B1J3K9

PR
Gene name
mraY
Protein name
Phospho-N-acetylmuramoyl-pentapeptide-transferase
Names
UDP-MurNAc-pentapeptide phosphotransferase
Species
Pseudomonas putida (strain W619)
KEGG Pathway
ppw:PputW619_0941
EC number
2.7.8.13: Transferases for other substituted phosphate groups
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

30-99 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for B1J3K9

Entry ID Method Resolution Chain Position Source
AF-B1J3K9-F1 Predicted AlphaFoldDB

No variants for B1J3K9

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for B1J3K9

No associated diseases with B1J3K9

2 regional properties for B1J3K9

Type Name Position InterPro Accession
conserved_site Phospho-N-acetylmuramoyl-pentapeptide transferase, conserved site 68 - 80 IPR018480-1
conserved_site Phospho-N-acetylmuramoyl-pentapeptide transferase, conserved site 189 - 200 IPR018480-2

Functions

Description
EC Number 2.7.8.13 Transferases for other substituted phosphate groups
Subcellular Localization
  • Cell inner membrane ; Multi-pass membrane protein
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
integral component of membrane The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.

3 GO annotations of molecular function

Name Definition
metal ion binding Binding to a metal ion.
phospho-N-acetylmuramoyl-pentapeptide-transferase activity Catalysis of the reaction: UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine + undecaprenyl phosphate = UMP + N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine-diphosphoundecaprenol.
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine:undecaprenyl-phosphate transferase activity Catalysis of the reaction: UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine + di-trans,poly-cis-undecaprenyl phosphate = UMP + N-acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine-diphosphoundecaprenol.

5 GO annotations of biological process

Name Definition
cell cycle The progression of biochemical and morphological phases and events that occur in a cell during successive cell replication or nuclear replication events. Canonically, the cell cycle comprises the replication and segregation of genetic material followed by the division of the cell, but in endocycles or syncytial cells nuclear replication or nuclear division may not be followed by cell division.
cell division The process resulting in division and partitioning of components of a cell to form more cells; may or may not be accompanied by the physical separation of a cell into distinct, individually membrane-bounded daughter cells.
cell wall organization A process that results in the assembly, arrangement of constituent parts, or disassembly of the cell wall, the rigid or semi-rigid envelope lying outside the cell membrane of plant, fungal and most prokaryotic cells, maintaining their shape and protecting them from osmotic lysis.
peptidoglycan biosynthetic process The chemical reactions and pathways resulting in the formation of peptidoglycans, any of a class of glycoconjugates found in bacterial cell walls.
regulation of cell shape Any process that modulates the surface configuration of a cell.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MLLLLAEYLQ QFHKGFAVFQ YLSLRGILGV LTALSLALWL GPWMIRTLQI RQIGQAVRND
70 80 90 100 110 120
GPQSHLSKSG TPTMGGALIL SAIGISTLLW ADLSNRYVWT VLIVTLLFGA IGWVDDYRKV
130 140 150 160 170 180
IEKNSRGLPS RWKYFWQSVF GLTAAIFLYQ TAPTTVETTL IVPFLKDVTI PLGIGFVVLT
190 200 210 220 230 240
YFVIVGSSNA VNLTDGLDGL AIMPTVMVGG ALGIFCYLSG NVKFAEYLLI PYVPGSGELI
250 260 270 280 290 300
VFCGALIGAG LGFLWFNTYP AQVFMGDVGA LALGAALGTI AVIVRQEIVL FIMGGIFVME
310 320 330 340 350
TLSVVIQVAS FKLTGKRVFR MAPIHHHFEL KGWPEPRVIV RFWIITVILV LIGLATLKLR