node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
atpE | cls | MS53_0410 | MS53_0393 | ATP synthase C chain; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. | Cardiolipin synthetase; Identified by sequence similarity; putative; ORF located using Blastx;COG1502. | 0.566 |
atpE | mgtA | MS53_0410 | MS53_0572 | ATP synthase C chain; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. | Cation-transporting P-type ATPase; Identified by sequence similarity; putative; ORF located using Blastx;COG0474;TC:3.A.3.2.4. | 0.755 |
atpE | plsC | MS53_0410 | MS53_0097 | ATP synthase C chain; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. | 1-acyl-sn-glycerol-3-phosphate acyltransferase; Identified by sequence similarity; putative; ORF located using Blastx;COG0204. | 0.467 |
atpE | rpsK | MS53_0410 | MS53_0575 | ATP synthase C chain; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. | 30S ribosomal protein S11; Located on the platform of the 30S subunit, it bridges several disparate RNA helices of the 16S rRNA. Forms part of the Shine- Dalgarno cleft in the 70S ribosome; Belongs to the universal ribosomal protein uS11 family. | 0.850 |
atpE | rpsM | MS53_0410 | MS53_0576 | ATP synthase C chain; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. | 30S ribosomal protein S13; Located at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNA. In the 70S ribosome it contacts the 23S rRNA (bridge B1a) and protein L5 of the 50S subunit (bridge B1b), connecting the 2 subunits; these bridges are implicated in subunit movement. Contacts the tRNAs in the A and P-sites. Belongs to the universal ribosomal protein uS13 family. | 0.749 |
atpE | secY | MS53_0410 | MS53_0581 | ATP synthase C chain; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. | Preprotein translocase secy subunit; The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently. | 0.773 |
cls | atpE | MS53_0393 | MS53_0410 | Cardiolipin synthetase; Identified by sequence similarity; putative; ORF located using Blastx;COG1502. | ATP synthase C chain; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. | 0.566 |
cls | mgtA | MS53_0393 | MS53_0572 | Cardiolipin synthetase; Identified by sequence similarity; putative; ORF located using Blastx;COG1502. | Cation-transporting P-type ATPase; Identified by sequence similarity; putative; ORF located using Blastx;COG0474;TC:3.A.3.2.4. | 0.526 |
cls | pdhD | MS53_0393 | MS53_0275 | Cardiolipin synthetase; Identified by sequence similarity; putative; ORF located using Blastx;COG1502. | Dihydrolipoamide dehydrogenase; Identified by sequence similarity; putative; ORF located using GeneMark;Blastx;COG1249. | 0.467 |
cls | plsC | MS53_0393 | MS53_0097 | Cardiolipin synthetase; Identified by sequence similarity; putative; ORF located using Blastx;COG1502. | 1-acyl-sn-glycerol-3-phosphate acyltransferase; Identified by sequence similarity; putative; ORF located using Blastx;COG0204. | 0.495 |
map | mgtA | MS53_0579 | MS53_0572 | Methionyl aminopeptidase; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily. | Cation-transporting P-type ATPase; Identified by sequence similarity; putative; ORF located using Blastx;COG0474;TC:3.A.3.2.4. | 0.522 |
map | pdhD | MS53_0579 | MS53_0275 | Methionyl aminopeptidase; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily. | Dihydrolipoamide dehydrogenase; Identified by sequence similarity; putative; ORF located using GeneMark;Blastx;COG1249. | 0.492 |
map | rplQ | MS53_0579 | MS53_0573 | Methionyl aminopeptidase; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily. | 50S ribosomal protein L17; Identified by sequence similarity; putative; ORF located using Blastx;COG0203. | 0.937 |
map | rpsK | MS53_0579 | MS53_0575 | Methionyl aminopeptidase; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily. | 30S ribosomal protein S11; Located on the platform of the 30S subunit, it bridges several disparate RNA helices of the 16S rRNA. Forms part of the Shine- Dalgarno cleft in the 70S ribosome; Belongs to the universal ribosomal protein uS11 family. | 0.996 |
map | rpsM | MS53_0579 | MS53_0576 | Methionyl aminopeptidase; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily. | 30S ribosomal protein S13; Located at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNA. In the 70S ribosome it contacts the 23S rRNA (bridge B1a) and protein L5 of the 50S subunit (bridge B1b), connecting the 2 subunits; these bridges are implicated in subunit movement. Contacts the tRNAs in the A and P-sites. Belongs to the universal ribosomal protein uS13 family. | 0.997 |
map | secY | MS53_0579 | MS53_0581 | Methionyl aminopeptidase; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily. | Preprotein translocase secy subunit; The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently. | 0.930 |
mgtA | atpE | MS53_0572 | MS53_0410 | Cation-transporting P-type ATPase; Identified by sequence similarity; putative; ORF located using Blastx;COG0474;TC:3.A.3.2.4. | ATP synthase C chain; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. | 0.755 |
mgtA | cls | MS53_0572 | MS53_0393 | Cation-transporting P-type ATPase; Identified by sequence similarity; putative; ORF located using Blastx;COG0474;TC:3.A.3.2.4. | Cardiolipin synthetase; Identified by sequence similarity; putative; ORF located using Blastx;COG1502. | 0.526 |
mgtA | map | MS53_0572 | MS53_0579 | Cation-transporting P-type ATPase; Identified by sequence similarity; putative; ORF located using Blastx;COG0474;TC:3.A.3.2.4. | Methionyl aminopeptidase; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily. | 0.522 |
mgtA | mgtE | MS53_0572 | MS53_0497 | Cation-transporting P-type ATPase; Identified by sequence similarity; putative; ORF located using Blastx;COG0474;TC:3.A.3.2.4. | Mg2+ transport protein; Acts as a magnesium transporter. | 0.598 |