mycle-LPQC

6_AlphaBeta_hydrolase : mycle-ML0376Mycobacterium leprae putative membrane protein, mycle-ML1921Mycobacterium leprae hypothetical protein ml1921, mycle-ML2269Mycobacterium leprae putative hydrolase, mycle-Q49856Mycobacterium leprae b229_c1_169.
A85-Mycolyl-transferase : mycle-a85aMycobacterium leprae (and strain Br4923) Antigen 85A, mycolytransferase, mycle-a85bMycobacterium leprae (strain Br4923; complex B) ag85B fibronectin-binding protein B, mycle-a85cMycobacterium leprae (and strain Br4923) binding protein C ag85C, mycle-mpt5Mycobacterium leprae (and strain Br4923) mpt51 antigen precursor.
Aclacinomycin-methylesterase_RdmC : mycle-lipGMycobacterium leprae (strains TN; Br4923) ML1899 lipG.
AlphaBeta_hydrolase : mycle-ML1339Mycobacterium leprae hypothetical protein (putative secreted protease), mycle-ML1632Mycobacterium leprae possible hydrolase, mycle-ML1633Mycobacterium leprae possible secreted hydrolase.
Carbon-carbon_bond_hydrolase : mycle-tpeaMycobacterium leprae tropinesterase ML0685 MLCB1779.02.
Chlorophyllase : mycle-ML0370Mycobacterium leprae hypothetical protein ml0370 b229_f1_20.
Cutinase : mycle-q9cdb3Mycobacterium leprae hypothetical protein ml0099.
Dienelactone_hydrolase : mycle-ML1444Mycobacterium leprae possible dienelactone hydrolase.
Epoxide_hydrolase : mycle-ML2297Mycobacterium leprae (and strain Br4923) putative hydrolase, mycle-MLCB22.16cMycobacterium leprae (and strain Br4923) MLCB22.16c gene.
Homoserine_transacetylase : mycle-metxMycobacterium leprae (and strain Br4923) (homoserine transacetylase) (hta).
Hormone-sensitive_lipase_like : mycle-ML0314Mycobacterium leprae ML0314c LipU Secreted carboxyl esterase.
Monoglyceridelipase_lysophospholip : mycle-ML2603 Mycobacterium leprae ML2603 similar to myctu-rv0183.
PE-PPE : mycle-q9cc62Mycobacterium leprae (and strain Br4923 Lepb1170_F3_112) Putative uncharacterized protein ML1232.
PHA_synth_III_C : mycle-MLC1351.21CMycobacterium leprae (and strain Br4923) hypothetical 109.2 kda protein.
S9N_PREPL_Peptidase_S9 : mycle-PTRBMycobacterium leprae ptrb (protease II).
Thioesterase : mycle-ML2359Mycobacterium leprae putative thioesterase, mycle-PKS13Mycobacterium leprae polyketide synthase

MNVARWLASVVLAVCLAGCVGRQVSASSRDQPGTFQFGGLNRTYVLHVPP
GSPVGLVLNLHGGGGTGAGQQGLTDFDAVADLNNLLVAYPDGYDKSWADG
RGASPADRRHVDDVGFLVELAAKLQSDFGVAPGHVFVTGMSNGGFMSNKL
ACDRADMFAAIAPVAGTLGVDVACHPSQPVSVMDAHGTDDPLVPFNGGDV
HGRGGVSHVVSVTNMVEKWRTADGCQGDPSQQELPDVGDGTFVRRFDYTV
CANSAEVVFYKINKGGHTWPGGKQYLPKVVIGSTTCVFDASEVIAQFFLT
HARS

Title: Massive gene decay in the leprosy bacillus
Cole ST, Eiglmeier K, Parkhill J, James KD, Thomson NR, Wheeler PR, Honore N, Garnier T, Churcher C and Barrell BG <34 more author(s)> Cole ST, Eiglmeier K, Parkhill J, James KD, Thomson NR, Wheeler PR, Honore N, Garnier T, Churcher C, Harris D, Mungall K, Basham D, Brown D, Chillingworth T, Connor R, Davies RM, Devlin K, Duthoy S, Feltwell T, Fraser A, Hamlin N, Holroyd S, Hornsby T, Jagels K, Lacroix C, Maclean J, Moule S, Murphy L, Oliver K, Quail MA, Rajandream MA, Rutherford KM, Rutter S, Seeger K, Simon S, Simmonds M, Skelton J, Squares R, Squares S, Stevens K, Taylor K, Whitehead S, Woodward JR, Barrell BG (- 34)
Ref: Nature, 409:1007, 2001 : PubMed
Abstract


ESTHER: Cole_2001_Nature_409_1007
PubMedSearch: Cole 2001 Nature 409 1007
PubMedID: 11234002
Gene_locus related to this paper: mycle-a85a, mycle-a85b, mycle-a85c, mycle-lipG, mycle-LPQC, mycle-metx, mycle-ML0314, mycle-ML0370, mycle-ML0376, mycle-ML1339, mycle-ML1444, mycle-ML1632, mycle-ML1633, mycle-ML1921, mycle-ML2269, mycle-ML2297, mycle-ML2359, mycle-ML2603, mycle-mpt5, mycle-PKS13, mycle-PTRB, mycle-q9cc62, mycle-q9cdb3

Abstract

Leprosy, a chronic human neurological disease, results from infection with the obligate intracellular pathogen Mycobacterium leprae, a close relative of the tubercle bacillus. Mycobacterium leprae has the longest doubling time of all known bacteria and has thwarted every effort at culture in the laboratory. Comparing the 3.27-megabase (Mb) genome sequence of an armadillo-derived Indian isolate of the leprosy bacillus with that of Mycobacterium tuberculosis (4.41 Mb) provides clear explanations for these properties and reveals an extreme case of reductive evolution. Less than half of the genome contains functional genes but pseudogenes, with intact counterparts in M. tuberculosis, abound. Genome downsizing and the current mosaic arrangement appear to have resulted from extensive recombination events between dispersed repetitive sequences. Gene deletion and decay have eliminated many important metabolic activities including siderophore production, part of the oxidative and most of the microaerophilic and anaerobic respiratory chains, and numerous catabolic systems and their regulatory circuits.



        

Title: Genomic organization of the mycobacterial sigma gene cluster
Doukhan L, Predich M, Nair G, Dussurget O, Mandic-Mulec I, Cole ST, Smith DR, Smith I
Ref: Gene, 165:67, 1995 : PubMed
Abstract


ESTHER: Doukhan_1995_Gene_165_67
PubMedSearch: Doukhan 1995 Gene 165 67
PubMedID: 7489918
Gene_locus related to this paper: mycle-LPQC

Abstract

We have previously described sigma A and sigma B and their structural genes, mysA and mysB, respectively, in Mycobacterium smegmatis. We have now sequenced the corresponding regions in the M. tuberculosis and M. leprae chromosomes, and have found the two homologous genes. The chromosomal linkage and the deduced amino acid (aa) sequences of the two genes show very high similarity in the three species of mycobacteria. We also report the finding of two other open reading frames (ORF) in these clusters. orfX, which has an unknown function, is located between mysA and mysB. The other ORF, located downstream from mysB, encodes a homolog of DtxR, the iron regulatory protein from Corynebacterium diphtheriae (Cd).