P-aminobenzoyl-glutamate hydrolase, A subunit; Component of the p-aminobenzoyl-glutamate hydrolase multicomponent enzyme system which catalyzes the cleavage of p- aminobenzoyl-glutamate (PABA-GLU) to form p-aminobenzoate (PABA) and glutamate. AbgAB does not degrade dipeptides and the physiological role of abgABT should be clarified; Belongs to the peptidase M20 family.

P-aminobenzoyl-glutamate hydrolase, B subunit; Component of the p-aminobenzoyl-glutamate hydrolase multicomponent enzyme system which catalyzes the cleavage of p- aminobenzoyl-glutamate (PABA-GLU) to form p-aminobenzoate (PABA) and glutamate. AbgAB does not degrade dipeptides and the physiological role of abgABT should be clarified.

P-aminobenzoyl-glutamate hydrolase, B subunit; Component of the p-aminobenzoyl-glutamate hydrolase multicomponent enzyme system which catalyzes the cleavage of p- aminobenzoyl-glutamate (PABA-GLU) to form p-aminobenzoate (PABA) and glutamate. AbgAB does not degrade dipeptides and the physiological role of abgABT should be clarified.

P-aminobenzoyl-glutamate hydrolase, A subunit; Component of the p-aminobenzoyl-glutamate hydrolase multicomponent enzyme system which catalyzes the cleavage of p- aminobenzoyl-glutamate (PABA-GLU) to form p-aminobenzoate (PABA) and glutamate. AbgAB does not degrade dipeptides and the physiological role of abgABT should be clarified; Belongs to the peptidase M20 family.

Dimethyl sulfoxide reductase, anaerobic, subunit A; Catalyzes the reduction of dimethyl sulfoxide (DMSO) to dimethyl sulfide (DMS). DMSO reductase serves as the terminal reductase under anaerobic conditions, with DMSO being the terminal electron acceptor. Terminal reductase during anaerobic growth on various sulfoxides and N-oxide compounds. Allows E.coli to grow anaerobically on DMSO as respiratory oxidant.

Assembly protein for periplasmic nitrate reductase; Chaperone for NapA, the catalytic subunit of the periplasmic nitrate reductase. It binds directly and specifically to the twin- arginine signal peptide of NapA, preventing premature interaction with the Tat translocase and premature export. May have a role in the insertion of the NapA molybdenum cofactor.

Dimethyl sulfoxide reductase, anaerobic, subunit A; Catalyzes the reduction of dimethyl sulfoxide (DMSO) to dimethyl sulfide (DMS). DMSO reductase serves as the terminal reductase under anaerobic conditions, with DMSO being the terminal electron acceptor. Terminal reductase during anaerobic growth on various sulfoxides and N-oxide compounds. Allows E.coli to grow anaerobically on DMSO as respiratory oxidant.

Nitrate reductase 1, alpha subunit; The nitrate reductase enzyme complex allows E.coli to use nitrate as an electron acceptor during anaerobic growth. The alpha chain is the actual site of nitrate reduction.

Dimethyl sulfoxide reductase, anaerobic, subunit A; Catalyzes the reduction of dimethyl sulfoxide (DMSO) to dimethyl sulfide (DMS). DMSO reductase serves as the terminal reductase under anaerobic conditions, with DMSO being the terminal electron acceptor. Terminal reductase during anaerobic growth on various sulfoxides and N-oxide compounds. Allows E.coli to grow anaerobically on DMSO as respiratory oxidant.

Molybdenum-cofactor-assembly chaperone delta subunit of nitrate reductase 1; Chaperone required for proper molybdenum cofactor insertion and final assembly of the membrane-bound respiratory nitrate reductase 1. Required for the insertion of the molybdenum into the apo-NarG subunit, maybe by keeping NarG in an appropriate competent-open conformation for the molybdenum cofactor insertion to occur. NarJ maintains the apoNarGH complex in a soluble state. Upon insertion of the molybdenum cofactor, NarJ seems to dissociate from the activated soluble NarGH complex, before its association with [...]

Dimethyl sulfoxide reductase, anaerobic, subunit A; Catalyzes the reduction of dimethyl sulfoxide (DMSO) to dimethyl sulfide (DMS). DMSO reductase serves as the terminal reductase under anaerobic conditions, with DMSO being the terminal electron acceptor. Terminal reductase during anaerobic growth on various sulfoxides and N-oxide compounds. Allows E.coli to grow anaerobically on DMSO as respiratory oxidant.

TatABCE protein translocation system subunit; Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin- arginine motif in their signal peptide across membranes. Together with TatC, TatB is part of a receptor directly interacting with Tat signal peptides. TatB may form an oligomeric binding site that transiently accommodates folded Tat precursor proteins before their translocation.

Dimethyl sulfoxide reductase, anaerobic, subunit A; Catalyzes the reduction of dimethyl sulfoxide (DMSO) to dimethyl sulfide (DMS). DMSO reductase serves as the terminal reductase under anaerobic conditions, with DMSO being the terminal electron acceptor. Terminal reductase during anaerobic growth on various sulfoxides and N-oxide compounds. Allows E.coli to grow anaerobically on DMSO as respiratory oxidant.

TatABCE protein translocation system subunit; Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin- arginine motif in their signal peptide across membranes. Together with TatB, TatC is part of a receptor directly interacting with Tat signal peptides.

Dimethyl sulfoxide reductase, anaerobic, subunit A; Catalyzes the reduction of dimethyl sulfoxide (DMSO) to dimethyl sulfide (DMS). DMSO reductase serves as the terminal reductase under anaerobic conditions, with DMSO being the terminal electron acceptor. Terminal reductase during anaerobic growth on various sulfoxides and N-oxide compounds. Allows E.coli to grow anaerobically on DMSO as respiratory oxidant.

TorA-maturation chaperone; Involved in the biogenesis of TorA. Acts on TorA before the insertion of the molybdenum cofactor and, as a result, probably favors a conformation of the apoenzyme that is competent for acquiring the cofactor.

Assembly protein for periplasmic nitrate reductase; Chaperone for NapA, the catalytic subunit of the periplasmic nitrate reductase. It binds directly and specifically to the twin- arginine signal peptide of NapA, preventing premature interaction with the Tat translocase and premature export. May have a role in the insertion of the NapA molybdenum cofactor.

Dimethyl sulfoxide reductase, anaerobic, subunit A; Catalyzes the reduction of dimethyl sulfoxide (DMSO) to dimethyl sulfide (DMS). DMSO reductase serves as the terminal reductase under anaerobic conditions, with DMSO being the terminal electron acceptor. Terminal reductase during anaerobic growth on various sulfoxides and N-oxide compounds. Allows E.coli to grow anaerobically on DMSO as respiratory oxidant.

Assembly protein for periplasmic nitrate reductase; Chaperone for NapA, the catalytic subunit of the periplasmic nitrate reductase. It binds directly and specifically to the twin- arginine signal peptide of NapA, preventing premature interaction with the Tat translocase and premature export. May have a role in the insertion of the NapA molybdenum cofactor.

Nitrate reductase 1, alpha subunit; The nitrate reductase enzyme complex allows E.coli to use nitrate as an electron acceptor during anaerobic growth. The alpha chain is the actual site of nitrate reduction.

Assembly protein for periplasmic nitrate reductase; Chaperone for NapA, the catalytic subunit of the periplasmic nitrate reductase. It binds directly and specifically to the twin- arginine signal peptide of NapA, preventing premature interaction with the Tat translocase and premature export. May have a role in the insertion of the NapA molybdenum cofactor.

Molybdenum-cofactor-assembly chaperone delta subunit of nitrate reductase 1; Chaperone required for proper molybdenum cofactor insertion and final assembly of the membrane-bound respiratory nitrate reductase 1. Required for the insertion of the molybdenum into the apo-NarG subunit, maybe by keeping NarG in an appropriate competent-open conformation for the molybdenum cofactor insertion to occur. NarJ maintains the apoNarGH complex in a soluble state. Upon insertion of the molybdenum cofactor, NarJ seems to dissociate from the activated soluble NarGH complex, before its association with [...]

Assembly protein for periplasmic nitrate reductase; Chaperone for NapA, the catalytic subunit of the periplasmic nitrate reductase. It binds directly and specifically to the twin- arginine signal peptide of NapA, preventing premature interaction with the Tat translocase and premature export. May have a role in the insertion of the NapA molybdenum cofactor.

TorA-maturation chaperone; Involved in the biogenesis of TorA. Acts on TorA before the insertion of the molybdenum cofactor and, as a result, probably favors a conformation of the apoenzyme that is competent for acquiring the cofactor.

Nitrate reductase 1, alpha subunit; The nitrate reductase enzyme complex allows E.coli to use nitrate as an electron acceptor during anaerobic growth. The alpha chain is the actual site of nitrate reduction.

Dimethyl sulfoxide reductase, anaerobic, subunit A; Catalyzes the reduction of dimethyl sulfoxide (DMSO) to dimethyl sulfide (DMS). DMSO reductase serves as the terminal reductase under anaerobic conditions, with DMSO being the terminal electron acceptor. Terminal reductase during anaerobic growth on various sulfoxides and N-oxide compounds. Allows E.coli to grow anaerobically on DMSO as respiratory oxidant.

Nitrate reductase 1, alpha subunit; The nitrate reductase enzyme complex allows E.coli to use nitrate as an electron acceptor during anaerobic growth. The alpha chain is the actual site of nitrate reduction.

Assembly protein for periplasmic nitrate reductase; Chaperone for NapA, the catalytic subunit of the periplasmic nitrate reductase. It binds directly and specifically to the twin- arginine signal peptide of NapA, preventing premature interaction with the Tat translocase and premature export. May have a role in the insertion of the NapA molybdenum cofactor.

Nitrate reductase 1, alpha subunit; The nitrate reductase enzyme complex allows E.coli to use nitrate as an electron acceptor during anaerobic growth. The alpha chain is the actual site of nitrate reduction.

Molybdenum-cofactor-assembly chaperone delta subunit of nitrate reductase 1; Chaperone required for proper molybdenum cofactor insertion and final assembly of the membrane-bound respiratory nitrate reductase 1. Required for the insertion of the molybdenum into the apo-NarG subunit, maybe by keeping NarG in an appropriate competent-open conformation for the molybdenum cofactor insertion to occur. NarJ maintains the apoNarGH complex in a soluble state. Upon insertion of the molybdenum cofactor, NarJ seems to dissociate from the activated soluble NarGH complex, before its association with [...]

Nitrate reductase 1, alpha subunit; The nitrate reductase enzyme complex allows E.coli to use nitrate as an electron acceptor during anaerobic growth. The alpha chain is the actual site of nitrate reduction.

TorA-maturation chaperone; Involved in the biogenesis of TorA. Acts on TorA before the insertion of the molybdenum cofactor and, as a result, probably favors a conformation of the apoenzyme that is competent for acquiring the cofactor.

Molybdenum-cofactor-assembly chaperone delta subunit of nitrate reductase 1; Chaperone required for proper molybdenum cofactor insertion and final assembly of the membrane-bound respiratory nitrate reductase 1. Required for the insertion of the molybdenum into the apo-NarG subunit, maybe by keeping NarG in an appropriate competent-open conformation for the molybdenum cofactor insertion to occur. NarJ maintains the apoNarGH complex in a soluble state. Upon insertion of the molybdenum cofactor, NarJ seems to dissociate from the activated soluble NarGH complex, before its association with [...]

Dimethyl sulfoxide reductase, anaerobic, subunit A; Catalyzes the reduction of dimethyl sulfoxide (DMSO) to dimethyl sulfide (DMS). DMSO reductase serves as the terminal reductase under anaerobic conditions, with DMSO being the terminal electron acceptor. Terminal reductase during anaerobic growth on various sulfoxides and N-oxide compounds. Allows E.coli to grow anaerobically on DMSO as respiratory oxidant.

Molybdenum-cofactor-assembly chaperone delta subunit of nitrate reductase 1; Chaperone required for proper molybdenum cofactor insertion and final assembly of the membrane-bound respiratory nitrate reductase 1. Required for the insertion of the molybdenum into the apo-NarG subunit, maybe by keeping NarG in an appropriate competent-open conformation for the molybdenum cofactor insertion to occur. NarJ maintains the apoNarGH complex in a soluble state. Upon insertion of the molybdenum cofactor, NarJ seems to dissociate from the activated soluble NarGH complex, before its association with [...]

Assembly protein for periplasmic nitrate reductase; Chaperone for NapA, the catalytic subunit of the periplasmic nitrate reductase. It binds directly and specifically to the twin- arginine signal peptide of NapA, preventing premature interaction with the Tat translocase and premature export. May have a role in the insertion of the NapA molybdenum cofactor.

Molybdenum-cofactor-assembly chaperone delta subunit of nitrate reductase 1; Chaperone required for proper molybdenum cofactor insertion and final assembly of the membrane-bound respiratory nitrate reductase 1. Required for the insertion of the molybdenum into the apo-NarG subunit, maybe by keeping NarG in an appropriate competent-open conformation for the molybdenum cofactor insertion to occur. NarJ maintains the apoNarGH complex in a soluble state. Upon insertion of the molybdenum cofactor, NarJ seems to dissociate from the activated soluble NarGH complex, before its association with [...]

Nitrate reductase 1, alpha subunit; The nitrate reductase enzyme complex allows E.coli to use nitrate as an electron acceptor during anaerobic growth. The alpha chain is the actual site of nitrate reduction.

Molybdenum-cofactor-assembly chaperone delta subunit of nitrate reductase 1; Chaperone required for proper molybdenum cofactor insertion and final assembly of the membrane-bound respiratory nitrate reductase 1. Required for the insertion of the molybdenum into the apo-NarG subunit, maybe by keeping NarG in an appropriate competent-open conformation for the molybdenum cofactor insertion to occur. NarJ maintains the apoNarGH complex in a soluble state. Upon insertion of the molybdenum cofactor, NarJ seems to dissociate from the activated soluble NarGH complex, before its association with [...]

TorA-maturation chaperone; Involved in the biogenesis of TorA. Acts on TorA before the insertion of the molybdenum cofactor and, as a result, probably favors a conformation of the apoenzyme that is competent for acquiring the cofactor.