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 Q57071

Entry ID Method Resolution Chain Position Source
AF-Q57071-F1 Predicted AlphaFoldDB

No variants for Q57071

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q57071

No associated diseases with Q57071

6 regional properties for Q57071

Type Name Position InterPro Accession
domain Phosphotransferase system, sugar-specific permease EIIA type 1 531 - 652 IPR001127
domain Phosphotransferase system, IIB component, type 1 404 - 506 IPR001996
domain Phosphotransferase system, EIIC 13 - 344 IPR003352
domain PTS system glucose-specific IIBC component 3 - 502 IPR011299
domain Phosphotransferase system, EIIC component, type 1 3 - 414 IPR013013
conserved_site Phosphotransferase system EIIB, cysteine phosphorylation site 425 - 500 IPR018113

Functions

Description
EC Number 2.7.1.199 Phosphotransferases with an alcohol group as acceptor
Subcellular Localization
  • Cell 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
glucose transmembrane transporter activity Enables the transfer of the hexose monosaccharide glucose from one side of a membrane to the other.
kinase activity Catalysis of the transfer of a phosphate group, usually from ATP, to a substrate molecule.
protein-N(PI)-phosphohistidine-sugar phosphotransferase activity Catalysis of the PEP-dependent, phosphoryl transfer-driven transport of substances across a membrane. The transport happens by catalysis of the reaction: protein N-phosphohistidine + sugar(out) = protein histidine + sugar phosphate(in). This differs from primary and secondary active transport in that the solute is modified during transport.

2 GO annotations of biological process

Name Definition
phosphoenolpyruvate-dependent sugar phosphotransferase system The uptake and phosphorylation of specific carbohydrates from the extracellular environment; uptake and phosphorylation are coupled, making the PTS a link between the uptake and metabolism of sugars; phosphoenolpyruvate is the original phosphate donor; phosphoenolpyruvate passes the phosphate via a signal transduction pathway, to enzyme 1 (E1), which in turn passes it on to the histidine protein, HPr; the next step in the system involves sugar-specific membrane-bound complex, enzyme 2 (EII), which transports the sugar into the cell; it includes the sugar permease, which catalyzes the transport reactions; EII is usually divided into three different domains, EIIA, EIIB, and EIIC.
phosphorylation The process of introducing a phosphate group into a molecule, usually with the formation of a phosphoric ester, a phosphoric anhydride or a phosphoric amide.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MWKKFFGQLQ RIGKALMLPV AILPAAGLLL ALGNAFQGDA LQSLMPFIKA EGFQNVAKMM
70 80 90 100 110 120
EGAGGIIFDN LAIIFALGVA IGLASGDGVA AIAAFVGFIV LNKTMGMFLG VTPEKAADAA
130 140 150 160 170 180
TGFANVLGIP TLQTGVFGGI IIGALAAWCY NKFYNISLPS YLGFFAGKRF VPIMMATCSF
190 200 210 220 230 240
ILAFPMAIIW PSIQGGLNAF SEGLLASNTG LAVFLFGFIK RLLIPFGLHH IFHAPFWFEF
250 260 270 280 290 300
GSYKNAAGQI IHGDQRIFIE QIRDNVPLTA GKFMQGEFPV MMFGLPAAAL AIYQTAKKEN
310 320 330 340 350 360
KKVVAGLMLS GALTSFLTGI TEPLEFSFLF VAPLLFFIHA VLDGLSFLIL YLLDLHLGYT
370 380 390 400 410 420
FSGGFIDFFL LGILPNKTQW WLVIPVGLVY AAIYYIIFRF LIVKFNFKTP GREDKEVKSS
430 440 450 460 470 480
NVAASELPFK VLDAMGGKAN IKHLDACITR LRVEVNDKAK VDVQELKDLG ASGVLEVGNN
490 500 510 520 530 540
MQAIFGPKSD QIKHDMQQIM DGKITSPEET TVTEEGDKET AEIAAAGGGV VYAPIKGEVV
550 560 570 580 590 600
DISEVPDKVF SEKMMGDGIA IKPETGEVVA PFDGVVKMVF PTKHAIGLES KDGIELLIHF
610 620 630 640 650 660
GLETVKLEGK GFDILVKEND NIVLGQPLMK VDLDYIKEHA DSTITPIVVT NLNGRTMEVL
670
QHGEVKQGDK VILVK