STRINGSTRING
KLT19482.1 KLT19482.1 priA priA def-2 def-2 fmt fmt KLT19486.1 KLT19486.1 rlmN rlmN KLT19487.1 KLT19487.1 KLT19488.1 KLT19488.1 KLT18606.1 KLT18606.1 KLT16482.1 KLT16482.1
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
KLT19482.1Phosphopantothenoylcysteine decarboxylase; Catalyzes two steps in the biosynthesis of coenzyme A. In the first step cysteine is conjugated to 4'-phosphopantothenate to form 4- phosphopantothenoylcysteine, in the latter compound is decarboxylated to form 4'-phosphopantotheine; In the C-terminal section; belongs to the PPC synthetase family. (407 aa)
priAPrimosomal protein N; Involved in the restart of stalled replication forks. Recognizes and binds the arrested nascent DNA chain at stalled replication forks. It can open the DNA duplex, via its helicase activity, and promote assembly of the primosome and loading of the major replicative helicase DnaB onto DNA; Belongs to the helicase family. PriA subfamily. (803 aa)
def-2Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. (161 aa)
fmtmethionyl-tRNA formyltransferase; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus; Belongs to the Fmt family. (314 aa)
KLT19486.116S rRNA methyltransferase; Specifically methylates the cytosine at position 967 (m5C967) of 16S rRNA. (449 aa)
rlmNRibosomal RNA large subunit methyltransferase N; Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs; Belongs to the radical SAM superfamily. RlmN family. (349 aa)
KLT19487.1Protein phosphatase; Derived by automated computational analysis using gene prediction method: Protein Homology. (249 aa)
KLT19488.1Serine/threonine protein kinase; Derived by automated computational analysis using gene prediction method: Protein Homology. (657 aa)
KLT18606.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (332 aa)
KLT16482.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (269 aa)
Your Current Organism:
Bacillus vireti
NCBI taxonomy Id: 220686
Other names: B. vireti, Bacillus vireti Heyrman et al. 2004, DSM 15602, JCM 21711, LMG 21834, LMG:21834, NBRC 102452, strain IDA3632, strain R-15447
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