STRINGSTRING
rne rne ligA ligA lysS lysS priB priB efp efp recO recO OHC10506.1 OHC10506.1 ccmE ccmE OHC10642.1 OHC10642.1 recG recG ruvA ruvA aspS aspS OHC10779.1 OHC10779.1 OHC09667.1 OHC09667.1 rpsL rpsL rplB rplB rpsQ rpsQ infA infA pheT pheT OHC09820.1 OHC09820.1 rnr rnr rlmD rlmD rho rho rimO rimO nusA nusA OHC10052.1 OHC10052.1 pnp pnp
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.
Node Color
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:
rneRibonuclease G; Endoribonuclease that plays a central role in RNA processing and decay. Required for the maturation of 5S and 16S rRNAs and the majority of tRNAs. Also involved in the degradation of most mRNAs. Belongs to the RNase E/G family. RNase E subfamily. (882 aa)
ligADNA ligase (NAD(+)) LigA; DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double- stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA; Belongs to the NAD-dependent DNA ligase family. LigA subfamily. (671 aa)
lysSlysine--tRNA ligase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the class-II aminoacyl-tRNA synthetase family. (516 aa)
priBPrimosomal replication protein N; Binds single-stranded DNA at the primosome assembly site (PAS); Belongs to the PriB family. (97 aa)
efpElongation factor P; Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase. (186 aa)
recODNA repair protein RecO; Involved in DNA repair and RecF pathway recombination. (244 aa)
OHC10506.130S ribosomal protein S1; Binds mRNA; thus facilitating recognition of the initiation point. It is needed to translate mRNA with a short Shine-Dalgarno (SD) purine-rich sequence. (557 aa)
ccmECytochrome c biogenesis protein CcmE; Heme chaperone required for the biogenesis of c-type cytochromes. Transiently binds heme delivered by CcmC and transfers the heme to apo-cytochromes in a process facilitated by CcmF and CcmH. Belongs to the CcmE/CycJ family. (144 aa)
OHC10642.1Cold-shock protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (67 aa)
recGATP-dependent DNA helicase RecG; Critical role in recombination and DNA repair. Helps process Holliday junction intermediates to mature products by catalyzing branch migration. Has a DNA unwinding activity characteristic of a DNA helicase with a 3'- to 5'- polarity. Unwinds branched duplex DNA (Y- DNA); Belongs to the helicase family. RecG subfamily. (695 aa)
ruvAHolliday junction DNA helicase RuvA; The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. RuvA stimulates, in the presence of DNA, the weak ATPase activity of RuvB. (194 aa)
aspSaspartate--tRNA ligase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. (599 aa)
OHC10779.1Single-stranded DNA-binding protein; Plays an important role in DNA replication, recombination and repair. Binds to ssDNA and to an array of partner proteins to recruit them to their sites of action during DNA metabolism. (151 aa)
OHC09667.1Ribonuclease II; Derived by automated computational analysis using gene prediction method: Protein Homology. (662 aa)
rpsL30S ribosomal protein S12; Interacts with and stabilizes bases of the 16S rRNA that are involved in tRNA selection in the A site and with the mRNA backbone. Located at the interface of the 30S and 50S subunits, it traverses the body of the 30S subunit contacting proteins on the other side and probably holding the rRNA structure together. The combined cluster of proteins S8, S12 and S17 appears to hold together the shoulder and platform of the 30S subunit. (126 aa)
rplB50S ribosomal protein L2; One of the primary rRNA binding proteins. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is somewhat controversial. Makes several contacts with the 16S rRNA in the 70S ribosome. Belongs to the universal ribosomal protein uL2 family. (276 aa)
rpsQ30S ribosomal protein S17; One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA. (89 aa)
infATranslation initiation factor IF-1; One of the essential components for the initiation of protein synthesis. Stabilizes the binding of IF-2 and IF-3 on the 30S subunit to which N-formylmethionyl-tRNA(fMet) subsequently binds. Helps modulate mRNA selection, yielding the 30S pre-initiation complex (PIC). Upon addition of the 50S ribosomal subunit IF-1, IF-2 and IF-3 are released leaving the mature 70S translation initiation complex. (72 aa)
pheTphenylalanine--tRNA ligase subunit beta; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. (818 aa)
OHC09820.1Involved in the processing of the 5'end of 16S rRNA; Derived by automated computational analysis using gene prediction method: Protein Homology. (487 aa)
rnrRibonuclease R; 3'-5' exoribonuclease that releases 5'-nucleoside monophosphates and is involved in maturation of structured RNAs. (803 aa)
rlmD23S rRNA (uracil(1939)-C(5))-methyltransferase; Catalyzes the formation of 5-methyl-uridine at position 1939 (m5U1939) in 23S rRNA; Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA M5U methyltransferase family. RlmD subfamily. (476 aa)
rhoTranscription termination factor Rho; Facilitates transcription termination by a mechanism that involves Rho binding to the nascent RNA, activation of Rho's RNA- dependent ATPase activity, and release of the mRNA from the DNA template. (420 aa)
rimORibosomal protein S12 methylthiotransferase; Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein S12; Belongs to the methylthiotransferase family. RimO subfamily. (452 aa)
nusATranscription termination/antitermination protein NusA; Participates in both transcription termination and antitermination. (493 aa)
OHC10052.1RNA-binding transcriptional accessory protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (789 aa)
pnpPolyribonucleotide nucleotidyltransferase; Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'- direction. (722 aa)
Your Current Organism:
Polynucleobacter sp. GWA24521
NCBI taxonomy Id: 1801989
Other names: P. sp. GWA2_45_21, Polynucleobacter sp. GWA2_45_21
Server load: low (20%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.