P9WHW5

PR
Gene name
pstP (mstp)
Protein name
Serine/threonine protein phosphatase PstP
Names
Mycobacterial Ser/Thr phosphatase, Mstp, PP2C-family Ser/Thr phosphatase
Species
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
KEGG Pathway
mtu:Rv0018c
EC number
3.1.3.16: Phosphoric monoester hydrolases
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

384-514 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

3 structures for P9WHW5

Entry ID Method Resolution Chain Position Source
1TXO X-ray 195 A A/B 5-237 PDB
2CM1 X-ray 200 A A 1-240 PDB
AF-P9WHW5-F1 Predicted AlphaFoldDB

No variants for P9WHW5

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P9WHW5

No associated diseases with P9WHW5

1 regional properties for P9WHW5

Type Name Position InterPro Accession
domain PPM-type phosphatase-like domain 5 - 238 IPR001932

Functions

Description
EC Number 3.1.3.16 Phosphoric monoester hydrolases
Subcellular Localization
  • Cell membrane ; Single-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.
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.
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.

5 GO annotations of molecular function

Name Definition
magnesium ion binding Binding to a magnesium (Mg) ion.
manganese ion binding Binding to a manganese ion (Mn).
myosin phosphatase activity Catalysis of the reaction: phosphomyosin + H2O = myosin + phosphate.
phosphoprotein phosphatase activity Catalysis of the reaction: a phosphoprotein + H2O = a protein + phosphate. Together with protein kinases, these enzymes control the state of phosphorylation of cellular proteins and thereby provide an important mechanism for regulating cellular activity.
protein serine/threonine phosphatase activity Catalysis of the reaction: protein serine phosphate + H2O = protein serine + phosphate, and protein threonine phosphate + H2O = protein threonine + phosphate.

5 GO annotations of biological process

Name Definition
negative regulation of catalytic activity Any process that stops or reduces the activity of an enzyme.
negative regulation of DNA binding Any process that stops or reduces the frequency, rate or extent of DNA binding. DNA binding is any process in which a gene product interacts selectively with DNA (deoxyribonucleic acid).
negative regulation of protein kinase activity Any process that stops, prevents, or reduces the frequency, rate or extent of protein kinase activity.
positive regulation of catalytic activity Any process that activates or increases the activity of an enzyme.
protein dephosphorylation The process of removing one or more phosphoric residues from a protein.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MARVTLVLRY AARSDRGLVR ANNEDSVYAG ARLLALADGM GGHAAGEVAS QLVIAALAHL
70 80 90 100 110 120
DDDEPGGDLL AKLDAAVRAG NSAIAAQVEM EPDLEGMGTT LTAILFAGNR LGLVHIGDSR
130 140 150 160 170 180
GYLLRDGELT QITKDDTFVQ TLVDEGRITP EEAHSHPQRS LIMRALTGHE VEPTLTMREA
190 200 210 220 230 240
RAGDRYLLCS DGLSDPVSDE TILEALQIPE VAESAHRLIE LALRGGGPDN VTVVVADVVD
250 260 270 280 290 300
YDYGQTQPIL AGAVSGDDDQ LTLPNTAAGR ASAISQRKEI VKRVPPQADT FSRPRWSGRR
310 320 330 340 350 360
LAFVVALVTV LMTAGLLIGR AIIRSNYYVA DYAGSVSIMR GIQGSLLGMS LHQPYLMGCL
370 380 390 400 410 420
SPRNELSQIS YGQSGGPLDC HLMKLEDLRP PERAQVRAGL PAGTLDDAIG QLRELAANSL
430 440 450 460 470 480
LPPCPAPRAT SPPGRPAPPT TSETTEPNVT SSPASPSPTT SAPAPTGTTP AIPTSASPAA
490 500 510
PASPPTPWPV TSSPTMAALP PPPPQPGIDC RAAA