P9WQJ9

PR
Gene name
irtA (Rv1348, MTCY02B10.12)
Protein name
Mycobactin import ATP-binding/permease protein IrtA
Names
Iron-regulated transporter A
Species
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
KEGG Pathway
mtu:Rv1348
EC number
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

214-297 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

5 structures for P9WQJ9

Entry ID Method Resolution Chain Position Source
7WIU EM 348 A A 1-859 PDB
7WIV EM 288 A A 1-859 PDB
7WIW EM 312 A A 1-859 PDB
7WIX EM 353 A A 1-859 PDB
AF-P9WQJ9-F1 Predicted AlphaFoldDB

No variants for P9WQJ9

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P9WQJ9

No associated diseases with P9WQJ9

7 regional properties for P9WQJ9

Type Name Position InterPro Accession
domain ABC transporter-like, ATP-binding domain 610 - 843 IPR003439
domain AAA+ ATPase domain 635 - 820 IPR003593
domain Siderophore-interacting protein, C-terminal domain 131 - 241 IPR007037
domain ABC transporter type 1, transmembrane domain 294 - 575 IPR011527
domain FAD-binding 9, siderophore-interacting 61 - 113 IPR013113
conserved_site ABC transporter-like, conserved site 746 - 760 IPR017871
domain FAD-binding domain, ferredoxin reductase-type 15 - 122 IPR017927

Functions

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

2 GO annotations of cellular component

Name Definition
integral component of plasma membrane The component of the plasma 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.

6 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.
ATPase-coupled transmembrane transporter activity Primary active transporter of a solute across a membrane, via the reaction: ATP + H2O = ADP + phosphate, to directly drive the transport of a substance across a membrane. The transport protein may be transiently phosphorylated (P-type transporters), or not (ABC-type transporters and other families of transporters). Primary active transport occurs up the solute's concentration gradient and is driven by a primary energy source.
FAD binding Binding to the oxidized form, FAD, of flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes.
oxidoreductase activity Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced.
siderophore transmembrane transporter activity Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: siderophore-iron(out) + H+(out) = siderophore-iron(in) + H+(in).

5 GO annotations of biological process

Name Definition
cellular response to iron ion starvation Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of deprivation of iron ions.
iron acquisition from host The process by which a symbiont acquires iron from its host, either from heme or other iron containing molecules such as transferrin and lactoferrin. Begins with either the secretion of symbiont gene products that bind iron- or heme-containing molecules (siderophores and hemophores) from the symbiont cell into the host, or by expression of receptors that bind iron- or heme-containing molecules on the symbiont cell surface. Ends when the iron-containing compound is transported into the symbiont cell.
iron ion homeostasis Any process involved in the maintenance of an internal steady state of iron ions within an organism or cell.
response to host iron concentration Any process that results in a change in state or activity of the symbiont or its cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of detecting iron concentration in its host organism. The host is defined as the larger of the organisms involved in a symbiotic interaction.
siderophore-dependent iron import into cell A process in which iron (Fe3+) is solubilized by ferric iron-specific chelators, known as siderophores, excreted by a cell; the iron-siderophore complex is then transported into the cell by specific cell surface receptors.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MARGLQGVML RSFGARDHTA TVIETISIAP HFVRVRMVSP TLFQDAEAEP AAWLRFWFPD
70 80 90 100 110 120
PNGSNTEFQR AYTISEADPA AGRFAVDVVL HDPAGPASSW ARTVKPGATI AVMSLMGSSR
130 140 150 160 170 180
FDVPEEQPAG YLLIGDSASI PGMNGIIETV PNDVPIEMYL EQHDDNDTLI PLAKHPRLRV
190 200 210 220 230 240
RWVMRRDEKS LAEAIENRDW SDWYAWATPE AAALKCVRVR LRDEFGFPKS EIHAQAYWNA
250 260 270 280 290 300
GRAMGTHRAT EPAATEPEVG AAPQPESAVP APARGSWRAQ AASRLLAPLK LPLVLSGVLA
310 320 330 340 350 360
ALVTLAQLAP FVLLVELSRL LVSGAGAHRL FTVGFAAVGL LGTGALLAAA LTLWLHVIDA
370 380 390 400 410 420
RFARALRLRL LSKLSRLPLG WFTSRGSGSI KKLVTDDTLA LHYLVTHAVP DAVAAVVAPV
430 440 450 460 470 480
GVLVYLFVVD WRVALVLFGP VLVYLTITSS LTIQSGPRIV QAQRWAEKMN GEAGSYLEGQ
490 500 510 520 530 540
PVIRVFGAAS SSFRRRLDEY IGFLVAWQRP LAGKKTLMDL ATRPATFLWL IAATGTLLVA
550 560 570 580 590 600
THRMDPVNLL PFMFLGTTFG ARLLGIAYGL GGLRTGLLAA RHLQVTLDET ELAVREHPRE
610 620 630 640 650 660
PLDGEAPATV VFDHVTFGYR PGVPVIQDVS LTLRPGTVTA LVGPSGSGKS TLATLLARFH
670 680 690 700 710 720
DVERGAIRVG GQDIRSLAAD ELYTRVGFVL QEAQLVHGTA AENIALAVPD APAEQVQVAA
730 740 750 760 770 780
REAQIHDRVL RLPDGYDTVL GANSGLSGGE RQRLTIARAI LGDTPVLILD EATAFADPES
790 800 810 820 830 840
EYLVQQALNR LTRDRTVLVI AHRLHTITRA DQIVVLDHGR IVERGTHEEL LAAGGRYCRL
850
WDTGQGSRVA VAAAQDGTR