MULTISPECIES: outer membrane protein assembly factor BamB [Stenotrophomonas]
PQQ-binding-like beta-propeller repeat protein( domain architecture ID 11445572)
PQQ (pyrrolo-quinoline quinone)-like beta-propeller repeat protein contains several instances of a beta-propeller repeat; similar to Bacillus subtilis protein YxaL
List of domain hits
Name | Accession | Description | Interval | E-value | ||||||
PQQ | COG1520 | Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell ... |
42-400 | 1.27e-153 | ||||||
Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell wall/membrane/envelope biogenesis]; : Pssm-ID: 441129 [Multi-domain] Cd Length: 370 Bit Score: 438.48 E-value: 1.27e-153
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Name | Accession | Description | Interval | E-value | ||||||
PQQ | COG1520 | Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell ... |
42-400 | 1.27e-153 | ||||||
Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 441129 [Multi-domain] Cd Length: 370 Bit Score: 438.48 E-value: 1.27e-153
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assembly_YfgL | TIGR03300 | outer membrane assembly lipoprotein YfgL; Members of this protein family are YfgL, a ... |
9-399 | 2.86e-143 | ||||||
outer membrane assembly lipoprotein YfgL; Members of this protein family are YfgL, a lipoprotein component of a complex that acts protein insertion into the bacterial outer membrane. Other members of this complex are NlpB, YfiO, and YaeT. This protein contains multiple copies of a repeat that, in other contexts, are associated with binding of the coenzyme PQQ. [Protein fate, Protein and peptide secretion and trafficking] Pssm-ID: 274511 [Multi-domain] Cd Length: 377 Bit Score: 412.40 E-value: 2.86e-143
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BamB_YfgL | cd10276 | Beta-barrel assembly machinery (Bam) complex component B and related proteins; BamB (YflG) is ... |
42-400 | 4.06e-106 | ||||||
Beta-barrel assembly machinery (Bam) complex component B and related proteins; BamB (YflG) is a non-essential component of the beta-barrel assembly machinery (Bam), a multi-subunit complex that inserts proteins with beta-barrel topology into the outer membrane. BamB has been found to interact with BamA, which in turn binds and stabilizes pre-folded beta-barrel proteins; it has been suggested that BamB participates in the stabilization. Pssm-ID: 199834 [Multi-domain] Cd Length: 358 Bit Score: 316.97 E-value: 4.06e-106
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PRK11138 | PRK11138 | outer membrane biogenesis protein BamB; Provisional |
44-400 | 2.63e-102 | ||||||
outer membrane biogenesis protein BamB; Provisional Pssm-ID: 236857 [Multi-domain] Cd Length: 394 Bit Score: 308.40 E-value: 2.63e-102
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PQQ_2 | pfam13360 | PQQ-like domain; This domain contains several repeats of the PQQ repeat. |
90-327 | 1.57e-54 | ||||||
PQQ-like domain; This domain contains several repeats of the PQQ repeat. Pssm-ID: 433144 [Multi-domain] Cd Length: 233 Bit Score: 180.29 E-value: 1.57e-54
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PQQ | smart00564 | beta-propeller repeat; Beta-propeller repeat occurring in enzymes with pyrrolo-quinoline ... |
123-152 | 1.72e-03 | ||||||
beta-propeller repeat; Beta-propeller repeat occurring in enzymes with pyrrolo-quinoline quinone (PQQ) as cofactor, in Ire1p-like Ser/Thr kinases, and in prokaryotic dehydrogenases. Pssm-ID: 128836 [Multi-domain] Cd Length: 33 Bit Score: 35.59 E-value: 1.72e-03
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Name | Accession | Description | Interval | E-value | ||||||
PQQ | COG1520 | Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell ... |
42-400 | 1.27e-153 | ||||||
Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 441129 [Multi-domain] Cd Length: 370 Bit Score: 438.48 E-value: 1.27e-153
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assembly_YfgL | TIGR03300 | outer membrane assembly lipoprotein YfgL; Members of this protein family are YfgL, a ... |
9-399 | 2.86e-143 | ||||||
outer membrane assembly lipoprotein YfgL; Members of this protein family are YfgL, a lipoprotein component of a complex that acts protein insertion into the bacterial outer membrane. Other members of this complex are NlpB, YfiO, and YaeT. This protein contains multiple copies of a repeat that, in other contexts, are associated with binding of the coenzyme PQQ. [Protein fate, Protein and peptide secretion and trafficking] Pssm-ID: 274511 [Multi-domain] Cd Length: 377 Bit Score: 412.40 E-value: 2.86e-143
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BamB_YfgL | cd10276 | Beta-barrel assembly machinery (Bam) complex component B and related proteins; BamB (YflG) is ... |
42-400 | 4.06e-106 | ||||||
Beta-barrel assembly machinery (Bam) complex component B and related proteins; BamB (YflG) is a non-essential component of the beta-barrel assembly machinery (Bam), a multi-subunit complex that inserts proteins with beta-barrel topology into the outer membrane. BamB has been found to interact with BamA, which in turn binds and stabilizes pre-folded beta-barrel proteins; it has been suggested that BamB participates in the stabilization. Pssm-ID: 199834 [Multi-domain] Cd Length: 358 Bit Score: 316.97 E-value: 4.06e-106
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PRK11138 | PRK11138 | outer membrane biogenesis protein BamB; Provisional |
44-400 | 2.63e-102 | ||||||
outer membrane biogenesis protein BamB; Provisional Pssm-ID: 236857 [Multi-domain] Cd Length: 394 Bit Score: 308.40 E-value: 2.63e-102
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PQQ_2 | pfam13360 | PQQ-like domain; This domain contains several repeats of the PQQ repeat. |
90-327 | 1.57e-54 | ||||||
PQQ-like domain; This domain contains several repeats of the PQQ repeat. Pssm-ID: 433144 [Multi-domain] Cd Length: 233 Bit Score: 180.29 E-value: 1.57e-54
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PQQ_DH_like | cd00216 | PQQ-dependent dehydrogenases and related proteins; This family is composed of dehydrogenases ... |
58-383 | 9.55e-19 | ||||||
PQQ-dependent dehydrogenases and related proteins; This family is composed of dehydrogenases with pyrroloquinoline quinone (PQQ) as a cofactor, such as ethanol, methanol, and membrane-bound glucose dehydrogenases. The alignment model contains an 8-bladed beta-propeller, and the family also includes distantly related proteins which are not enzymatically active and do not bind PQQ. Pssm-ID: 199833 [Multi-domain] Cd Length: 434 Bit Score: 87.66 E-value: 9.55e-19
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PQQ_2 | pfam13360 | PQQ-like domain; This domain contains several repeats of the PQQ repeat. |
220-402 | 1.46e-15 | ||||||
PQQ-like domain; This domain contains several repeats of the PQQ repeat. Pssm-ID: 433144 [Multi-domain] Cd Length: 233 Bit Score: 75.52 E-value: 1.46e-15
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Gcd | COG4993 | Glucose dehydrogenase, PQQ-dependent [Carbohydrate transport and metabolism]; |
58-191 | 1.64e-14 | ||||||
Glucose dehydrogenase, PQQ-dependent [Carbohydrate transport and metabolism]; Pssm-ID: 444017 [Multi-domain] Cd Length: 515 Bit Score: 74.81 E-value: 1.64e-14
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PQQ | COG1520 | Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell ... |
284-402 | 2.04e-14 | ||||||
Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 441129 [Multi-domain] Cd Length: 370 Bit Score: 74.08 E-value: 2.04e-14
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assembly_YfgL | TIGR03300 | outer membrane assembly lipoprotein YfgL; Members of this protein family are YfgL, a ... |
282-402 | 2.70e-14 | ||||||
outer membrane assembly lipoprotein YfgL; Members of this protein family are YfgL, a lipoprotein component of a complex that acts protein insertion into the bacterial outer membrane. Other members of this complex are NlpB, YfiO, and YaeT. This protein contains multiple copies of a repeat that, in other contexts, are associated with binding of the coenzyme PQQ. [Protein fate, Protein and peptide secretion and trafficking] Pssm-ID: 274511 [Multi-domain] Cd Length: 377 Bit Score: 73.81 E-value: 2.70e-14
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PQQ_ADH_II | cd10279 | PQQ_like domain of the quinohemoprotein alcohol dehydrogenase (type II); This family of ... |
58-191 | 8.32e-12 | ||||||
PQQ_like domain of the quinohemoprotein alcohol dehydrogenase (type II); This family of monomeric and soluble type II alcohol dehydrogenases utilizes pyrroloquinoline quinone (PQQ) as a cofactor and is related to ethanol, methanol, and membrane-bound glucose dehydrogenases. The alignment model contains an 8-bladed beta-propeller. Pssm-ID: 199837 [Multi-domain] Cd Length: 549 Bit Score: 66.51 E-value: 8.32e-12
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PQQ_ADH_I | cd10277 | Ethanol dehydrogenase, a bacterial quinoprotein (PQQ-dependent type I alcohol dehydrogenase); ... |
58-191 | 1.06e-11 | ||||||
Ethanol dehydrogenase, a bacterial quinoprotein (PQQ-dependent type I alcohol dehydrogenase); This bacterial family of homodimeric ethanol dehydrogenases utilize pyrroloquinoline quinone (PQQ) as a cofactor. It represents proteins whose expression may be induced by ethanol, and which are similar to quinoprotein methanol dehydrogenases, but have higher specificities for ethanol and other primary and secondary alcohols. Dehydrogenases with PQQ cofactors, such as ethanol, methanol, and membrane-bound glucose dehydrogenases, form an 8-bladed beta-propeller. Pssm-ID: 199835 [Multi-domain] Cd Length: 529 Bit Score: 66.17 E-value: 1.06e-11
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PQQ_2 | pfam13360 | PQQ-like domain; This domain contains several repeats of the PQQ repeat. |
56-191 | 4.81e-09 | ||||||
PQQ-like domain; This domain contains several repeats of the PQQ repeat. Pssm-ID: 433144 [Multi-domain] Cd Length: 233 Bit Score: 56.26 E-value: 4.81e-09
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Gcd | COG4993 | Glucose dehydrogenase, PQQ-dependent [Carbohydrate transport and metabolism]; |
89-165 | 3.51e-07 | ||||||
Glucose dehydrogenase, PQQ-dependent [Carbohydrate transport and metabolism]; Pssm-ID: 444017 [Multi-domain] Cd Length: 515 Bit Score: 52.08 E-value: 3.51e-07
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PQQ_MDH | cd10278 | Large subunit of methanol dehydrogenase (moxF); Methanol dehydrogenase is a key enzyme in the ... |
122-191 | 1.12e-06 | ||||||
Large subunit of methanol dehydrogenase (moxF); Methanol dehydrogenase is a key enzyme in the utilization of C1 compounds as a source of energy and carbon by bacteria. It catalyzes the oxidation of methanol to formaldehyde, transfering two electrons per methanol to cytochrome c(L) as the acceptor. Methanol dehydrogenase belongs to a family of dehydrogenases with pyrroloquinoline quinone (PQQ) as cofactor, which also includes dehydrogenases specific to other alcohols and membrane-bound glucose dehydrogenases. This alignment model for the large subunit contains an 8-bladed beta-propeller; the functional enzyme forms a heterotetramer composed of two large and two small subunits. Pssm-ID: 199836 [Multi-domain] Cd Length: 553 Bit Score: 50.40 E-value: 1.12e-06
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PQQ_ADH_II | cd10279 | PQQ_like domain of the quinohemoprotein alcohol dehydrogenase (type II); This family of ... |
248-367 | 1.69e-06 | ||||||
PQQ_like domain of the quinohemoprotein alcohol dehydrogenase (type II); This family of monomeric and soluble type II alcohol dehydrogenases utilizes pyrroloquinoline quinone (PQQ) as a cofactor and is related to ethanol, methanol, and membrane-bound glucose dehydrogenases. The alignment model contains an 8-bladed beta-propeller. Pssm-ID: 199837 [Multi-domain] Cd Length: 549 Bit Score: 49.95 E-value: 1.69e-06
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PQQ | pfam01011 | PQQ enzyme repeat; The family represent a single repeat of a beta propeller. This propeller ... |
128-163 | 6.85e-06 | ||||||
PQQ enzyme repeat; The family represent a single repeat of a beta propeller. This propeller has been found in several enzymes which utilize pyrrolo-quinoline quinone as a prosthetic group. Pssm-ID: 395799 [Multi-domain] Cd Length: 36 Bit Score: 42.56 E-value: 6.85e-06
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PQQ_ADH_I | cd10277 | Ethanol dehydrogenase, a bacterial quinoprotein (PQQ-dependent type I alcohol dehydrogenase); ... |
256-328 | 8.99e-06 | ||||||
Ethanol dehydrogenase, a bacterial quinoprotein (PQQ-dependent type I alcohol dehydrogenase); This bacterial family of homodimeric ethanol dehydrogenases utilize pyrroloquinoline quinone (PQQ) as a cofactor. It represents proteins whose expression may be induced by ethanol, and which are similar to quinoprotein methanol dehydrogenases, but have higher specificities for ethanol and other primary and secondary alcohols. Dehydrogenases with PQQ cofactors, such as ethanol, methanol, and membrane-bound glucose dehydrogenases, form an 8-bladed beta-propeller. Pssm-ID: 199835 [Multi-domain] Cd Length: 529 Bit Score: 47.68 E-value: 8.99e-06
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PQQ_ADH_II | cd10279 | PQQ_like domain of the quinohemoprotein alcohol dehydrogenase (type II); This family of ... |
72-152 | 1.98e-05 | ||||||
PQQ_like domain of the quinohemoprotein alcohol dehydrogenase (type II); This family of monomeric and soluble type II alcohol dehydrogenases utilizes pyrroloquinoline quinone (PQQ) as a cofactor and is related to ethanol, methanol, and membrane-bound glucose dehydrogenases. The alignment model contains an 8-bladed beta-propeller. Pssm-ID: 199837 [Multi-domain] Cd Length: 549 Bit Score: 46.48 E-value: 1.98e-05
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Gcd | COG4993 | Glucose dehydrogenase, PQQ-dependent [Carbohydrate transport and metabolism]; |
137-191 | 1.99e-05 | ||||||
Glucose dehydrogenase, PQQ-dependent [Carbohydrate transport and metabolism]; Pssm-ID: 444017 [Multi-domain] Cd Length: 515 Bit Score: 46.69 E-value: 1.99e-05
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PQQ_ADH_I | cd10277 | Ethanol dehydrogenase, a bacterial quinoprotein (PQQ-dependent type I alcohol dehydrogenase); ... |
89-163 | 2.31e-05 | ||||||
Ethanol dehydrogenase, a bacterial quinoprotein (PQQ-dependent type I alcohol dehydrogenase); This bacterial family of homodimeric ethanol dehydrogenases utilize pyrroloquinoline quinone (PQQ) as a cofactor. It represents proteins whose expression may be induced by ethanol, and which are similar to quinoprotein methanol dehydrogenases, but have higher specificities for ethanol and other primary and secondary alcohols. Dehydrogenases with PQQ cofactors, such as ethanol, methanol, and membrane-bound glucose dehydrogenases, form an 8-bladed beta-propeller. Pssm-ID: 199835 [Multi-domain] Cd Length: 529 Bit Score: 46.52 E-value: 2.31e-05
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Gcd | COG4993 | Glucose dehydrogenase, PQQ-dependent [Carbohydrate transport and metabolism]; |
177-243 | 2.50e-05 | ||||||
Glucose dehydrogenase, PQQ-dependent [Carbohydrate transport and metabolism]; Pssm-ID: 444017 [Multi-domain] Cd Length: 515 Bit Score: 46.30 E-value: 2.50e-05
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PQQ_3 | pfam13570 | PQQ-like domain; |
147-182 | 2.69e-05 | ||||||
PQQ-like domain; Pssm-ID: 463925 [Multi-domain] Cd Length: 36 Bit Score: 41.03 E-value: 2.69e-05
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PQQ_ADH_I | cd10277 | Ethanol dehydrogenase, a bacterial quinoprotein (PQQ-dependent type I alcohol dehydrogenase); ... |
177-243 | 9.37e-05 | ||||||
Ethanol dehydrogenase, a bacterial quinoprotein (PQQ-dependent type I alcohol dehydrogenase); This bacterial family of homodimeric ethanol dehydrogenases utilize pyrroloquinoline quinone (PQQ) as a cofactor. It represents proteins whose expression may be induced by ethanol, and which are similar to quinoprotein methanol dehydrogenases, but have higher specificities for ethanol and other primary and secondary alcohols. Dehydrogenases with PQQ cofactors, such as ethanol, methanol, and membrane-bound glucose dehydrogenases, form an 8-bladed beta-propeller. Pssm-ID: 199835 [Multi-domain] Cd Length: 529 Bit Score: 44.60 E-value: 9.37e-05
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PQQ_MDH | cd10278 | Large subunit of methanol dehydrogenase (moxF); Methanol dehydrogenase is a key enzyme in the ... |
72-153 | 2.66e-04 | ||||||
Large subunit of methanol dehydrogenase (moxF); Methanol dehydrogenase is a key enzyme in the utilization of C1 compounds as a source of energy and carbon by bacteria. It catalyzes the oxidation of methanol to formaldehyde, transfering two electrons per methanol to cytochrome c(L) as the acceptor. Methanol dehydrogenase belongs to a family of dehydrogenases with pyrroloquinoline quinone (PQQ) as cofactor, which also includes dehydrogenases specific to other alcohols and membrane-bound glucose dehydrogenases. This alignment model for the large subunit contains an 8-bladed beta-propeller; the functional enzyme forms a heterotetramer composed of two large and two small subunits. Pssm-ID: 199836 [Multi-domain] Cd Length: 553 Bit Score: 43.08 E-value: 2.66e-04
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PQQ_MDH | cd10278 | Large subunit of methanol dehydrogenase (moxF); Methanol dehydrogenase is a key enzyme in the ... |
257-372 | 3.55e-04 | ||||||
Large subunit of methanol dehydrogenase (moxF); Methanol dehydrogenase is a key enzyme in the utilization of C1 compounds as a source of energy and carbon by bacteria. It catalyzes the oxidation of methanol to formaldehyde, transfering two electrons per methanol to cytochrome c(L) as the acceptor. Methanol dehydrogenase belongs to a family of dehydrogenases with pyrroloquinoline quinone (PQQ) as cofactor, which also includes dehydrogenases specific to other alcohols and membrane-bound glucose dehydrogenases. This alignment model for the large subunit contains an 8-bladed beta-propeller; the functional enzyme forms a heterotetramer composed of two large and two small subunits. Pssm-ID: 199836 [Multi-domain] Cd Length: 553 Bit Score: 42.70 E-value: 3.55e-04
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PQQ_MDH | cd10278 | Large subunit of methanol dehydrogenase (moxF); Methanol dehydrogenase is a key enzyme in the ... |
89-163 | 7.52e-04 | ||||||
Large subunit of methanol dehydrogenase (moxF); Methanol dehydrogenase is a key enzyme in the utilization of C1 compounds as a source of energy and carbon by bacteria. It catalyzes the oxidation of methanol to formaldehyde, transfering two electrons per methanol to cytochrome c(L) as the acceptor. Methanol dehydrogenase belongs to a family of dehydrogenases with pyrroloquinoline quinone (PQQ) as cofactor, which also includes dehydrogenases specific to other alcohols and membrane-bound glucose dehydrogenases. This alignment model for the large subunit contains an 8-bladed beta-propeller; the functional enzyme forms a heterotetramer composed of two large and two small subunits. Pssm-ID: 199836 [Multi-domain] Cd Length: 553 Bit Score: 41.54 E-value: 7.52e-04
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PQQ | smart00564 | beta-propeller repeat; Beta-propeller repeat occurring in enzymes with pyrrolo-quinoline ... |
123-152 | 1.72e-03 | ||||||
beta-propeller repeat; Beta-propeller repeat occurring in enzymes with pyrrolo-quinoline quinone (PQQ) as cofactor, in Ire1p-like Ser/Thr kinases, and in prokaryotic dehydrogenases. Pssm-ID: 128836 [Multi-domain] Cd Length: 33 Bit Score: 35.59 E-value: 1.72e-03
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PQQ | smart00564 | beta-propeller repeat; Beta-propeller repeat occurring in enzymes with pyrrolo-quinoline ... |
76-105 | 2.42e-03 | ||||||
beta-propeller repeat; Beta-propeller repeat occurring in enzymes with pyrrolo-quinoline quinone (PQQ) as cofactor, in Ire1p-like Ser/Thr kinases, and in prokaryotic dehydrogenases. Pssm-ID: 128836 [Multi-domain] Cd Length: 33 Bit Score: 35.20 E-value: 2.42e-03
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PQQ_mGDH | cd10280 | Membrane-bound PQQ-dependent glucose dehydrogenase; This bacterial subfamily of enzymes ... |
90-168 | 2.65e-03 | ||||||
Membrane-bound PQQ-dependent glucose dehydrogenase; This bacterial subfamily of enzymes belongs to the dehydrogenase family with pyrroloquinoline quinone (PQQ) as cofactor, and is the only subfamily that is bound to the membrane. Glucose dehydrogenase converts D-glucose to D-glucono-1,5-lactone in a reaction that is coupled with the respiratory chain in the periplasmic oxidation of sugars and alcohols in gram-negative bacteria. Ubiquinone functions as the electron acceptor. The alignment model contains an 8-bladed beta-propeller. Pssm-ID: 199838 [Multi-domain] Cd Length: 616 Bit Score: 39.87 E-value: 2.65e-03
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Blast search parameters | ||||
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