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 Q9ZJJ3

Entry ID Method Resolution Chain Position Source
AF-Q9ZJJ3-F1 Predicted AlphaFoldDB

No variants for Q9ZJJ3

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q9ZJJ3

No associated diseases with Q9ZJJ3

4 regional properties for Q9ZJJ3

Type Name Position InterPro Accession
domain Fork head domain 258 - 352 IPR001766
conserved_site Fork head domain conserved site1 260 - 273 IPR018122
conserved_site Fork head domain conserved site 2 305 - 311 IPR030456
domain Forkhead box protein M1, forkhead domain 260 - 336 IPR047516

Functions

Description
EC Number 7.1.2.2 Hydron translocation linked to the hydrolysis of a nucleoside triphosphate
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.
type III protein secretion system complex A complex of approximately 20 proteins, most of which are located in the cytoplasmic membrane that carries out protein secretion in the bacterial type III secretion system; type III secretion also requires a cytoplasmic, probably membrane-associated ATPase.

4 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
ATP hydrolysis activity Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient.
proton-transporting ATP synthase activity, rotational mechanism Enables the synthesis of ATP from ADP and phosphate by the transfer of protons from one side of a membrane to the other by a rotational mechanism driven by a gradient according to the reaction: ADP + H2O + phosphate + H+(in) -> ATP + H+(out).
proton-transporting ATPase activity, rotational mechanism Enables the transfer of protons from one side of a membrane to the other according to the reaction: ATP + H2O + H+(in) = ADP + phosphate + H+(out), by a rotational mechanism.

2 GO annotations of biological process

Name Definition
bacterial-type flagellum organization A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a bacterial-type flagellum, a motor complex composed of an extracellular helical protein filament coupled to a rotary motor embedded in the cell envelope which functions in cell motility.
protein secretion by the type III secretion system The process in which proteins are transferred into the extracellular milieu or directly into host cells by the bacterial type III secretion system; secretion occurs in a continuous process without the distinct presence of periplasmic intermediates and does not involve proteolytic processing of secreted proteins.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MPLKSLKNRL NQHFELSPRY GSVKKIMPNI VYADGFNPSV GDVVKIEKSD GTECVGMVVV
70 80 90 100 110 120
AEKEQFGFTP FNFIEGARAG DKVLFLKEGL NFPVGRNLLG RVLNPLGQVI DNKGVLDYER
130 140 150 160 170 180
LAPVITTPIA PLKRGLIDEV FSVGVKSIDG LLTCGKGQKL GIFAGSGVGK STLMGMITRG
190 200 210 220 230 240
CLAPIKVIAL IGERGREIPE FIEKNLKGDL SSCVLVVATS DDSPLMRKYG AFCAMSVAEY
250 260 270 280 290 300
FKNQGLDVLF IMDSVTRFAM AQREIGLALG EPPTSKGYPP SALSLLPQLM ERAGKEENKG
310 320 330 340 350 360
SITAFFSVLV EGDDLSDPIA DQARSILDGH IVLSRELTDY GIYPPINILN SASRVAKDII
370 380 390 400 410 420
SESQNLCARK FRRLYALLKE NEMLIRIGSY QMGNDKELDE AIKKKALMEQ FLVQDENALQ
430
PFEQSFQQLE EILR