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dnaK | Chaperone Hsp70; Acts as a chaperone. (638 aa) | ||||
surA | Peptidyl-prolyl cis-trans isomerase; 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) | ||||
mopB | Chaperone Hsp10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. (97 aa) | ||||
purD | GAR synthetase; phosphoribosylamine--glycine ligase. (SW:PUR2_SALTY); Belongs to the GARS family. (429 aa) | ||||
bfr | Bacterioferrin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex. (158 aa) | ||||
bacA | Bacitracin resistance; Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin; Belongs to the UppP family. (274 aa) | ||||
pgk | Similar to E. coli phosphoglycerate kinase (AAC75963.1); Blastp hit to AAC75963.1 (387 aa), 97% identity in aa 1 - 387. (387 aa) | ||||
purG | Phosphoribosylformylglycinamidine synthetase; Phosphoribosylformylglycinamidine synthase involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. (1295 aa) | ||||
prpA | Serine/threonine protein phosphatase; Can hydrolyze phosphorylated Ser-, Thr- or Tyr-substrates in vitro. The natural substrate is unknown. (216 aa) | ||||
sodC-2 | Copper/zinc superoxide dismutase; Destroys radicals which are normally produced within the cells and which are toxic to biological systems; Belongs to the Cu-Zn superoxide dismutase family. (173 aa) | ||||
infC | Protein chain initiation factor IF-3; IF-3 binds to the 30S ribosomal subunit and shifts the equilibrum between 70S ribosomes and their 50S and 30S subunits in favor of the free subunits, thus enhancing the availability of 30S subunits on which protein synthesis initiation begins. (144 aa) | ||||
purE | Phosphoribosylaminoimidazole carboxylase = AIR carboxylase, catalytic subunit; Catalyzes the conversion of N5-carboxyaminoimidazole ribonucleotide (N5-CAIR) to 4-carboxy-5-aminoimidazole ribonucleotide (CAIR). (169 aa) | ||||
hemH | Ferrochelatase; Catalyzes the ferrous insertion into protoporphyrin IX. (320 aa) | ||||
tig | Peptidyl-prolyl cis/trans isomerase; Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase; Belongs to the FKBP-type PPIase family. Tig subfamily. (432 aa) | ||||
ribH | Riboflavin synthase, beta chain; Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2- butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin (By similarity); Belongs to the DMRL synthase family. (156 aa) | ||||
yajC | Preprotein translocase IISP family, membrane subunit; The SecYEG-SecDF-YajC-YidC holo-translocon (HTL) protein secretase/insertase is a supercomplex required for protein secretion, insertion of proteins into membranes, and assembly of membrane protein complexes. While the SecYEG complex is essential for assembly of a number of proteins and complexes, the SecDF-YajC-YidC subcomplex facilitates these functions. (110 aa) | ||||
htrA | Periplasmic serine protease Do, heat shock protein; DegP acts as a chaperone at low temperatures but switches to a peptidase (heat shock protein) at higher temperatures. It degrades transiently denatured and unfolded proteins which accumulate in the periplasm following heat shock or other stress conditions. DegP is efficient with Val-Xaa and Ile-Xaa peptide bonds, suggesting a preference for beta-branched side chain amino acids. Only unfolded proteins devoid of disulfide bonds appear capable of being cleaved, thereby preventing non-specific proteolysis of folded proteins. Its proteolyt [...] (475 aa) | ||||
mopA | Chaperone Hsp60 with peptide-dependent ATPase activity; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. (548 aa) |