to the HAM1 NTPase family.	0.658
BER92_03555	pepQ_1	BER92_03555	BER92_03545	Pilus assembly protein PilZ; Incomplete; partial on complete genome; missing start; Derived by automated computational analysis using gene prediction method: Protein Homology.	Xaa-Pro dipeptidase; Splits dipeptides with a prolyl residue in the C-terminal position.	0.548
map	pepQ_1	BER92_06475	BER92_03545	Type I methionyl aminopeptidase; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.	Xaa-Pro dipeptidase; Splits dipeptides with a prolyl residue in the C-terminal position.	0.567
pepN	AOD16452.1	BER92_02725	BER92_01665	Aminopeptidase; Derived by automated computational analysis using gene prediction method: Protein Homology.	Peptidase S9; Derived by automated computational analysis using gene prediction method: Protein Homology.	0.634
pepN	pepQ_1	BER92_02725	BER92_03545	Aminopeptidase; Derived by automated computational analysis using gene prediction method: Protein Homology.	Xaa-Pro dipeptidase; Splits dipeptides with a prolyl residue in the C-terminal position.	0.537
pepQ_1	AOD16452.1	BER92_03545	BER92_01665	Xaa-Pro dipeptidase; Splits dipeptides with a prolyl residue in the C-terminal position.	Peptidase S9; Derived by automated computational analysis using gene prediction method: Protein Homology.	0.407
pepQ_1	AOD16482.1	BER92_03545	BER92_03565	Xaa-Pro dipeptidase; Splits dipeptides with a prolyl residue in the C-terminal position.	Non-canonical purine NTP pyrophosphatase, RdgB/HAM1 family; Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions. Belongs to the HAM1 NTPase family.	0.423
pepQ_1	BER92_03555	BER92_03545	BER92_03555	Xaa-Pro dipeptidase; Splits dipeptides with a prolyl residue in the C-terminal position.	Pilus assembly protein PilZ; Incomplete; partial on complete genome; missing start; Derived by automated computational analysis using gene prediction method: Protein Homology.	0.548
pepQ_1	map	BER92_03545	BER92_06475	Xaa-Pro dipeptidase; Splits dipeptides with a prolyl residue in the C-terminal position.	Type I methionyl aminopeptidase; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.	0.567
pepQ_1	pepN	BER92_03545	BER92_02725	Xaa-Pro dipeptidase; Splits dipeptides with a prolyl residue in the C-terminal position.	Aminopeptidase; Derived by automated computational analysis using gene prediction method: Protein Homology.	0.537
pepQ_1	plsB	BER92_03545	BER92_00400	Xaa-Pro dipeptidase; Splits dipeptides with a prolyl residue in the C-terminal position.	Glycerol-3-phosphate 1-O-acyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the GPAT/DAPAT family.	0.543
plsB	pepQ_1	BER92_00400	BER92_03545	Glycerol-3-phosphate 1-O-acyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the GPAT/DAPAT family.	Xaa-Pro dipeptidase; Splits dipeptides with a prolyl residue in the C-terminal position.	0.543