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Chlamydia trachomatis Search Results

Record: 1 of 1  
MiniMap IGR224 IGR221 IGR220 IGR222 IGR225 IGR223 ihfA, - CT267 CT272 CT266 murE, - CT269 msbA, - CT264 penA,pbp, - CT270 CT273 ihfA, - CT267 CT272 CT266 murE, - CT269 msbA, - CT264 penA,pbp, - CT270 CT273 ihfA, - CT267 CT272 CT266 murE, - CT269 msbA, - CT264 penA,pbp, - CT270 CT271 amiA, - CT268 accA, - CT265 CT271 amiA, - CT268 accA, - CT265 CT273
* Calculated from Protein Sequence

Gene ID: CT269

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
murE  

Definition:
N-acetylymuramoylalanyl-D-glutamate-2,6-diaminopimelate ligase

Gene Start:
301478

Gene Stop:
300030

Gene Length:
1449

Molecular Weight*:
53323

pI*:
5.79

Net Charge*:
-9.31

EC:
6.3.2.13  

Functional Class:
cell envelope; peptidoglycan  

Pathway: pathway table
Amino Acid Metabolism; Lysine biosynthesis
Metabolism of Complex Carbohydrates; Peptideglycan biosynthesis

Comment:
The MURE enzyme in B.subtilis adds diaminopimelate to
N-acetylmuramoyl-L-alanyl-D-glutamate in the course of
peptidoglycan biosynthesis. Other E.C. numbers assigned
to this activity have been 6.3.2.17 and 6.3.2.12. See
CT268, CT270, CT272, CT756, CT758, CT761, and CT762.

Blast Summary:  PSI-Blast Search
Numerous hits in gapped BLAST to N-acetylmuramoylalanyl-D-glutamate-2,6-
diaminopimelate ligase sequences, e.g., residues 1-482
are 36% similar to MURE_BACSU. CT269 is similar to TP0933,
TP0386, TP0341 of T.pallidum and PG518 of P.gingivalis. No similarity to M.genitalium.

COGS Summary:  COGS Search
BeTs to 12 clades of COG0769
COG name: UDP-N-acetylmuramyl tripeptide synthase
Functional Class:  M
The phylogenetic pattern of COG0769 is --T--qvCebRhuj--olinx
Number of proteins in this genome belonging to this COG is 1


Blocks Summary:  Blocks Search
Significant match to blocks BL01011A,B, which encompass
folylpolyglutamate synthase domains: residues 1-5-246 and 270-311
are relevant. FOLC_BACSU and FOLC_LACCA are examples of
proteins with this signature.

ProDom Summary:  Protein Domain Search
Residues 23-278 are 35% similar to a domain observed in
MURE-BACSU.

Paralogs:  Local Blast Search
CT269 is paralogously related to CT758, CT762 and CT756, all regarded to have ligase
function in cell wall biosynthesis: residues 99-279 of
CT269 are 25% similar to CT758; residues 165-418 are
25% similar to CT762, and residues 83-184 are 34% similar to
CT756.

Pfam Summary:  Pfam Search
Residues 35 to 319 (E-value = 1.1e-87) place CT269 in the Mur_ligase family which is described as Mur ligase family, catalytic domain (PF01225)
Residues 328 to 416 (E-value = 1.5e-28) place CT269 in the Mur_ligase_C family which is described as Mur ligase family, glutamate ligase domain (PF02875)

Structural Feature(s):
Feature Type  Start  Stop
transmembrane  
60  
81

PDB Hit:
gi|2981818|pdb|1UAG| Udp-N-Acetylmuramoyl-L-Alanine:d-Glutamate Ligase Ligase, Peptidoglycan Synthesis, Murd, Adp-Forming Enzyme Mol_id: 1; Molecule: Udp-N-Acetylmuramoyl-L-Alanine:D-Glutamate Ligase; Chain: Null; Synonym: Murd; Ec: 6.3.2.9; Engineered:

Gene Protein Sequence:
MHLDQLLQNIPAKIYGKVESIPVRNLTRDSRCVGVGDIFIARQGQFCNGN
DYSSQAVANGAIAVLSSLYNPFLSVVQIIAEDPIALEASLAARFYNNPSR
HLDVIGITGTNGKTTVSCLVRELMERSGRRTGLIGTIEHILGENRIIDSF
TTPDAILLQKYFAEMVKQNLSAAVMEVSSIGMALGRVRETEFLAGVLTNI
TSDHLDFHGSLEEYIAAKKQFFASLPEKGIAVVNLDCEYAPSFLNGSQAR
AVSYAIHQEADYRADRLKLYSSGSSYDIWYQGQVFPCETSLIGEHNVYNV
LASLAVVHQFLGRDFADLVRDVRFLSAPKGRLDPILLGPFPVYIDYAHTP
DALDNVCRILLQLLPKDGRLIIVFGCGGDRDRVKRPLMAKVSEHYGFSFV
TSDNPRTEDPDQIIADICKGFSTDHYVVESDRKLAIEKAISMASDKDIVL
VAGKGHEGYQIFKHQTIVFDDREVVCEALAALC

Gene Nucleotide Sequence:  Sequence Viewer
ATGCATTTAGACCAACTTCTTCAGAATATTCCGGCTAAAATTTATGGGAA
AGTCGAGTCTATTCCTGTTAGAAATTTGACTCGAGATTCTCGTTGTGTTG
GAGTTGGTGATATTTTCATCGCTCGACAAGGGCAGTTTTGCAATGGCAAT
GACTATTCTTCTCAGGCTGTTGCGAATGGAGCGATTGCAGTTCTCTCTTC
TCTATACAATCCTTTTTTATCGGTTGTTCAGATTATCGCAGAAGATCCTA
TAGCATTGGAAGCCTCTTTGGCAGCAAGGTTTTATAATAATCCTTCAAGG
CATCTGGATGTAATAGGAATTACAGGAACTAATGGGAAGACAACAGTCTC
CTGTTTGGTTAGAGAACTTATGGAGCGTTCAGGAAGAAGAACTGGTCTTA
TTGGAACCATAGAGCACATTTTAGGTGAGAATAGGATTATTGATAGCTTT
ACCACTCCTGATGCGATTTTATTGCAGAAGTATTTTGCTGAAATGGTTAA
GCAGAACTTATCTGCAGCCGTTATGGAAGTATCTTCTATAGGGATGGCTC
TTGGTCGAGTTCGTGAAACAGAGTTCTTAGCTGGAGTTTTAACTAACATT
ACTTCAGATCATTTAGATTTTCATGGGTCTCTTGAAGAATATATTGCAGC
TAAAAAGCAGTTTTTCGCTTCCTTGCCAGAGAAAGGTATAGCTGTTGTCA
ATTTGGATTGTGAGTATGCGCCCAGCTTTTTAAATGGTTCTCAGGCAAGA
GCAGTCTCCTATGCAATCCATCAAGAAGCTGATTATCGAGCAGATAGATT
GAAGCTGTATTCATCAGGATCTTCTTATGACATTTGGTATCAGGGGCAAG
TTTTCCCTTGTGAGACATCCTTGATAGGAGAACATAATGTATATAATGTT
TTAGCATCTTTAGCTGTTGTCCATCAATTTTTAGGCAGAGACTTTGCTGA
TTTAGTACGCGATGTTCGTTTCTTATCAGCTCCTAAAGGACGTTTGGATC
CGATTTTATTGGGACCATTCCCTGTTTATATTGATTATGCCCATACTCCA
GATGCATTGGACAATGTATGTAGAATTTTATTACAACTCCTTCCTAAAGA
TGGTCGGCTAATTATTGTGTTTGGGTGTGGTGGAGATAGAGATCGTGTTA
AGCGTCCTCTTATGGCCAAAGTATCTGAGCATTACGGTTTTTCTTTTGTG
ACTTCAGATAATCCTCGGACAGAAGATCCAGACCAGATTATTGCTGATAT
ATGTAAAGGTTTCTCAACTGATCATTATGTTGTTGAGAGCGATAGGAAGC
TAGCCATAGAGAAAGCAATATCAATGGCTTCAGATAAAGATATTGTACTA
GTTGCAGGAAAGGGACATGAGGGGTATCAGATCTTCAAACATCAGACGAT
TGTCTTTGATGATCGAGAGGTTGTGTGTGAAGCCTTGGCAGCCCTTTGT


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