VV1295 protein (Vibrio vulnificus) - STRING interaction network

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Score

VV1295

annotation not available (465 aa)

Predicted Functional Partners:

dnaE2

0.987

VV1296

0.979

lexA

0.779

polA

0.766

dnaN

0.623

recA

0.600

VVA0035

0.562

VV1232

0.559

VVA1111

0.544

VV1297

0.533

Your Current Organism:

Vibrio vulnificus

NCBI taxonomy Id: 672
Other names: ATCC 27562, BCRC 12905, Beneckea vulnifica, CAIM 610, CCRC 12905, CCUG 13448, CCUG 16394, CIP 75.4, DSM 10143, IFO 15645, JCM 3725, LMG 13545, NBRC 15645, V. vulnificus, Vibrio vulnificus, strain 324

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
VV1232	VV1295	VV93_v1c11490	VV93_v1c12110	annotation not available	annotation not available	0.559
VV1232	dnaN	VV93_v1c11490	VV93_v1c00020	annotation not available	Beta sliding clamp; Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP-independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3’-5’ exonuclease proofreading activity. The beta chain is required for initiation of replication as [...]	0.727
VV1232	lexA	VV93_v1c11490	VV93_v1c01110	annotation not available	LexA repressor; Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair	0.590
VV1232	polA	VV93_v1c11490	VV93_v1c01730	annotation not available	DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5’-3’ exonuclease activity	0.857
VV1232	recA	VV93_v1c11490	VV93_v1c25160	annotation not available	Protein RecA; Can catalyze the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage	0.575
VV1295	VV1232	VV93_v1c12110	VV93_v1c11490	annotation not available	annotation not available	0.559
VV1295	VV1296	VV93_v1c12110	VV93_v1c12120	annotation not available	annotation not available	0.979
VV1295	VV1297	VV93_v1c12110	VV93_v1c12130	annotation not available	annotation not available	0.533
VV1295	VVA0035	VV93_v1c12110	VV93_v1c30430	annotation not available	annotation not available	0.562
VV1295	VVA1111	VV93_v1c12110	VV93_v1c40510	annotation not available	annotation not available	0.544
VV1295	dnaE2	VV93_v1c12110	VV93_v1c12100	annotation not available	Error-prone DNA polymerase; DNA polymerase involved in damage-induced mutagenesis and translesion synthesis (TLS). It is not the major replicative DNA polymerase	0.987
VV1295	dnaN	VV93_v1c12110	VV93_v1c00020	annotation not available	Beta sliding clamp; Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP-independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3’-5’ exonuclease proofreading activity. The beta chain is required for initiation of replication as [...]	0.623
VV1295	lexA	VV93_v1c12110	VV93_v1c01110	annotation not available	LexA repressor; Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair	0.779
VV1295	polA	VV93_v1c12110	VV93_v1c01730	annotation not available	DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5’-3’ exonuclease activity	0.766
VV1295	recA	VV93_v1c12110	VV93_v1c25160	annotation not available	Protein RecA; Can catalyze the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage	0.600
VV1296	VV1295	VV93_v1c12120	VV93_v1c12110	annotation not available	annotation not available	0.979
VV1296	VV1297	VV93_v1c12120	VV93_v1c12130	annotation not available	annotation not available	0.533
VV1296	VVA1111	VV93_v1c12120	VV93_v1c40510	annotation not available	annotation not available	0.509
VV1296	dnaE2	VV93_v1c12120	VV93_v1c12100	annotation not available	Error-prone DNA polymerase; DNA polymerase involved in damage-induced mutagenesis and translesion synthesis (TLS). It is not the major replicative DNA polymerase	0.974
VV1296	lexA	VV93_v1c12120	VV93_v1c01110	annotation not available	LexA repressor; Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair	0.664

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