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8G01

YES Complex - E. coli MraY, Protein E ID21, E. coli SlyD

Functional Information from GO Data
ChainGOidnamespacecontents
A0005886cellular_componentplasma membrane
A0008360biological_processregulation of cell shape
A0008963molecular_functionphospho-N-acetylmuramoyl-pentapeptide-transferase activity
A0009252biological_processpeptidoglycan biosynthetic process
A0016020cellular_componentmembrane
A0016740molecular_functiontransferase activity
A0016780molecular_functionphosphotransferase activity, for other substituted phosphate groups
A0044038biological_processcell wall macromolecule biosynthetic process
A0046872molecular_functionmetal ion binding
A0051301biological_processcell division
A0051992molecular_functionUDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine:undecaprenyl-phosphate transferase activity
A0071555biological_processcell wall organization
B0004857molecular_functionenzyme inhibitor activity
B0031640biological_processkilling of cells of another organism
C0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
D0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
E0005886cellular_componentplasma membrane
E0008360biological_processregulation of cell shape
E0008963molecular_functionphospho-N-acetylmuramoyl-pentapeptide-transferase activity
E0009252biological_processpeptidoglycan biosynthetic process
E0016020cellular_componentmembrane
E0016740molecular_functiontransferase activity
E0016780molecular_functionphosphotransferase activity, for other substituted phosphate groups
E0044038biological_processcell wall macromolecule biosynthetic process
E0046872molecular_functionmetal ion binding
E0051301biological_processcell division
E0051992molecular_functionUDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine:undecaprenyl-phosphate transferase activity
E0071555biological_processcell wall organization
G0004857molecular_functionenzyme inhibitor activity
G0031640biological_processkilling of cells of another organism
Functional Information from PROSITE/UniProt
site_idPS01347
Number of Residues13
DetailsMRAY_1 MraY family signature 1. KrgTPTMGGImIL
ChainResidueDetails
ALYS68-LEU80

site_idPS01348
Number of Residues12
DetailsMRAY_2 MraY family signature 2. NavNlTDGLDGL
ChainResidueDetails
AASN189-LEU200

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues118
DetailsTopological domain: {"description":"Periplasmic","evidences":[{"source":"PubMed","id":"10564498","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues324
DetailsTransmembrane: {"description":"Helical"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues236
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"10564498","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues188
DetailsDomain: {"description":"PPIase FKBP-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00277","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues136
DetailsRegion: {"description":"PPIase first part"}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues88
DetailsRegion: {"description":"IF-chaperone"}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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