A new cell surface proteinase: Sequencing and analysis of the prtB gene from Lactobacillus delbrueckii subsp bulgaricus

被引:98
作者
Gilbert, C
Atlan, D
Blanc, B
Portalier, R
Germond, JE
Lapierre, L
Mollet, B
机构
[1] UNIV LYON 1,LAB MICROBIOL & GENET MOL,UMR CNRS 106,F-69622 VILLEURBANNE,FRANCE
[2] NESTEC LTD,NESTLE RES CTR,CH-1000 LAUSANNE 26,SWITZERLAND
关键词
D O I
10.1128/jb.178.11.3059-3065.1996
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Investigation of the chromosomal region downstream of the lacZ gene from Lactobacillus delbrueckii subsp. bulgaricus revealed the presence of a gene (prtB) encoding a proteinase of 1,946 residues with a predicted molecular mass of 212 kDa. The deduced amino acid sequence showed that PrtB proteinase displays significant homology with the N termini and catalytic domains of lactococcal PrtP cell surface proteinases and is probably synthesized as a preproprotein. However, the presence of a cysteine near the histidine Of the PrtB active site suggests that PrtB belongs to the subfamily of cysteine subtilisins. The C-terminal region strongly differs from those of PrtP proteinases by having a high lysine content, an imperfect duplication of 41 residues, and a degenerated sequence compared with the consensus sequence for proteins anchoring in the cell walls of gram-positive bacteria. Finally, the product of the truncated prtM-like gene located immediately upstream of the prtB gene seems too short to be involved in the maturation of PrtB.
引用
收藏
页码:3059 / 3065
页数:7
相关论文
共 52 条
[1]   ISOLATION AND CHARACTERIZATION OF AMINOPEPTIDASE-DEFICIENT LACTOBACILLUS-BULGARICUS MUTANTS [J].
ATLAN, D ;
LALOI, P ;
PORTALIER, R .
APPLIED AND ENVIRONMENTAL MICROBIOLOGY, 1989, 55 (07) :1717-1723
[2]   CLONING, SEQUENCING AND CHARACTERIZATION OF THE PEPIP GENE ENCODING A PROLINE IMINOPEPTIDASE FROM LACTOBACILLUS-DELBRUECKII SUBSP BULGARICUS CNRZ-397 [J].
ATLAN, D ;
GILBERT, C ;
BLANC, B ;
PORTALIER, R .
MICROBIOLOGY-UK, 1994, 140 :527-535
[3]   S-LAYER PROTEIN OF LACTOBACILLUS-ACIDOPHILUS ATCC-4356 - PURIFICATION, EXPRESSION IN ESCHERICHIA-COLI, AND NUCLEOTIDE-SEQUENCE OF THE CORRESPONDING GENE [J].
BOOT, HJ ;
KOLEN, CPAM ;
VANNOORT, JM ;
POUWELS, PH .
JOURNAL OF BACTERIOLOGY, 1993, 175 (19) :6089-6096
[4]  
BOSMAN B, 1993, FEMS MICROBIOL REV, V12
[5]   PRESENCE OF X-PROLYL-DIPEPTIDYL-PEPTIDASE IN LACTIC-ACID BACTERIA [J].
CASEY, MG ;
MEYER, J .
JOURNAL OF DAIRY SCIENCE, 1985, 68 (12) :3212-3215
[6]  
DE MAN J. C., 1960, JOUR APPL BACT, V23, P130, DOI 10.1111/j.1365-2672.1960.tb00188.x
[7]   DNA PROBE FOR LACTOBACILLUS-DELBRUECKII [J].
DELLEY, M ;
MOLLET, B ;
HOTTINGER, H .
APPLIED AND ENVIRONMENTAL MICROBIOLOGY, 1990, 56 (06) :1967-1970
[8]  
DESSEN P, 1990, CABIOS, V6, P335
[9]   GENETICS OF LACTOSE UTILIZATION IN LACTIC-ACID BACTERIA [J].
DEVOS, WM ;
VAUGHAN, EE .
FEMS MICROBIOLOGY REVIEWS, 1994, 15 (2-3) :217-237
[10]   DIVERSITY OF CELL-ENVELOPE PROTEINASE SPECIFICITY AMONG STRAINS OF LACTOCOCCUS-LACTIS AND ITS RELATIONSHIP TO CHARGE CHARACTERISTICS OF THE SUBSTRATE-BINDING REGION [J].
EXTERKATE, FA ;
ALTING, AC ;
BRUINENBERG, PG .
APPLIED AND ENVIRONMENTAL MICROBIOLOGY, 1993, 59 (11) :3640-3647