P23702

PR
Gene name
ltxB
Protein name
Leukotoxin export ATP-binding protein LtxB
Names
Species
Aggregatibacter actinomycetemcomitans (Actinobacillus actinomycetemcomitans) (Haemophilus actinomycetemcomitans)
KEGG Pathway
EC number
7.4.2.5: 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)

418-491 (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 P23702

Entry ID Method Resolution Chain Position Source
AF-P23702-F1 Predicted AlphaFoldDB

No variants for P23702

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P23702

No associated diseases with P23702

6 regional properties for P23702

Type Name Position InterPro Accession
domain ABC transporter-like, ATP-binding domain 468 - 703 IPR003439
domain AAA+ ATPase domain 494 - 680 IPR003593
domain Peptidase C39, bacteriocin processing 4 - 129 IPR005074
domain ABC transporter type 1, transmembrane domain 157 - 436 IPR011527
conserved_site ABC transporter-like, conserved site 606 - 620 IPR017871
domain Peptidase C39-like A 3 - 125 IPR039395

Functions

Description
EC Number 7.4.2.5 Linked to the hydrolysis of a nucleoside triphosphate
Subcellular Localization
  • Cell inner 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.

4 GO annotations of molecular function

Name Definition
ABC-type peptide transporter activity Catalysis of the reaction: ATP + H2O + peptide(in) = ADP + phosphate + peptide(out). Peptides exported include alpha-hemolysin, cyclolysin, colicin V and siderophores from Gram-negative bacteria, and bacteriocin, subtilin, competence factor and pediocin from Gram-positive bacteria.
ABC-type protein 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 + protein(out) = ADP + phosphate + protein(in).
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.

2 GO annotations of biological process

Name Definition
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
MDSQKNTNLA LQALEVLAQY HNISINPEEI KHKFDIDGHG LNQTKWLLAA KSLGLKVRTA
70 80 90 100 110 120
NKTVDRLPFL HLPALAWRDD GEHFILLKID QETDRYLIFD LIQKNPIVLD KNEFEERYQS
130 140 150 160 170 180
KVILIASRAS IVGNLAKFDF TWFIPAVIKY RKIFIETLIV SIFLQIFALI TPLFFQVVMD
190 200 210 220 230 240
KVLVHRGFST LNVITVALAI VVLFEIILGG LRTYVFAHST SRIDVELGAR LFRHLLALPI
250 260 270 280 290 300
SYFEARRVGD TVARVRELDQ IRNFLTGQAL TSILDLLFSF IFFAVMWYYS PKLTLVVLGS
310 320 330 340 350 360
LPCYVIWSVF ISPILRRRLD DKFARNADNQ SFLVESVTAI NTIKAMAISP QMTNIWDKQL
370 380 390 400 410 420
ASYVAVSFKV TVLATIGQQG IQLIQKAVMV INLWLGAHLV ISGDLSIGQL IAFNMLAGQI
430 440 450 460 470 480
ISPVIRLAQI WQDFQQVGIS VTRLGDVLNS PTENNTASVS LPEIQGEISF RNIKFRYKPD
490 500 510 520 530 540
SPMILNNINL DISQGEVIGI VGRSGSGKST LTKLIQRFYI PEQGQVLIDG HDLALADPNW
550 560 570 580 590 600
LRRQVGVVLQ DNVLLNRSIR ENIALTNPGM PMEKVIAAAK LAGAHDFISE LREGYNTVVG
610 620 630 640 650 660
EQGAGLSGGQ RQRIAIARAL VNNPRILIFD EATSALDYES ENIIMHNMHK ICQNRTVLII
670 680 690 700
AHRLSTVKNA DRIIVMDKGE IIEQGKHQEL LKDEKGLYSY LHQLQVN