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 Q04473

Entry ID Method Resolution Chain Position Source
AF-Q04473-F1 Predicted AlphaFoldDB

8 variants for Q04473

Variant ID(s) Position Change Description Diseaes Association Provenance
61 M>A serotype 8 [UniProt] No
91 M>T serotype 8 [UniProt] No
125 G>DV serotype 8 [UniProt] No
213 S>N serotype 8 [UniProt] No
416 T>A serotype 8 [UniProt] No
469 F>K serotype 8 [UniProt] No
606 L>Q serotype 8 [UniProt] No
638 S>R serotype 8 [UniProt] No

No associated diseases with Q04473

6 regional properties for Q04473

Type Name Position InterPro Accession
domain ABC transporter-like, ATP-binding domain 472 - 707 IPR003439
domain AAA+ ATPase domain 498 - 684 IPR003593
domain Peptidase C39, bacteriocin processing 6 - 133 IPR005074
domain ABC transporter type 1, transmembrane domain 161 - 440 IPR011527
conserved_site ABC transporter-like, conserved site 610 - 624 IPR017871
domain Peptidase C39-like A 8 - 129 IPR039395

Functions

Description
EC Number
Subcellular Localization
  • Cell membrane; Multi-pass membrane protein
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 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.
type I protein secretion system complex A complex of three secretory proteins that carry out secretion in the type I secretion system: an inner membrane transport ATPase (termed ABC protein for ATP-binding cassette), which provides the energy for protein secretion; an outer membrane protein, which is exported via the sec pathway; and a membrane fusion protein, which is anchored in the inner membrane and spans the periplasmic space.

3 GO annotations of molecular function

Name Definition
ABC-type transporter activity Primary active transporter characterized by two nucleotide-binding domains and two transmembrane domains. Uses the energy generated from ATP hydrolysis to drive the transport of a substance across a membrane.
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
peptidase activity Catalysis of the hydrolysis of a peptide bond. A peptide bond is a covalent bond formed when the carbon atom from the carboxyl group of one amino acid shares electrons with the nitrogen atom from the amino group of a second amino acid.

3 GO annotations of biological process

Name Definition
cytolysis The rupture of cell membranes and the loss of cytoplasm.
protein secretion by the type I secretion system The process in which proteins are secreted into the extracellular milieu via the type I secretion system; secretion occurs in a continuous process without the distinct presence of periplasmic intermediates and does not involve proteolytic processing of secreted proteins.
proteolysis The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MESQMPFNEK IDYGLHALVI LAQYHNVAVN PEEVKHKFDL DGKGLDLVAW LLAAKSLELK
70 80 90 100 110 120
MKRVKKSIER LPFIHLPALI WRDDGQHVIL MKIDTQTNRY LIFDLEERNP KVLSAAEFHE
130 140 150 160 170 180
IFQGGMILIT SRASIMGQLA KFDFTWFIPA VIKYRKIFVE TIIVSIFLQL FALITPLFFQ
190 200 210 220 230 240
VVMDKVLVHR GFSTLNVITV ALSVVVIFEI VLSGLRTYIF SHSTSRIDVE LGAKLFRHLL
250 260 270 280 290 300
ALPISYFENR RVGDTVARVR ELDQIRNFLT GQALTSVLDL LFSFIFFAVM WYYSPKLTIV
310 320 330 340 350 360
ILLSLPCYIA WSIFISPILR RRLDEKFARN ADNQSFLVES VSAIDTIKAL AVTPQMTNIW
370 380 390 400 410 420
DKQLASYVSA DFRVTVLATI GQQGVQLIQK TVMIINLWLG AHLVISGDLS IGQLITFNML
430 440 450 460 470 480
SGQVIAPVVR LAQLWQDFQQ VGISITRLGD VLNSPTENYQ GKLSLPEIFG DIAFKHIRFR
490 500 510 520 530 540
YKPDAPIILD DVNLSVKQGE VIGIVGRSGS GKSTLTKLLQ RFYIPENGQV LIDGHDLALA
550 560 570 580 590 600
DPNWLRRQIG VVLQDNVLLN RSIRDNIALT DPSMSMERVI YAAKLAGAHD FISELREGYN
610 620 630 640 650 660
TIVGELGAGL SGGQRQRIAI ARALVNNPRI LIFDEATSAL DYESEHIIMQ NMQKICHGRT
670 680 690 700 710
VIIIAHRLST VKNADRIIVM EKGHIVEQGK HNQLLENENG LYYYLNQLQS N