node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
CAZ94709.1 | CAZ94710.1 | ZOBELLIA_638 | ZOBELLIA_639 | OmpA-like outer membrane protein; This protein has a modular architecture with two N-terminal TPR repeats, a central beta-propeller domain, encompassing five WD40 repeats, and a C-terminal OmpA domain. OmpA-like domain is thought to be responsible for non-covalent interactions with peptidoglycan. The tetratrico peptide repeat (TPR) is a structural motif, which mediates proteinprotein interactions. Signal peptide cleaved between the residues 21 and 22; Localized in the outer membrane; Function unclear. | Conserved hypothetical protein; Contains a signal peptide cleaved between the residues 29 and 30; Localized in the periplasmic space. | 0.943 |
CAZ94709.1 | CAZ94711.1 | ZOBELLIA_638 | ZOBELLIA_640 | OmpA-like outer membrane protein; This protein has a modular architecture with two N-terminal TPR repeats, a central beta-propeller domain, encompassing five WD40 repeats, and a C-terminal OmpA domain. OmpA-like domain is thought to be responsible for non-covalent interactions with peptidoglycan. The tetratrico peptide repeat (TPR) is a structural motif, which mediates proteinprotein interactions. Signal peptide cleaved between the residues 21 and 22; Localized in the outer membrane; Function unclear. | Hypothetical membrane protein; Proteins that probably binds the calcium ions; Contains fifteen type-3 thrombospondin repeats; signal peptide cleaved between the residues 33 and 34; probably localized in the outer membrane; Hypothetical protein. | 0.835 |
CAZ94709.1 | CAZ95780.1 | ZOBELLIA_638 | ZOBELLIA_1727 | OmpA-like outer membrane protein; This protein has a modular architecture with two N-terminal TPR repeats, a central beta-propeller domain, encompassing five WD40 repeats, and a C-terminal OmpA domain. OmpA-like domain is thought to be responsible for non-covalent interactions with peptidoglycan. The tetratrico peptide repeat (TPR) is a structural motif, which mediates proteinprotein interactions. Signal peptide cleaved between the residues 21 and 22; Localized in the outer membrane; Function unclear. | OmpA-like outer membrane protein; This protein has a modular architecture with a N-terminal domain of unknown function, a central beta-propeller domain, encompassing three WD40 repeats, and a C-terminal OmpA domain. OmpA-like domains are thought to be responsible for non-covalent interactions with peptidoglycan. Contains a signal peptide cleaved between the residues 18 and 19; Localized in the outer membrane; Function unclear. | 0.411 |
CAZ94709.1 | CAZ96554.1 | ZOBELLIA_638 | ZOBELLIA_2401 | OmpA-like outer membrane protein; This protein has a modular architecture with two N-terminal TPR repeats, a central beta-propeller domain, encompassing five WD40 repeats, and a C-terminal OmpA domain. OmpA-like domain is thought to be responsible for non-covalent interactions with peptidoglycan. The tetratrico peptide repeat (TPR) is a structural motif, which mediates proteinprotein interactions. Signal peptide cleaved between the residues 21 and 22; Localized in the outer membrane; Function unclear. | Conserved hypothetical protein; Features a signal peptide cleaved between the residues 20 and 21; Localized in the periplasm. | 0.619 |
CAZ94709.1 | CAZ97221.1 | ZOBELLIA_638 | ZOBELLIA_3082 | OmpA-like outer membrane protein; This protein has a modular architecture with two N-terminal TPR repeats, a central beta-propeller domain, encompassing five WD40 repeats, and a C-terminal OmpA domain. OmpA-like domain is thought to be responsible for non-covalent interactions with peptidoglycan. The tetratrico peptide repeat (TPR) is a structural motif, which mediates proteinprotein interactions. Signal peptide cleaved between the residues 21 and 22; Localized in the outer membrane; Function unclear. | OmpA-like periplasmic protein; This protein has a modular architecture composed of a N-terminal TPR motif, a central beta-propeller domain, encompassing four WD40 repeats, and a C-terminal OmpA domain. OmpA-like domains are thought to be responsible for non-covalent interactions with peptidoglycan. The tetratrico peptide repeat (TPR) is a structural motif, which mediates proteinprotein interactions; Signal peptide cleaved between the residues 23 and 24; Localized in the periplasmic space and/or in the outer membrane; Family membership. | 0.416 |
CAZ94710.1 | CAZ94709.1 | ZOBELLIA_639 | ZOBELLIA_638 | Conserved hypothetical protein; Contains a signal peptide cleaved between the residues 29 and 30; Localized in the periplasmic space. | OmpA-like outer membrane protein; This protein has a modular architecture with two N-terminal TPR repeats, a central beta-propeller domain, encompassing five WD40 repeats, and a C-terminal OmpA domain. OmpA-like domain is thought to be responsible for non-covalent interactions with peptidoglycan. The tetratrico peptide repeat (TPR) is a structural motif, which mediates proteinprotein interactions. Signal peptide cleaved between the residues 21 and 22; Localized in the outer membrane; Function unclear. | 0.943 |
CAZ94710.1 | CAZ94711.1 | ZOBELLIA_639 | ZOBELLIA_640 | Conserved hypothetical protein; Contains a signal peptide cleaved between the residues 29 and 30; Localized in the periplasmic space. | Hypothetical membrane protein; Proteins that probably binds the calcium ions; Contains fifteen type-3 thrombospondin repeats; signal peptide cleaved between the residues 33 and 34; probably localized in the outer membrane; Hypothetical protein. | 0.834 |
CAZ94710.1 | CAZ95780.1 | ZOBELLIA_639 | ZOBELLIA_1727 | Conserved hypothetical protein; Contains a signal peptide cleaved between the residues 29 and 30; Localized in the periplasmic space. | OmpA-like outer membrane protein; This protein has a modular architecture with a N-terminal domain of unknown function, a central beta-propeller domain, encompassing three WD40 repeats, and a C-terminal OmpA domain. OmpA-like domains are thought to be responsible for non-covalent interactions with peptidoglycan. Contains a signal peptide cleaved between the residues 18 and 19; Localized in the outer membrane; Function unclear. | 0.771 |
CAZ94710.1 | CAZ96554.1 | ZOBELLIA_639 | ZOBELLIA_2401 | Conserved hypothetical protein; Contains a signal peptide cleaved between the residues 29 and 30; Localized in the periplasmic space. | Conserved hypothetical protein; Features a signal peptide cleaved between the residues 20 and 21; Localized in the periplasm. | 0.751 |
CAZ94710.1 | CAZ96634.1 | ZOBELLIA_639 | ZOBELLIA_2484 | Conserved hypothetical protein; Contains a signal peptide cleaved between the residues 29 and 30; Localized in the periplasmic space. | Modular protein consisting of a N-terminal domain of unknown function, a central beta-propeller domain, encompassing four WD40 repeats, and a C-terminal OmpA domain. OmpA-like domains are thought to be responsible for non-covalent interactions with peptidoglycan; Signal peptide cleaved between the residues 19 and 20; Localized in the periplasmic space or outer membrane; Function unclear. | 0.757 |
CAZ94710.1 | CAZ97040.1 | ZOBELLIA_639 | ZOBELLIA_2893 | Conserved hypothetical protein; Contains a signal peptide cleaved between the residues 29 and 30; Localized in the periplasmic space. | OmpA-like periplasmic protein; This protein has a modular architecture consisting of a N-terminal TPR motif, a central beta-propeller domain, encompassing three WD40 repeats, and a C-terminal OmpA domain. OmpA-like domains are thought to be responsible for non-covalent interactions with peptidoglycan. The tetratrico peptide repeat (TPR) is a structural motif, which mediates proteinprotein interactions; Signal peptide cleaved between the residues 23 and 24; localized in the periplasmic space and/or outer membrane; Family membership. | 0.769 |
CAZ94710.1 | CAZ97221.1 | ZOBELLIA_639 | ZOBELLIA_3082 | Conserved hypothetical protein; Contains a signal peptide cleaved between the residues 29 and 30; Localized in the periplasmic space. | OmpA-like periplasmic protein; This protein has a modular architecture composed of a N-terminal TPR motif, a central beta-propeller domain, encompassing four WD40 repeats, and a C-terminal OmpA domain. OmpA-like domains are thought to be responsible for non-covalent interactions with peptidoglycan. The tetratrico peptide repeat (TPR) is a structural motif, which mediates proteinprotein interactions; Signal peptide cleaved between the residues 23 and 24; Localized in the periplasmic space and/or in the outer membrane; Family membership. | 0.760 |
CAZ94710.1 | CAZ97787.1 | ZOBELLIA_639 | ZOBELLIA_3649 | Conserved hypothetical protein; Contains a signal peptide cleaved between the residues 29 and 30; Localized in the periplasmic space. | OmpA-like periplasmic protein; This protein has a modular architecture with a N-terminal TPR motif, a central beta-propeller domain, encompassing three WD40 repeats, and a C-terminal OmpA domain. OmpA-like domains are thought to be responsible for non-covalent interactions with peptidoglycan; Signal peptide cleaved between the residues 20 and 21; localized in the periplasmic space and/or in the outer membrane; Family membership. | 0.775 |
CAZ94710.1 | CAZ97790.1 | ZOBELLIA_639 | ZOBELLIA_3652 | Conserved hypothetical protein; Contains a signal peptide cleaved between the residues 29 and 30; Localized in the periplasmic space. | OmpA-like periplasmic protein; This protein has a modular architecture with a N-terminal TPR motif, a central beta-propeller domain, encompassing three WD40 repeats, and a C-terminal OmpA domain. OmpA-like domains are thought to be responsible for non-covalent interactions with peptidoglycan. The tetratrico peptide repeat (TPR) is a structural motif, which mediates proteinprotein interactions; Signal peptide cleaved between the residues 20 and 21; Localized in the outer membrane and/or periplasmic space; Family membership. | 0.775 |
CAZ94710.1 | CAZ98770.1 | ZOBELLIA_639 | ZOBELLIA_4635 | Conserved hypothetical protein; Contains a signal peptide cleaved between the residues 29 and 30; Localized in the periplasmic space. | Protein belonging to the OmpA family. OmpA-like domains are thought to be responsible for non-covalent interactions with peptidoglycan; Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 16 and 17; Localized in the outer membrane; Family membership. | 0.756 |
CAZ94711.1 | CAZ94709.1 | ZOBELLIA_640 | ZOBELLIA_638 | Hypothetical membrane protein; Proteins that probably binds the calcium ions; Contains fifteen type-3 thrombospondin repeats; signal peptide cleaved between the residues 33 and 34; probably localized in the outer membrane; Hypothetical protein. | OmpA-like outer membrane protein; This protein has a modular architecture with two N-terminal TPR repeats, a central beta-propeller domain, encompassing five WD40 repeats, and a C-terminal OmpA domain. OmpA-like domain is thought to be responsible for non-covalent interactions with peptidoglycan. The tetratrico peptide repeat (TPR) is a structural motif, which mediates proteinprotein interactions. Signal peptide cleaved between the residues 21 and 22; Localized in the outer membrane; Function unclear. | 0.835 |
CAZ94711.1 | CAZ94710.1 | ZOBELLIA_640 | ZOBELLIA_639 | Hypothetical membrane protein; Proteins that probably binds the calcium ions; Contains fifteen type-3 thrombospondin repeats; signal peptide cleaved between the residues 33 and 34; probably localized in the outer membrane; Hypothetical protein. | Conserved hypothetical protein; Contains a signal peptide cleaved between the residues 29 and 30; Localized in the periplasmic space. | 0.834 |
CAZ94711.1 | CAZ95780.1 | ZOBELLIA_640 | ZOBELLIA_1727 | Hypothetical membrane protein; Proteins that probably binds the calcium ions; Contains fifteen type-3 thrombospondin repeats; signal peptide cleaved between the residues 33 and 34; probably localized in the outer membrane; Hypothetical protein. | OmpA-like outer membrane protein; This protein has a modular architecture with a N-terminal domain of unknown function, a central beta-propeller domain, encompassing three WD40 repeats, and a C-terminal OmpA domain. OmpA-like domains are thought to be responsible for non-covalent interactions with peptidoglycan. Contains a signal peptide cleaved between the residues 18 and 19; Localized in the outer membrane; Function unclear. | 0.570 |
CAZ94711.1 | CAZ98770.1 | ZOBELLIA_640 | ZOBELLIA_4635 | Hypothetical membrane protein; Proteins that probably binds the calcium ions; Contains fifteen type-3 thrombospondin repeats; signal peptide cleaved between the residues 33 and 34; probably localized in the outer membrane; Hypothetical protein. | Protein belonging to the OmpA family. OmpA-like domains are thought to be responsible for non-covalent interactions with peptidoglycan; Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 16 and 17; Localized in the outer membrane; Family membership. | 0.592 |
CAZ95780.1 | CAZ94709.1 | ZOBELLIA_1727 | ZOBELLIA_638 | OmpA-like outer membrane protein; This protein has a modular architecture with a N-terminal domain of unknown function, a central beta-propeller domain, encompassing three WD40 repeats, and a C-terminal OmpA domain. OmpA-like domains are thought to be responsible for non-covalent interactions with peptidoglycan. Contains a signal peptide cleaved between the residues 18 and 19; Localized in the outer membrane; Function unclear. | OmpA-like outer membrane protein; This protein has a modular architecture with two N-terminal TPR repeats, a central beta-propeller domain, encompassing five WD40 repeats, and a C-terminal OmpA domain. OmpA-like domain is thought to be responsible for non-covalent interactions with peptidoglycan. The tetratrico peptide repeat (TPR) is a structural motif, which mediates proteinprotein interactions. Signal peptide cleaved between the residues 21 and 22; Localized in the outer membrane; Function unclear. | 0.411 |