TECHNOLOGY FOCUS - BIOTECHNOLOGY - Preferred Bacterium: The cell wall sorting signal comprises an Leu-Pro-X-Thr-Gly (SEQ ID NO: 14), given in the specification, motif where X is any amino acid. The cell wall sorting signal comprises a cell wall sorting signal from a Gram-positive microorganism that encodes an endogenous sortase enzyme. The cell wall sorting signal comprises a cell wall sorting signal from an organism selected from Staphylococcus aureus, Streptococcus sobrinus, Enterococcus faecalis, Streptococcus pyogenes, Listeria monocytogenes, Actinomyces viscosus, Streptococcus agalactiae, and Streptococcus mutans. The cell wall sorting signal comprises a domain of the S. aureus Fibronectin Binding Protein B. The cell wall sorting signal comprises a motif selected from SEQ ID NO: 14, Asn-Pro-Gln-Thr-Asn (SEQ ID NO: 13), Leu-Pro-X-Thr-Gly-Gly (SEQ ID NO: 18), Leu-Pro-X-Thr-Ala-(Ser-Thr) (SEQ ID NO: 19), and Leu-Ala-X-Thr-Gly (SEQ ID NO: 20), where X is any amino acid, where sequences are given in the specification. The cell wall sorting signal comprises any of the 12 defined sequences comprising 32-38 (SEQ ID NO: 1-12), given in the specification. The bacterium encodes an endogenous sortase transpeptidase, where the endogenous sortase transpeptidase is upregulated. The bacterium further comprises a construct encoding a sortase transpeptidase, where the sortase transpeptidase is a sortase A enzyme or its homolog. The sortase A enzyme is a Bacillus anthracis sortase A enzyme or its homolog. The sortase transpeptidase is under control of an inducible promoter or a constitutive promoter. The secretory signal sequence comprises a secretory signal sequence from the Bacillus subtilis PhrC protein. The secretory signal sequence comprises a defined sequence of 35 amino acids (SEQ ID NO: 13), given in the specification. One or more endogenous proteases of the bacterium are down-regulated or knocked out, where the one or more endogenous proteases comprise a cell wall protease, and where the cell wall protease comprises a WprA protease or its homolog. The bacterium comprises a protein comprising one or more cellulolytic enzymes covalently linked to the surface of the microorganism, and a nucleic acid construct that encodes the protein and one or more cellulolytic enzymes attached to a secretory signal sequence at the N-terminus of the protein and a cell wall sorting signal at the carboxyl terminus of the protein, where the protein further comprises a comprises a cellulose or carbohydrate binding domain (CBD). The bacterium comprises a protein comprising one or more cohesin domains covalently linked to the surface of the microorganism, where the bacterium, comprises a nucleic acid construct that encodes the protein comprising the one or more cohesin domains attached to a secretory signal sequence at the N-terminus of the protein and a cell wall sorting signal at the carboxyl terminus of the protein. One or more of the cohesin domains are attached to one or more proteins comprising a dockerin attached to one or more cellulolytic enzymes where the dockerin is bound to the one or more cohesin domains. The protein comprising a dockerin attached to a cellulolytic enzyme further comprises a cellulose or CBD. The cohesin domain comprises a cohesin domain from a Clostridium sp.. The dockerin comprises a dockerin domain from an organism selected from Clostridium thermocellum, Clostridium cellulolyticum, Ruminococcus flavefaciens, Clostridium cellulovorans, Clostridium acetobutylicum, Clostridium josui, Clostridium papyrosolvens, Acidothermus cellulolyticus, and Ruminococcus albus. The dockerin attached to a cellulolytic enzyme is encoded by a construct in the bacterium. The dockerin attached to a cellulolytic enzyme provided from a source extrinsic to the bacterium. The cellulolytic enzyme(s) on dormant bacteria are stable for at least 1 day, more preferably for at least 2 days, and most preferably at least 3 days. The cellulolytic enzyme(s) comprise one or more enzymes selected from an endocellulase, an exocellulase, a beta-glucosidase (cellobiase), an oxidative cellulase, a xylanase, a hemicellulase, a lichenase, a chitenase, and a cellulose phosphorylase. Cellulolytic enzymes are present forming a minicellulosome, where the minicellulosome comprises at least 2 or 3 different enzymes. The minicellulosome comprises at least one endoglucanase or at least one exoglucanase. The minicellulsome comprises at least two endoglucanases and at least one exoglucanase. The minicellulosome comprises C. cellulolyticum endoglucanase Cel5A, C. cellulolyticum endoglucanase Cel48F, and C. cellulolyticum exoglucanase Cel9E. The Gram-positive bacterium comprises a Gram-positive bacterium that encodes a sortase. The Gram-positive bacterium comprises a Gram-positive bacillus, where the Gram-positive bacterium comprises a genus selected from Corynebacterium, Clostridium, Listeria, and Bacillus. The bacterium is a C. acetobutylicum. The Gram-positive bacterium is B. subtilis or thermophilic Geobacillus spp.. The Gram-positive bacterium comprises a Gram-positive coccus, where the bacterium is selected from Staphylococcus aureus, Staphylococcus epidermis, and Staphylococcus saprophyticus. Preferred Vector: The promoter is a constitutive promoter or an inducible promoter. The promoter is endogenous to a Gram-positive bacterium. The promoter is endogenous to the bacterium into which the vector is to be placed. Preferred Method: In the method of degrading cellulosic biomass into fermentable sugars, the contacting comprises contacting dormant bacteria to the cellulosic biomass. The contacting comprises culturing the bacteria with the cellulosic biomass. The cellulosic biomass comprise one or more materials selected from an agricultural plant waste (e.g., con stover, cereal straw, sugarcane bagasse), a plant waste from an industrial process (e.g., sawdust, paper pulp), and a non-food energy crop (e.g., switchgrass). The cellulosic biomass comprises one or more materials selected from grasses, rice hulls, bagasse, jute, hemp, flax, bamboo, sisal, abaca, straw, corn cobs, con stover, alfalfa, hay, coconut hair, seaweed, and algae. In the method of identifying cellulolytic enzyme combinations that enhance degradation of a particular substrate, or identifying cellulolytic enzyme variants that enhance degradation of a particular substrate, the cellulolytic enzyme(s) and/or the cellulolytic enzyme variants comprise a mutant cellulolytic enzyme. The mutant cellulolytic enzyme comprises a mutant cellulase. The selecting comprises selecting bacteria that show improved growth on the substrate. EXAMPLE - No suitable example given.