P07109

PR
Gene name
hisP (b2306, JW2303)
Protein name
Histidine transport ATP-binding protein HisP
Names
Species
Escherichia coli (strain K12)
KEGG Pathway
eco:b2306
EC number
7.4.2.1: Linked to the hydrolysis of a nucleoside triphosphate
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

204-257 (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 P07109

Entry ID Method Resolution Chain Position Source
AF-P07109-F1 Predicted AlphaFoldDB

No variants for P07109

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P07109

No associated diseases with P07109

3 regional properties for P07109

Type Name Position InterPro Accession
domain ABC transporter-like, ATP-binding domain 2 - 236 IPR003439
domain AAA+ ATPase domain 26 - 213 IPR003593
conserved_site ABC transporter-like, conserved site 137 - 151 IPR017871

Functions

Description
EC Number 7.4.2.1 Linked to the hydrolysis of a nucleoside triphosphate
Subcellular Localization
  • Cell inner membrane ; Peripheral membrane protein
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing A complex for the transport of metabolites into the cell, consisting of 5 subunits: two ATP-binding subunits, two membrane spanning subunits, and one substrate-binding subunit. In organisms with two membranes, the substrate-binding protein moves freely in the periplasmic space and joins the other subunits only when bound with substrate. In organisms with only one membrane the substrate-binding protein is tethered to the cytoplasmic membrane and associated with the other subunits. Transport of the substrate across the membrane is driven by the hydrolysis of ATP.
membrane A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.

3 GO annotations of molecular function

Name Definition
ABC-type amino acid transporter activity Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + amino acid(out/in) = ADP + phosphate + amino acid(in/out).
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
high-affinity L-histidine transmembrane transporter activity Enables the transfer of L-histidine from one side of a membrane to the other. L-histidine is 2-amino-3-(1H-imidazol-4-yl)propanoic acid. In high-affinity transport the transporter is able to bind the solute even if it is only present at very low concentrations.

3 GO annotations of biological process

Name Definition
amino acid import across plasma membrane The directed movement of an amino acid from outside of a cell, across the plasma membrane and into the cytosol.
L-histidine import across plasma membrane The directed movement of L-histidine from outside of a cell, across the plasma membrane and into the cytosol.
L-histidine transmembrane transport The directed movement of L-histidine across a membrane.

3 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P30750 metN Methionine import ATP-binding protein MetN Escherichia coli (strain K12) PR
P37774 tcyN L-cystine transport system ATP-binding protein TcyN Escherichia coli (strain K12) PR
P10346 glnQ Glutamine transport ATP-binding protein GlnQ Escherichia coli (strain K12) PR
10 20 30 40 50 60
MSENKLNVID LHKRYGEHEV LKGVSLQANA GDVISIIGSS GSGKSTFLRC INFLEKPSEG
70 80 90 100 110 120
SIVVNGQTIN LVRDKDGQLK VADKNQLRLL RTRLTMVFQH FNLWSHMTVL ENVMEAPIQV
130 140 150 160 170 180
LGLSKQEARE RAVKYLAKVG IDERAQGKYP VHLSGGQQQR VSIARALAME PEVLLFDEPT
190 200 210 220 230 240
SALDPELVGE VLRIMQQLAE EGKTMVVVTH EMGFARHVST HVIFLHQGKI EEEGAPEQLF
250
GNPQSPRLQR FLKGSLK