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. 2012 Feb 27;7(2):e32301. doi: 10.1371/journal.pone.0032301

Table 1. The PGH complement of L. casei BL23 predicted in silico on whole genome sequence.

Locus tag MMa (kDa) SPb Putative hydrolytic specificity Catalytic domainc Other domainsd
LCABL_02350 100.5 Yes Muramidase GH25
LCABL_12360 28.0 No Muramidase GH25
LCABL_04610 27.4 No Muramidase GH25 LysM
LCABL_13470e 42.9 Yes Muramidase GH25 SH3, LysM
LCABL_12760 24.0 Yes Glucosaminidase Glucosaminidase
LCABL_05960 35.8 Yes Glucosaminidase and endopeptidase Glucosaminidase and NplC/P60
LCABL_17510 46.9 Yes Amidase Amidase_3 SH3
LCABL_11280e 37.6 No Amidase Amidase_2
LCABL_10020e 34.8 No Amidase Amidase_5
LCABL_02770 49.6 Yes Endopeptidase NplC/P60
LCABL_21960 41.4 Yes Endopeptidase NplC/P60
LCABL_00230 42.3 Yes Endopeptidase or amidase CHAP
LCABL_02100 46.9 Yes Carboxypeptidase Peptidase_S11 PBP5_C
a

Calculated molecular mass.

b

SP, signal peptide predicted with SignalP tool [40].

c

Catalytic domains were predicted with Pfam domain prediction [41]. Glucosaminidase (PF01832), muramidase (glyco_hydro_25; PF01183), Amidase_2 (PF01510), Amidase_3 (PF01520), CHAP (cysteine, histidine-dependant amidohydrolase/peptidase) domain (amidase or peptidase) (PF05257), NlpC_P60 (PF00877) (including γ-glutamyl-diamino-acid endopeptidases), Peptidase_S11 (PF00768).

d

SH3, SH3-domain (PF08460); LysM, LysM-domain (PF01476); PBP5_C (PF07943).

e

Putative prophage-encoded PGH.