Mbov_0121 family peptidase domain-containing ABC transporter [Metamycoplasma hominis]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||||||||
| SunT super family | cl34455 | ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
5-672 | 9.65e-42 | |||||||||||
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms]; The actual alignment was detected with superfamily member COG2274: Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 161.54 E-value: 9.65e-42
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| Name | Accession | Description | Interval | E-value | |||||||||||
| SunT | COG2274 | ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
5-672 | 9.65e-42 | |||||||||||
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms]; Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 161.54 E-value: 9.65e-42
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| Peptidase_C39 | pfam03412 | Peptidase C39 family; Lantibiotic and non-lantibiotic bacteriocins are synthesized as ... |
5-138 | 6.31e-15 | |||||||||||
Peptidase C39 family; Lantibiotic and non-lantibiotic bacteriocins are synthesized as precursor peptides containing N-terminal extensions (leader peptides) which are cleaved off during maturation. Most non-lantibiotics and also some lantibiotics have leader peptides of the so-called double-glycine type. These leader peptides share consensus sequences and also a common processing site with two conserved glycine residues in positions -1 and -2. The double- glycine-type leader peptides are unrelated to the N-terminal signal sequences which direct proteins across the cytoplasmic membrane via the sec pathway. Their processing sites are also different from typical signal peptidase cleavage sites, suggesting that a different processing enzyme is involved. Peptide bacteriocins are exported across the cytoplasmic membrane by a dedicated ATP-binding cassette (ABC) transporter. The ABC transporter is the maturation protease and its proteolytic domain resides in the N-terminal part of the protein. This peptidase domain is found in a wide range of ABC transporters, however the presumed catalytic cysteine and histidine are not conserved in all members of this family. Pssm-ID: 367483 [Multi-domain] Cd Length: 133 Bit Score: 71.87 E-value: 6.31e-15
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| Peptidase_C39B | cd02418 | A sub-family of peptidase family C39. Peptidase family C39 mostly contains ... |
5-138 | 1.32e-14 | |||||||||||
A sub-family of peptidase family C39. Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The cysteine peptidases in family C39 cleave the "double-glycine" leader peptides from the precursors of various bacteriocins (mostly non-lantibiotic). The cleavage is mediated by the transporter as part of the secretion process. Bacteriocins are antibiotic proteins secreted by some species of bacteria that inhibit the growth of other bacterial species. The bacteriocin is synthesized as a precursor with an N-terminal leader peptide, and processing involves removal of the leader peptide by cleavage at a Gly-Gly bond, followed by translocation of the mature bacteriocin across the cytoplasmic membrane. Most endopeptidases of family C39 are N-terminal domains in larger proteins (ABC transporters) that serve both functions. The proposed protease active site is conserved in this sub-family. Pssm-ID: 239099 [Multi-domain] Cd Length: 136 Bit Score: 71.09 E-value: 1.32e-14
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| PRK10790 | PRK10790 | SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
411-630 | 3.57e-08 | |||||||||||
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 56.65 E-value: 3.57e-08
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| 3a01208 | TIGR00958 | Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
478-672 | 2.23e-03 | |||||||||||
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 41.25 E-value: 2.23e-03
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| Name | Accession | Description | Interval | E-value | |||||||||||
| SunT | COG2274 | ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
5-672 | 9.65e-42 | |||||||||||
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms]; Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 161.54 E-value: 9.65e-42
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| MdlB | COG1132 | ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
150-627 | 5.59e-22 | |||||||||||
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 100.24 E-value: 5.59e-22
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| Peptidase_C39 | pfam03412 | Peptidase C39 family; Lantibiotic and non-lantibiotic bacteriocins are synthesized as ... |
5-138 | 6.31e-15 | |||||||||||
Peptidase C39 family; Lantibiotic and non-lantibiotic bacteriocins are synthesized as precursor peptides containing N-terminal extensions (leader peptides) which are cleaved off during maturation. Most non-lantibiotics and also some lantibiotics have leader peptides of the so-called double-glycine type. These leader peptides share consensus sequences and also a common processing site with two conserved glycine residues in positions -1 and -2. The double- glycine-type leader peptides are unrelated to the N-terminal signal sequences which direct proteins across the cytoplasmic membrane via the sec pathway. Their processing sites are also different from typical signal peptidase cleavage sites, suggesting that a different processing enzyme is involved. Peptide bacteriocins are exported across the cytoplasmic membrane by a dedicated ATP-binding cassette (ABC) transporter. The ABC transporter is the maturation protease and its proteolytic domain resides in the N-terminal part of the protein. This peptidase domain is found in a wide range of ABC transporters, however the presumed catalytic cysteine and histidine are not conserved in all members of this family. Pssm-ID: 367483 [Multi-domain] Cd Length: 133 Bit Score: 71.87 E-value: 6.31e-15
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| Peptidase_C39B | cd02418 | A sub-family of peptidase family C39. Peptidase family C39 mostly contains ... |
5-138 | 1.32e-14 | |||||||||||
A sub-family of peptidase family C39. Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The cysteine peptidases in family C39 cleave the "double-glycine" leader peptides from the precursors of various bacteriocins (mostly non-lantibiotic). The cleavage is mediated by the transporter as part of the secretion process. Bacteriocins are antibiotic proteins secreted by some species of bacteria that inhibit the growth of other bacterial species. The bacteriocin is synthesized as a precursor with an N-terminal leader peptide, and processing involves removal of the leader peptide by cleavage at a Gly-Gly bond, followed by translocation of the mature bacteriocin across the cytoplasmic membrane. Most endopeptidases of family C39 are N-terminal domains in larger proteins (ABC transporters) that serve both functions. The proposed protease active site is conserved in this sub-family. Pssm-ID: 239099 [Multi-domain] Cd Length: 136 Bit Score: 71.09 E-value: 1.32e-14
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| Peptidase_C39E | cd02424 | A sub-family of peptidase family C39. Peptidase family C39 mostly contains ... |
1-132 | 4.11e-14 | |||||||||||
A sub-family of peptidase family C39. Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The cysteine peptidases in family C39 cleave the "double-glycine" leader peptides from the precursors of various bacteriocins (mostly non-lantibiotic). The cleavage is mediated by the transporter as part of the secretion process. Bacteriocins are antibiotic proteins secreted by some species of bacteria that inhibit the growth of other bacterial species. The bacteriocin is synthesized as a precursor with an N-terminal leader peptide, and processing involves removal of the leader peptide by cleavage at a Gly-Gly bond, followed by translocation of the mature bacteriocin across the cytoplasmic membrane. Most endopeptidases of family C39 are N-terminal domains in larger proteins (ABC transporters) that serve both functions. The proposed protease active site is conserved in this sub-family, which contains Colicin V perocessing peptidase. Pssm-ID: 239104 [Multi-domain] Cd Length: 129 Bit Score: 69.29 E-value: 4.11e-14
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| ABC_tran | pfam00005 | ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
482-627 | 3.68e-13 | |||||||||||
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains. Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 67.29 E-value: 3.68e-13
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| ABCC_MRP_domain2 | cd03244 | ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
455-626 | 1.77e-12 | |||||||||||
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate. Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 67.13 E-value: 1.77e-12
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| ABCC_Glucan_exporter_like | cd03254 | ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
479-672 | 2.40e-12 | |||||||||||
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins. Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 66.87 E-value: 2.40e-12
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| ABC_6TM_PCAT1_LagD_like | cd18570 | Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
156-432 | 6.00e-09 | |||||||||||
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins. Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 57.84 E-value: 6.00e-09
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| PRK10790 | PRK10790 | SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
411-630 | 3.57e-08 | |||||||||||
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 56.65 E-value: 3.57e-08
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| Peptidase_C39F | cd02425 | A sub-family of peptidase family C39. Peptidase family C39 mostly contains ... |
11-132 | 4.95e-08 | |||||||||||
A sub-family of peptidase family C39. Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The cysteine peptidases in family C39 cleave the "double-glycine" leader peptides from the precursors of various bacteriocins (mostly non-lantibiotic). The cleavage is mediated by the transporter as part of the secretion process. Bacteriocins are antibiotic proteins secreted by some species of bacteria that inhibit the growth of other bacterial species. The bacteriocin is synthesized as a precursor with an N-terminal leader peptide, and processing involves removal of the leader peptide by cleavage at a Gly-Gly bond, followed by translocation of the mature bacteriocin across the cytoplasmic membrane. Most endopeptidases of family C39 are N-terminal domains in larger proteins (ABC transporters) that serve both functions. The proposed protease active site is conserved in this sub-family. Pssm-ID: 239105 [Multi-domain] Cd Length: 126 Bit Score: 51.88 E-value: 4.95e-08
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| C39G | COG3271 | Predicted double-glycine leader peptidase, C39-like (CLD) domain [Intracellular trafficking, ... |
12-133 | 8.22e-08 | |||||||||||
Predicted double-glycine leader peptidase, C39-like (CLD) domain [Intracellular trafficking, secretion, and vesicular transport]; Pssm-ID: 442502 [Multi-domain] Cd Length: 179 Bit Score: 52.69 E-value: 8.22e-08
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| ABC_MTABC3_MDL1_MDL2 | cd03249 | ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
481-626 | 4.78e-07 | |||||||||||
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another. Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 51.39 E-value: 4.78e-07
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| ABCC_NFT1 | cd03369 | ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
481-672 | 6.56e-07 | |||||||||||
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate. Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 50.49 E-value: 6.56e-07
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| ABC_ATPase | cd00267 | ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
471-663 | 8.20e-07 | |||||||||||
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins. Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 49.17 E-value: 8.20e-07
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| Peptidase_C39G | cd02423 | A sub-family of peptidase family C39. Peptidase family C39 mostly contains ... |
25-133 | 6.40e-06 | |||||||||||
A sub-family of peptidase family C39. Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The cysteine peptidases in family C39 cleave the "double-glycine" leader peptides from the precursors of various bacteriocins (mostly non-lantibiotic). The cleavage is mediated by the transporter as part of the secretion process. Bacteriocins are antibiotic proteins secreted by some species of bacteria that inhibit the growth of other bacterial species. The bacteriocin is synthesized as a precursor with an N-terminal leader peptide, and processing involves removal of the leader peptide by cleavage at a Gly-Gly bond, followed by translocation of the mature bacteriocin across the cytoplasmic membrane. Most endopeptidases of family C39 are N-terminal domains in larger proteins (ABC transporters) that serve both functions. The proposed protease active site is conserved in this sub-family of proteins with a single peptidase domain, which are lacking the nucleotide-binding transporter signature. Pssm-ID: 239103 [Multi-domain] Cd Length: 129 Bit Score: 46.11 E-value: 6.40e-06
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| PRK11160 | PRK11160 | cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
480-628 | 8.60e-06 | |||||||||||
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 49.05 E-value: 8.60e-06
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| ABCC_MRP_domain1 | cd03250 | ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
467-627 | 3.32e-05 | |||||||||||
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate. Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 45.54 E-value: 3.32e-05
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| PhnK | COG1101 | ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
466-528 | 1.67e-04 | |||||||||||
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 43.92 E-value: 1.67e-04
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| PRK11174 | PRK11174 | cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
448-625 | 1.83e-04 | |||||||||||
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 44.45 E-value: 1.83e-04
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| ABC_Class3 | cd03229 | ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
467-528 | 2.86e-04 | |||||||||||
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins. Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 42.17 E-value: 2.86e-04
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| MK0520 | COG2401 | ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
471-625 | 3.78e-04 | |||||||||||
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only]; Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 42.25 E-value: 3.78e-04
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| ABC_YhbG | cd03218 | ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
476-657 | 4.44e-04 | |||||||||||
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium. Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 42.14 E-value: 4.44e-04
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| ABCF_EF-3 | cd03221 | ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
467-535 | 4.88e-04 | |||||||||||
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions. Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 40.89 E-value: 4.88e-04
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| ABC_FeS_Assembly | cd03217 | ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
469-532 | 1.36e-03 | |||||||||||
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet. Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 40.59 E-value: 1.36e-03
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| ABC_membrane | pfam00664 | ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
159-423 | 1.52e-03 | |||||||||||
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions. Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 41.09 E-value: 1.52e-03
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| potA | PRK09452 | spermidine/putrescine ABC transporter ATP-binding protein PotA; |
462-531 | 1.53e-03 | |||||||||||
spermidine/putrescine ABC transporter ATP-binding protein PotA; Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 41.47 E-value: 1.53e-03
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| ABC_6TM_T1SS_like | cd18555 | Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
156-437 | 2.06e-03 | |||||||||||
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides. Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 40.57 E-value: 2.06e-03
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| 3a01208 | TIGR00958 | Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
478-672 | 2.23e-03 | |||||||||||
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 41.25 E-value: 2.23e-03
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| PRK13540 | PRK13540 | cytochrome c biogenesis protein CcmA; Provisional |
467-625 | 7.86e-03 | |||||||||||
cytochrome c biogenesis protein CcmA; Provisional Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 38.39 E-value: 7.86e-03
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