Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P75168

- PT1_MYCPN

UniProt

P75168 - PT1_MYCPN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Phosphoenolpyruvate-protein phosphotransferase

Gene

ptsI

Organism
Mycoplasma pneumoniae (strain ATCC 29342 / M129)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

Functioni

General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. Enzyme I transfers the phosphoryl group from phosphoenolpyruvate (PEP) to the phosphoryl carrier protein (HPr) (By similarity).By similarity

Catalytic activityi

Phosphoenolpyruvate + protein L-histidine = pyruvate + protein N(pi)-phospho-L-histidine.

Cofactori

Mg2+By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei190 – 1901Tele-phosphohistidine intermediateBy similarity
Binding sitei297 – 2971SubstrateBy similarity
Binding sitei333 – 3331SubstrateBy similarity
Metal bindingi427 – 4271MagnesiumBy similarity
Binding sitei427 – 4271SubstrateBy similarity
Binding sitei448 – 4481Substrate; via carbonyl oxygenBy similarity
Binding sitei449 – 4491Substrate; via amide nitrogenBy similarity
Binding sitei450 – 4501SubstrateBy similarity
Metal bindingi451 – 4511MagnesiumBy similarity
Binding sitei451 – 4511Substrate; via amide nitrogenBy similarity
Active sitei498 – 4981Proton donorBy similarity

GO - Molecular functioni

  1. kinase activity Source: UniProtKB-KW
  2. metal ion binding Source: UniProtKB-KW
  3. phosphoenolpyruvate-protein phosphotransferase activity Source: UniProtKB-EC

GO - Biological processi

  1. phosphoenolpyruvate-dependent sugar phosphotransferase system Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Phosphotransferase system, Sugar transport, Transport

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciMPNE272634:GJ6Z-673-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoenolpyruvate-protein phosphotransferase (EC:2.7.3.9)
Alternative name(s):
Phosphotransferase system, enzyme I
Gene namesi
Name:ptsI
Ordered Locus Names:MPN_627
ORF Names:MP215
OrganismiMycoplasma pneumoniae (strain ATCC 29342 / M129)
Taxonomic identifieri272634 [NCBI]
Taxonomic lineageiBacteriaTenericutesMollicutesMycoplasmataceaeMycoplasma
ProteomesiUP000000808: Chromosome

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 572572Phosphoenolpyruvate-protein phosphotransferasePRO_0000147077Add
BLAST

Proteomic databases

PaxDbiP75168.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

IntActiP75168. 1 interaction.
STRINGi272634.MPN627.

Structurei

3D structure databases

ProteinModelPortaliP75168.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

The N-terminal domain contains the HPr binding site, the central domain the pyrophosphate/phosphate carrier histidine, and the C-terminal domain the pyruvate binding site.By similarity

Sequence similaritiesi

Belongs to the PEP-utilizing enzyme family.Curated

Phylogenomic databases

eggNOGiCOG1080.
KOiK08483.
OMAiWQISSIV.
OrthoDBiEOG657JBQ.

Family and domain databases

Gene3Di1.10.274.10. 1 hit.
3.20.20.60. 1 hit.
3.50.30.10. 1 hit.
InterProiIPR008279. PEP-util_enz_mobile_dom.
IPR018274. PEP_util_AS.
IPR000121. PEP_util_C.
IPR023151. PEP_util_CS.
IPR006318. PEP_util_enz.
IPR024692. PTS_EI.
IPR008731. PTS_EIN.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
[Graphical view]
PfamiPF05524. PEP-utilisers_N. 1 hit.
PF00391. PEP-utilizers. 1 hit.
PF02896. PEP-utilizers_C. 1 hit.
[Graphical view]
PIRSFiPIRSF000732. PTS_enzyme_I. 1 hit.
PRINTSiPR01736. PHPHTRNFRASE.
SUPFAMiSSF47831. SSF47831. 1 hit.
SSF51621. SSF51621. 1 hit.
SSF52009. SSF52009. 1 hit.
TIGRFAMsiTIGR01417. PTS_I_fam. 1 hit.
PROSITEiPS00742. PEP_ENZYMES_2. 1 hit.
PS00370. PEP_ENZYMES_PHOS_SITE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P75168-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKKLSGIGVS DGMALAKAFL VKTPEFAVNK YLKHQLTKAQ AKRLLDSAFK
60 70 80 90 100
KAVKDLEEIK EITVNNINTE AGMIFDAHIQ MLNDPTITEQ LEQQLAQNVH
110 120 130 140 150
PVIAVDTVFS QTATMFSQMQ DKYFQERAAD ILDLRQRLLA YLTGQKPHDL
160 170 180 190 200
VKIKSDVIIV AHDLTPSQTA TLNKKYVKGF LTEIGGRTSH AAIMARSLEI
210 220 230 240 250
PAVVGIKGIT TKVKDGQIVG VDGRKGIAGL DLNSKDTTEW KKQKALEEKY
260 270 280 290 300
QQELKQYTNK ETVTLDGHAV VVAANIGNVK DMELACQYNT NGVGLFRTEF
310 320 330 340 350
LYMNSQEWPD EETQYQAYKA VLEQAHGDLV IIRTLDIGGD KKLNYYEFPH
360 370 380 390 400
EDNPFLGYRA LRLTLDKQDI FKTQLRALLR AADHGQLGIM FPMVATLDEL
410 420 430 440 450
LQAKQLLNQV HQELGGNKQF KLGIMIEIPA AVLAANTLSH HVDFFSIGTN
460 470 480 490 500
DLIQYSFAAD RMNKNVSYLY QPLNPALLKL IYLTIEGGKV NDIWTGMCGE
510 520 530 540 550
MAGEPLAIPL LLGLGLKEFS MSASSMFKAR MIIAKLNYTE CQTLAQKALT
560 570
LANAKEVEKL VEKFFKKKDI FI
Length:572
Mass (Da):63,950
Last modified:February 1, 1997 - v1
Checksum:i5B12EF54B0CB80CB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00089 Genomic DNA. Translation: AAB95863.1.
PIRiS73541.
RefSeqiNP_110316.1. NC_000912.1.

Genome annotation databases

EnsemblBacteriaiAAB95863; AAB95863; MPN_627.
GeneIDi876731.
KEGGimpn:MPN627.
PATRICi20022737. VBIMycPne110_0691.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00089 Genomic DNA. Translation: AAB95863.1 .
PIRi S73541.
RefSeqi NP_110316.1. NC_000912.1.

3D structure databases

ProteinModelPortali P75168.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P75168. 1 interaction.
STRINGi 272634.MPN627.

Proteomic databases

PaxDbi P75168.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAB95863 ; AAB95863 ; MPN_627 .
GeneIDi 876731.
KEGGi mpn:MPN627.
PATRICi 20022737. VBIMycPne110_0691.

Phylogenomic databases

eggNOGi COG1080.
KOi K08483.
OMAi WQISSIV.
OrthoDBi EOG657JBQ.

Enzyme and pathway databases

BioCyci MPNE272634:GJ6Z-673-MONOMER.

Family and domain databases

Gene3Di 1.10.274.10. 1 hit.
3.20.20.60. 1 hit.
3.50.30.10. 1 hit.
InterProi IPR008279. PEP-util_enz_mobile_dom.
IPR018274. PEP_util_AS.
IPR000121. PEP_util_C.
IPR023151. PEP_util_CS.
IPR006318. PEP_util_enz.
IPR024692. PTS_EI.
IPR008731. PTS_EIN.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
[Graphical view ]
Pfami PF05524. PEP-utilisers_N. 1 hit.
PF00391. PEP-utilizers. 1 hit.
PF02896. PEP-utilizers_C. 1 hit.
[Graphical view ]
PIRSFi PIRSF000732. PTS_enzyme_I. 1 hit.
PRINTSi PR01736. PHPHTRNFRASE.
SUPFAMi SSF47831. SSF47831. 1 hit.
SSF51621. SSF51621. 1 hit.
SSF52009. SSF52009. 1 hit.
TIGRFAMsi TIGR01417. PTS_I_fam. 1 hit.
PROSITEi PS00742. PEP_ENZYMES_2. 1 hit.
PS00370. PEP_ENZYMES_PHOS_SITE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Complete sequence analysis of the genome of the bacterium Mycoplasma pneumoniae."
    Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.
    Nucleic Acids Res. 24:4420-4449(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 29342 / M129.

Entry informationi

Entry nameiPT1_MYCPN
AccessioniPrimary (citable) accession number: P75168
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: November 26, 2014
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The reaction takes place in three steps, mediated by a phosphocarrier histidine residue located on the surface of the central domain. The two first partial reactions are catalyzed at an active site located on the N-terminal domain, and the third partial reaction is catalyzed at an active site located on the C-terminal domain. For catalytic turnover, the central domain swivels from the concave surface of the N-terminal domain to that of the C-terminal domain (By similarity).By similarity

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Mycoplasma pneumoniae
    Mycoplasma pneumoniae (strain M129): entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3