Descriptions

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

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for Q8PCK2

Entry ID Method Resolution Chain Position Source
AF-Q8PCK2-F1 Predicted AlphaFoldDB

No variants for Q8PCK2

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q8PCK2

No associated diseases with Q8PCK2

6 regional properties for Q8PCK2

Type Name Position InterPro Accession
domain SpoVT-AbrB domain 4 - 47 IPR007159-1
domain SpoVT-AbrB domain 77 - 120 IPR007159-2
domain MraZ domain 2 - 66 IPR020603-1
domain MraZ domain 74 - 138 IPR020603-2
domain MraZ, N-terminal 2 - 58 IPR035642
domain MraZ, C-terminal 70 - 128 IPR035644

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

1 GO annotations of cellular component

Name Definition
integral component of plasma membrane The component of the plasma 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.

4 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.
phosphotransferase activity, for other substituted phosphate groups Catalysis of the transfer of a substituted phosphate group, other than diphosphate or nucleotidyl residues, from one compound (donor) to a another (acceptor).
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.

6 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 macromolecule biosynthetic process The chemical reactions and pathways resulting in the formation of a macromolecule destined to form part of a cell wall.
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
MLLELARWLQ QLESLFGLFN YLTFRGILAA LTALFLSLWM GPAVIRKLAQ FKGGQPIRQD
70 80 90 100 110 120
GPQTHFSKAG TPTMGGSLIL LTVTLSVLLW GDLRNRYVWL VLAVMICFGA IGWYDDWIKI
130 140 150 160 170 180
VRRDPNGLKS RWKYLLQSIF GLAAGLFLYY TADVPAAITF YIPMFKAIAL PLAGVSFVVI
190 200 210 220 230 240
AYFWIVGFSN AVNLTDGLDG LAIMPTVLVA CALGVFAYAS GNVVFAEYLK IPLIPGAGEL
250 260 270 280 290 300
IIICSAIAGA GLGFLWFNTY PAMVFMGDIG ALSLGAVLGT VAVIVRQELV LVIMGGVFVI
310 320 330 340 350 360
ETLSVMIQVA SFKLTGKRVF RMAPIHHHFE LKGWPEPRVI VRFWIISVVL VLIGLATLKV
R