STRINGSTRING
glmU glmU rpoB rpoB rpoC rpoC rpoA rpoA nadD nadD gtaB_2 gtaB_2 gtaB_1 gtaB_1 pcnB pcnB ribF ribF rmlA2 rmlA2 GCA_900177895_00319 GCA_900177895_00319 kdsB kdsB dnaQ dnaQ ispD ispD dnaE dnaE rfaE rfaE dinB dinB pseB pseB hddC hddC galT galT GCA_900177895_00839 GCA_900177895_00839 cca cca pnp pnp mobA mobA moaB moaB holA holA holB holB GCA_900177895_01252 GCA_900177895_01252 GCA_900177895_01319 GCA_900177895_01319 glnD glnD thiF thiF GCA_900177895_01513 GCA_900177895_01513 rph rph GCA_900177895_01553 GCA_900177895_01553 rpoZ rpoZ neuA neuA GCA_900177895_01620 GCA_900177895_01620 polC polC vbhT vbhT dnaX dnaX dnaG_2 dnaG_2 GCA_900177895_01839 GCA_900177895_01839 coaD coaD glnE glnE GCA_900177895_02021 GCA_900177895_02021 GCA_900177895_02022 GCA_900177895_02022 dnaN dnaN cdsA cdsA polA polA tsaC_2-2 tsaC_2-2
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
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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:
glmUUnannotated protein; Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C- terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N- acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5- triphosphate), a reaction catalyzed by the N-terminal domain. (455 aa)
rpoBUnannotated protein; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. (1398 aa)
rpoCUnannotated protein; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. (1399 aa)
rpoAUnannotated protein; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. (328 aa)
nadDUnannotated protein; Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD). (201 aa)
gtaB_2Unannotated protein. (295 aa)
gtaB_1Unannotated protein. (468 aa)
pcnBUnannotated protein; Adds poly(A) tail to the 3' end of many RNAs, which usually targets these RNAs for decay. Plays a significant role in the global control of gene expression, through influencing the rate of transcript degradation, and in the general RNA quality control. Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family. (442 aa)
ribFUnannotated protein; Belongs to the ribF family. (308 aa)
rmlA2Unannotated protein; Catalyzes the formation of dTDP-glucose, from dTTP and glucose 1-phosphate, as well as its pyrophosphorolysis. Belongs to the glucose-1-phosphate thymidylyltransferase family. (288 aa)
GCA_900177895_00319Unannotated protein. (311 aa)
kdsBUnannotated protein; Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria. (251 aa)
dnaQUnannotated protein; DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. The epsilon subunit contain the editing function and is a proofreading 3'- 5' exonuclease. (244 aa)
ispDUnannotated protein; Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D- erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP). (232 aa)
dnaEUnannotated protein. (1152 aa)
rfaEUnannotated protein. (316 aa)
dinBUnannotated protein; Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII. (350 aa)
pseBUnannotated protein. (332 aa)
hddCUnannotated protein. (234 aa)
galTUnannotated protein. (344 aa)
GCA_900177895_00839Unannotated protein. (96 aa)
ccaUnannotated protein; Catalyzes the addition and repair of the essential 3'- terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. Also shows phosphatase, 2'-nucleotidase and 2',3'-cyclic phosphodiesterase activities. These phosphohydrolase activities are probably involved in the repair of the tRNA 3'-CCA terminus degraded by intracellular RNases. (415 aa)
pnpUnannotated protein; Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'- direction. (715 aa)
mobAUnannotated protein; Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor; Belongs to the MobA family. (194 aa)
moaBUnannotated protein; May be involved in the biosynthesis of molybdopterin. Belongs to the MoaB/Mog family. (186 aa)
holAUnannotated protein. (336 aa)
holBUnannotated protein. (323 aa)
GCA_900177895_01252Unannotated protein. (358 aa)
GCA_900177895_01319Unannotated protein. (246 aa)
glnDUnannotated protein; Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen metabolism. (826 aa)
thiFUnannotated protein. (245 aa)
GCA_900177895_01513Unannotated protein. (290 aa)
rphUnannotated protein; Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation. (241 aa)
GCA_900177895_01553Unannotated protein. (85 aa)
rpoZUnannotated protein; Promotes RNA polymerase assembly. Latches the N- and C- terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits. (68 aa)
neuAUnannotated protein. (231 aa)
GCA_900177895_01620Unannotated protein. (102 aa)
polCUnannotated protein. (464 aa)
vbhTUnannotated protein. (199 aa)
dnaXUnannotated protein; DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity. (660 aa)
dnaG_2Unannotated protein; RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. (586 aa)
GCA_900177895_01839Unannotated protein; Catalyzes the ADP transfer from ATP to D-glycero-beta-D- manno-heptose 1-phosphate, yielding ADP-D-glycero-beta-D-manno-heptose. (163 aa)
coaDUnannotated protein; Reversibly transfers an adenylyl group from ATP to 4'- phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. Belongs to the bacterial CoaD family. (169 aa)
glnEUnannotated protein; Involved in the regulation of glutamine synthetase GlnA, a key enzyme in the process to assimilate ammonia. When cellular nitrogen levels are high, the C-terminal adenylyl transferase (AT) inactivates GlnA by covalent transfer of an adenylyl group from ATP to specific tyrosine residue of GlnA, thus reducing its activity. Conversely, when nitrogen levels are low, the N-terminal adenylyl removase (AR) activates GlnA by removing the adenylyl group by phosphorolysis, increasing its activity. The regulatory region of GlnE binds the signal transduction protein PII (GlnB) [...] (895 aa)
GCA_900177895_02021Unannotated protein. (355 aa)
GCA_900177895_02022Unannotated protein. (568 aa)
dnaNUnannotated protein; 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 [...] (367 aa)
cdsAUnannotated protein; Belongs to the CDS family. (264 aa)
polAUnannotated protein; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family. (919 aa)
tsaC_2-2Unannotated protein; Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Catalyzes the conversion of L-threonine, HCO(3)(-)/CO(2) and ATP to give threonylcarbamoyl-AMP (TC-AMP) as the acyladenylate intermediate, with the release of diphosphate. (190 aa)
Your Current Organism:
Kingella negevensis
NCBI taxonomy Id: 1522312
Other names: CCUG 69806, CSUR P957, K. negevensis, Kingella negevensis El Houmami et al. 2017, Kingella sp. AA267, Kingella sp. AA503, Kingella sp. BB632, Kingella sp. BB713, Kingella sp. CC132, Kingella sp. CC173_6, Kingella sp. CC505b, Kingella sp. CC546, Kingella sp. CHUV31, Kingella sp. D2292, Kingella sp. D2756, Kingella sp. D7323, Kingella sp. EE451, Kingella sp. EPA009, Kingella sp. EPA014, Kingella sp. PED555, Kingella sp. PVC1712, Kingella sp. PVC1735, Kingella sp. SW7208426, Kingella sp. Sch1437, Kingella sp. Sch538, Kingella sp. Sch690, strain Sch538
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