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 P77439

Entry ID Method Resolution Chain Position Source
AF-P77439-F1 Predicted AlphaFoldDB

No variants for P77439

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P77439

No associated diseases with P77439

8 regional properties for P77439

Type Name Position InterPro Accession
domain Phosphocarrier protein HPr-like 1 - 90 IPR000032
domain PEP-utilising enzyme, C-terminal 360 - 650 IPR000121
domain PTS EIIA type-2 domain 685 - 828 IPR002178
domain Phosphotransferase system, IIA component fructose subfamily 687 - 812 IPR004715
domain Phosphotransferase system, enzyme I-like 118 - 674 IPR006318
domain PEP-utilising enzyme, mobile domain 262 - 334 IPR008279
domain Phosphotransferase system, enzyme I N-terminal 119 - 234 IPR008731
conserved_site PEP-utilising enzyme, conserved site 556 - 574 IPR023151

Functions

Description
EC Number 2.7.1.202 Phosphotransferases with an alcohol group as acceptor
Subcellular Localization
  • Cytoplasm
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
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.

4 GO annotations of molecular function

Name Definition
kinase activity Catalysis of the transfer of a phosphate group, usually from ATP, to a substrate molecule.
metal ion binding Binding to a metal ion.
phosphoenolpyruvate-protein phosphotransferase activity Catalysis of the reaction: phosphoenolpyruvate + protein L-histidine = pyruvate + protein N(pi)-phospho-L-histidine.
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.

1 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P08839 ptsI Phosphoenolpyruvate-protein phosphotransferase Escherichia coli (strain K12) PR
10 20 30 40 50 60
MLTIQFLCPL PNGLHARPAW ELKEQCSQWQ SEITFINHRQ NAKADAKSSL ALIGTGTLFN
70 80 90 100 110 120
DSCSLNISGS DEEQARRVLE EYIQVRFIDS DSVQPTQAEL TAHPLPRSLS RLNPDLLYGN
130 140 150 160 170 180
VLASGVGVGT LTLLQSDSLD SYRAIPASAQ DSTRLEHSLA TLAEQLNQQL RERDGESKTI
190 200 210 220 230 240
LSAHLSLIQD DEFAGNIRRL MTEQHQGLGA AIISNMEQVC AKLSASASDY LRERVSDIRD
250 260 270 280 290 300
ISEQLLHITW PELKPRNKLV LEKPTILVAE DLTPSQFLSL DLKNLAGMIL EKTGRTSHTL
310 320 330 340 350 360
ILARASAIPV LSGLPLDAIA RYAGQPAVLD AQCGVLAINP NDAVSGYYQV AQTLADKRQK
370 380 390 400 410 420
QQAQAAAQLA YSRDNKRIDI AANIGTALEA PGAFANGAEG VGLFRTEMLY MDRDSAPDEQ
430 440 450 460 470 480
EQFEAYQQVL LAAGDKPIIF RTMDIGGDKS IPYLNIPQEE NPFLGYRAVR IYPEFAGLFR
490 500 510 520 530 540
TQLRAILRAA SFGNAQLMIP MVHSLDQILW VKGEIQKAIV ELKRDGLRHA ETITLGIMVE
550 560 570 580 590 600
VPSVCYIIDH FCDEVDFFSI GSNDMTQYLY AVDRNNPRVS PLYNPITPSF LRMLQQIVTT
610 620 630 640 650 660
AHQRGKWVGI CGELGGESRY LPLLLGLGLD ELSMSSPRIP AVKSQLRQLD SEACRELARQ
670 680 690 700 710 720
ACECRSAQEI EALLTAFTPE EDVRPLLALE NIFVDQDFSN KEQAIQFLCG NLGVNGRTEH
730 740 750 760 770 780
PFELEEDVWQ REEIVTTGVG FGVAIPHTKS QWIRHSSISI ARLAKPIGWQ SEMGEVELVI
790 800 810 820 830
MLTLGANEGM NHVKVFSQLA RKLVNKNFRQ SLFAAQDAQS ILTLLETELT F