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Chlamydia trachomatis Search Results

Record: 1 of 1  
MiniMap tRNA-Leu-4 IGR442 IGR445 IGR444 IGR440 IGR441 IGR446 IGR447 IGR443 spoU,yibK, - CT540 vldD,yciA, - CT535 CT538 mip, - CT541 dnaQ, - CT536 cutE,lnt, - CT534 aspS, - CT542 trxA, - CT539 uhpC, - CT544 spoU,yibK, - CT540 vldD,yciA, - CT535 CT538 mip, - CT541 dnaQ, - CT536 cutE,lnt, - CT534 aspS, - CT542 trxA, - CT539 uhpC, - CT544 Type: tandem, Name:  - 3 spoU,yibK, - CT540 vldD,yciA, - CT535 CT538 mip, - CT541 dnaQ, - CT536 cutE,lnt, - CT534 aspS, - CT542 CT537 hisS, - CT543 CT537 hisS, - CT543 trxA, - CT539 uhpC, - CT544
* Calculated from Protein Sequence

Gene ID: CT541

DNA Molecule Name:
1  

Genbank ID:
3328979

Gene Name:
mip  

Definition:
FkbP-type peptidyl-prolyl cis-trans isomerase (MIP-like protein)

Gene Start:
607569

Gene Stop:
606841

Gene Length:
729

Molecular Weight*:
26649

pI*:
4.84

Net Charge*:
-8.35

EC:
5.2.1.8  

Functional Class:
translation; protein modification  

Pathway: pathway table

Primary Evidence:
Rockey DD, Chesebro BB, Heinzen RA, Hackstadt T. 1996. A 28 kDa major immunogen of Chlamydia psittaci shares
identity with Mip proteins of Legionella spp. and Chlamydia
trachomatis-cloning and characterization of the C. psittaci
mip-like gene. Microbiology 142 ( Pt 4):945-53. Medline: 8936321.


Lundemose AG, Kay JE, Pearce JH. 1993. Chlamydia trachomatis Mip-like protein has peptidyl-prolyl cis/trans isomerase activity that is inhibited by FK506 and rapamycin and is implicated in initiation of chlamydial infection. Mol Microbiol 7(5):777-83. Medline: 7682281.


Lundemose AG, Rouch DA, Birkelund S, Christiansen G, Pearce JH. 1992. Chlamydia trachomatis Mip-like protein. Mol Microbiol
6(17):2539-48. Medline: 1406289.


Lundemose AG, Birkelund S, Fey SJ, Larsen PM, Christiansen G. 1991. Chlamydia trachomatis contains a protein similar to the Legionella pneumophila mip gene product. Mol Microbiol 5(1):109-15. Medline: 2013997.

Comment:
This mip-like peptidyl-prolyl cis-trans isomerase (PPIASE) is an outer membrane protein that catalyzes cis-trans isomerization of proline imidic peptide bonds in oligopeptides.

From Prosite PDOC00426:

FKBP is the major high-affinity binding protein, in vertebrates, for the immunosuppressive drug FK506. It exhibits peptidyl-prolyl cis-trans isomerase activity (EC 5.2.1.8) (PPIase or rotamase). PPIase is an enzyme that accelerates protein folding by catalyzing the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.

Blast Summary:  PSI-Blast Search
Hits in gapped BLAST to MIP (macrophage infectivity potentiator)
sequences e.g. residues 42-235 are 36% similar to the MIP protein from
Legionella (U92229). CT541 is identical to the previously
published mip-like protein from trachomatis MIP_CHLTR (X66126).
See also X66127, X66126, L39892. Psi-BLAST did not reveal any additional
kinds of relationships. CT541 is similar to TP0862 in T.pallidum, a predicted
peptidyl-prolyl cis-trans isomerase. No similarity to M.genitalium.


CT541 is orthologously related to CPn0661: residues 1-240 of CT541 are 62%
similar to residues 1-248 of CPn0661, a predicted FKBP-type peptidyl-prolylcis-trans isomerase (MIP-like protein) from C. pneumoniae.

COGS Summary:  COGS Search
BeTs to 5 clades of COG0545
COG name: FKBP-type peptidyl-prolyl cis-trans isomerases 1
Functional Class:  O
The phylogenetic pattern of COG0545 is ----Y--cE--h-----lin-
Number of proteins in this genome belonging to this COG is 1


Blocks Summary:  Blocks Search
Residues 158-172, 181-214, 219-231 are matched to blocks
BL00453A,B,C, concerned with MIP_CHLTR.

ProDom Summary:  Protein Domain Search
Residues 155-224 are identical to a domain of the previously published
MIP_CHLTR. Residues 1-62, 63-86, 90-111 also correspond to
MIP_CHLTR domains. Residues 145-236 are 31% similar to
a trigger factor domain of TIG_CAMJE.

Paralogs:  Local Blast Search
No evidence of paralogs in C.trachomatis.

Pfam Summary:  Pfam Search
Residues 25 to 140 (E-value = 1.5e-05) place CT541 in the FKBP_N family which is described as Domain amino terminal to FKBP-type peptidyl-prolyl isomerase (PF01346)
Residues 142 to 232 (E-value = 4.3e-34) place CT541 in the FKBP_C family which is described as FKBP-type peptidyl-prolyl cis-trans isomerase (PF00254)

Structural Feature(s):
Feature Type  Start  Stop
gram negative signal  
1  
14
non-globular  
85  
163

PDB Hit:
gi|1311027|pdb|1FKL| Atomic Structure Of Fkbp12-Rapaymycin, An Immunophilin-Immunosuppressant Complex Fk506 Binding Protein, Fkbp12, Fkbp, Cis-Trans Prolyl-Isomerase Mol_id: 1; Molecule: Fk506 Binding Protein; Chain: Null; Synonym: Fkbp12, Fkbp; Ec: 5.2.

Gene Protein Sequence:
MKNILSWMLMFAVALPIVGCDNGGGSQTSATEKSMVEDSALTDNQKLSRT
FGHLLSRQLSRTEDFSLDLVEVIKGMQSEIDGQSAPLTDTEYEKQMAEVQ
KASFEAKCSENLASAEKFLKENKEKAGVIELEPNKLQYRVVKEGTGRVLS
GKPTALLHYTGSFIDGKVFDSSEKNKEPILLPLTKVIPGFSQGMQGMKEG
EVRVLYIHPDLAYGTAGQLPPNSLLIFEVKLIEANDDNVSVTE

Gene Nucleotide Sequence:  Sequence Viewer
ATGAAGAATATATTAAGTTGGATGCTTATGTTTGCAGTCGCTCTGCCTAT
CGTAGGATGTGATAACGGAGGCGGTTCGCAAACATCGGCTACGGAGAAAA
GCATGGTAGAAGACTCTGCATTGACAGACAATCAAAAGTTATCAAGAACT
TTTGGGCATTTATTGTCTCGTCAGTTGAGCCGAACGGAAGATTTTTCGTT
AGATCTTGTTGAAGTGATTAAAGGGATGCAATCTGAAATAGATGGACAGA
GTGCTCCTTTAACAGACACAGAATATGAAAAACAAATGGCAGAAGTACAA
AAAGCTAGTTTCGAAGCAAAATGCTCGGAAAATTTAGCTTCTGCAGAAAA
ATTCTTAAAAGAAAATAAAGAGAAGGCTGGGGTTATTGAGTTAGAGCCTA
ATAAGTTACAGTACCGTGTTGTGAAAGAGGGTACAGGACGGGTTCTTTCT
GGGAAGCCTACAGCTTTGCTTCACTATACAGGGAGCTTCATCGATGGGAA
GGTTTTTGATTCTTCAGAGAAGAATAAAGAGCCCATTTTACTGCCTTTGA
CCAAAGTAATTCCTGGATTTTCCCAAGGTATGCAAGGTATGAAAGAAGGA
GAGGTTCGAGTTCTTTACATACATCCAGATTTAGCTTACGGAACAGCTGG
ACAATTACCTCCAAACTCTCTACTCATTTTTGAAGTGAAGTTAATTGAAG
CAAACGACGATAATGTATCTGTTACAGAA


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