surA protein (Vibrio vulnificus) - STRING interaction network

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surA

Chaperone SurA; Chaperone involved in the correct folding and assembly of outer membrane proteins. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane-associated steps of protein maturation (428 aa)

Predicted Functional Partners:

lptD

0.956

ksgA

0.949

pdxA

0.934

bamA

0.932

bamB

0.924

apaH

0.854

apaG

0.792

bamD

0.781

tolC

0.779

VV2548

0.774

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
VV2548	bamA	VV93_v1c22670	VV93_v1c22680	Chaperone protein skp; Molecular chaperone that interacts specifically with outer membrane proteins, thus maintaining the solubility of early folding intermediates during passage through the periplasm	Outer membrane protein assembly factor BamA; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane	0.980
VV2548	bamB	VV93_v1c22670	VV93_v1c07150	Chaperone protein skp; Molecular chaperone that interacts specifically with outer membrane proteins, thus maintaining the solubility of early folding intermediates during passage through the periplasm	Outer membrane protein assembly factor BamB; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane	0.622
VV2548	bamD	VV93_v1c22670	VV93_v1c06480	Chaperone protein skp; Molecular chaperone that interacts specifically with outer membrane proteins, thus maintaining the solubility of early folding intermediates during passage through the periplasm	Outer membrane protein assembly factor BamD; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane	0.650
VV2548	lptD	VV93_v1c22670	VV93_v1c04480	Chaperone protein skp; Molecular chaperone that interacts specifically with outer membrane proteins, thus maintaining the solubility of early folding intermediates during passage through the periplasm	LPS-assembly protein LptD; Together with LptE, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane	0.651
VV2548	surA	VV93_v1c22670	VV93_v1c04470	Chaperone protein skp; Molecular chaperone that interacts specifically with outer membrane proteins, thus maintaining the solubility of early folding intermediates during passage through the periplasm	Chaperone SurA; Chaperone involved in the correct folding and assembly of outer membrane proteins. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane-associated steps of protein maturation	0.774
apaG	apaH	VV93_v1c04440	VV93_v1c04430	annotation not available	Bis(5’-nucleosyl)-tetraphosphatase, symmetrical; Hydrolyzes diadenosine 5’,5’’’-P1,P4-tetraphosphate to yield ADP	0.954
apaG	ksgA	VV93_v1c04440	VV93_v1c04450	annotation not available	Ribosomal RNA small subunit methyltransferase A; Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3’-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits	0.915
apaG	lptD	VV93_v1c04440	VV93_v1c04480	annotation not available	LPS-assembly protein LptD; Together with LptE, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane	0.678
apaG	pdxA	VV93_v1c04440	VV93_v1c04460	annotation not available	4-hydroxythreonine-4-phosphate dehydrogenase; Catalyzes the NAD(P)-dependent oxidation of 4- (phosphohydroxy)-L-threonine (HTP) into 2-amino-3-oxo-4- (phosphohydroxy)butyric acid which spontaneously decarboxylates to form 3-amino-2-oxopropyl phosphate (AHAP)	0.876
apaG	surA	VV93_v1c04440	VV93_v1c04470	annotation not available	Chaperone SurA; Chaperone involved in the correct folding and assembly of outer membrane proteins. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane-associated steps of protein maturation	0.792
apaH	apaG	VV93_v1c04430	VV93_v1c04440	Bis(5’-nucleosyl)-tetraphosphatase, symmetrical; Hydrolyzes diadenosine 5’,5’’’-P1,P4-tetraphosphate to yield ADP	annotation not available	0.954
apaH	ksgA	VV93_v1c04430	VV93_v1c04450	Bis(5’-nucleosyl)-tetraphosphatase, symmetrical; Hydrolyzes diadenosine 5’,5’’’-P1,P4-tetraphosphate to yield ADP	Ribosomal RNA small subunit methyltransferase A; Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3’-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits	0.878
apaH	lptD	VV93_v1c04430	VV93_v1c04480	Bis(5’-nucleosyl)-tetraphosphatase, symmetrical; Hydrolyzes diadenosine 5’,5’’’-P1,P4-tetraphosphate to yield ADP	LPS-assembly protein LptD; Together with LptE, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane	0.762
apaH	pdxA	VV93_v1c04430	VV93_v1c04460	Bis(5’-nucleosyl)-tetraphosphatase, symmetrical; Hydrolyzes diadenosine 5’,5’’’-P1,P4-tetraphosphate to yield ADP	4-hydroxythreonine-4-phosphate dehydrogenase; Catalyzes the NAD(P)-dependent oxidation of 4- (phosphohydroxy)-L-threonine (HTP) into 2-amino-3-oxo-4- (phosphohydroxy)butyric acid which spontaneously decarboxylates to form 3-amino-2-oxopropyl phosphate (AHAP)	0.846
apaH	surA	VV93_v1c04430	VV93_v1c04470	Bis(5’-nucleosyl)-tetraphosphatase, symmetrical; Hydrolyzes diadenosine 5’,5’’’-P1,P4-tetraphosphate to yield ADP	Chaperone SurA; Chaperone involved in the correct folding and assembly of outer membrane proteins. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane-associated steps of protein maturation	0.854
bamA	VV2548	VV93_v1c22680	VV93_v1c22670	Outer membrane protein assembly factor BamA; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane	Chaperone protein skp; Molecular chaperone that interacts specifically with outer membrane proteins, thus maintaining the solubility of early folding intermediates during passage through the periplasm	0.980
bamA	bamB	VV93_v1c22680	VV93_v1c07150	Outer membrane protein assembly factor BamA; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane	Outer membrane protein assembly factor BamB; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane	0.984
bamA	bamD	VV93_v1c22680	VV93_v1c06480	Outer membrane protein assembly factor BamA; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane	Outer membrane protein assembly factor BamD; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane	0.990
bamA	lptD	VV93_v1c22680	VV93_v1c04480	Outer membrane protein assembly factor BamA; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane	LPS-assembly protein LptD; Together with LptE, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane	0.863
bamA	surA	VV93_v1c22680	VV93_v1c04470	Outer membrane protein assembly factor BamA; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane	Chaperone SurA; Chaperone involved in the correct folding and assembly of outer membrane proteins. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane-associated steps of protein maturation	0.932

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