P9WHG9

PR
Gene name
relA (Rv2583c, MTCY227.18)
Protein name
Bifunctional (p)ppGpp synthase/hydrolase RelA
Names
Species
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
KEGG Pathway
mtu:Rv2583c
EC number
2.7.6.5: Diphosphotransferases
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

540-612 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

4 structures for P9WHG9

Entry ID Method Resolution Chain Position Source
5XNX X-ray 370 A A/B/C/D 1-394 PDB
6LXG NMR - A/B 660-738 PDB
7DOJ NMR - A 394-459 PDB
AF-P9WHG9-F1 Predicted AlphaFoldDB

No variants for P9WHG9

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P9WHG9

No associated diseases with P9WHG9

7 regional properties for P9WHG9

Type Name Position InterPro Accession
domain ACT domain 657 - 736 IPR002912
domain HD/PDEase domain 49 - 172 IPR003607
domain TGS 398 - 459 IPR004095
domain HD domain 53 - 150 IPR006674
domain RelA/SpoT 221 - 351 IPR007685
domain RelA/SpoT, TGS domain 401 - 459 IPR033655
domain RelA/SpoT, AH and RIS domains 473 - 645 IPR045600

Functions

Description
EC Number 2.7.6.5 Diphosphotransferases
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
peptidoglycan-based cell wall A protective structure outside the cytoplasmic membrane composed of peptidoglycan (also known as murein), a molecule made up of a glycan (sugar) backbone of repetitively alternating N-acetylglucosamine and N-acetylmuramic acid with short, attached, cross-linked peptide chains containing unusual amino acids. An example of this component is found in Escherichia coli.
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
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
GTP binding Binding to GTP, guanosine triphosphate.
GTP diphosphokinase activity Catalysis of the reaction: ATP + GTP = AMP + guanosine 3'-diphosphate 5'-triphosphate.
guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity Catalysis of the reaction: guanosine 3',5'-bis(diphosphate) + H2O = guanosine 5'-diphosphate + diphosphate.
kinase activity Catalysis of the transfer of a phosphate group, usually from ATP, to a substrate molecule.
manganese ion binding Binding to a manganese ion (Mn).

3 GO annotations of biological process

Name Definition
guanosine tetraphosphate biosynthetic process The chemical reactions and pathways resulting in the formation of guanine tetraphosphate (5'-ppGpp-3'), a derivative of guanine riboside with four phosphates.
phosphorylation The process of introducing a phosphate group into a molecule, usually with the formation of a phosphoric ester, a phosphoric anhydride or a phosphoric amide.
stringent response A specific global change in the metabolism of a bacterial cell (the downregulation of nucleic acid and protein synthesis, and the simultaneous upregulation of protein degradation and amino acid synthesis) as a result of starvation.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MTAQRSTTNP VLEPLVAVHR EIYPKADLSI LQRAYEVADQ RHASQLRQSG DPYITHPLAV
70 80 90 100 110 120
ANILAELGMD TTTLVAALLH DTVEDTGYTL EALTEEFGEE VGHLVDGVTK LDRVVLGSAA
130 140 150 160 170 180
EGETIRKMIT AMARDPRVLV IKVADRLHNM RTMRFLPPEK QARKARETLE VIAPLAHRLG
190 200 210 220 230 240
MASVKWELED LSFAILHPKK YEEIVRLVAG RAPSRDTYLA KVRAEIVNTL TASKIKATVE
250 260 270 280 290 300
GRPKHYWSIY QKMIVKGRDF DDIHDLVGVR ILCDEIRDCY AAVGVVHSLW QPMAGRFKDY
310 320 330 340 350 360
IAQPRYGVYQ SLHTTVVGPE GKPLEVQIRT RDMHRTAEYG IAAHWRYKEA KGRNGVLHPH
370 380 390 400 410 420
AAAEIDDMAW MRQLLDWQRE AADPGEFLES LRYDLAVQEI FVFTPKGDVI TLPTGSTPVD
430 440 450 460 470 480
FAYAVHTEVG HRCIGARVNG RLVALERKLE NGEVVEVFTS KAPNAGPSRD WQQFVVSPRA
490 500 510 520 530 540
KTKIRQWFAK ERREEALETG KDAMAREVRR GGLPLQRLVN GESMAAVARE LHYADVSALY
550 560 570 580 590 600
TAIGEGHVSA KHVVQRLLAE LGGIDQAEEE LAERSTPATM PRRPRSTDDV GVSVPGAPGV
610 620 630 640 650 660
LTKLAKCCTP VPGDVIMGFV TRGGGVSVHR TDCTNAASLQ QQAERIIEVL WAPSPSSVFL
670 680 690 700 710 720
VAIQVEALDR HRLLSDVTRA LADEKVNILS ASVTTSGDRV AISRFTFEMG DPKHLGHLLN
730
AVRNVEGVYD VYRVTSAA