Reviewed, UniProtKB/Swiss-Prot O07126 (PT1_LACSK)

Names and origin

Protein names

Recommended name:
    Phosphoenolpyruvate-protein phosphotransferase
    EC=2.7.3.9
Alternative name(s):
    Phosphotransferase system, enzyme I

Gene names

Name:

ptsI

Organism

Lactobacillus sakei

Taxonomic identifier

1599 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Lactobacillales › Lactobacillaceae › Lactobacillus

Protein attributes

Sequence length	574 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	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.
Catalytic activity	Phosphoenolpyruvate + protein L-histidine = pyruvate + protein N(pi)-phospho-L-histidine.
Cofactor	Magnesium By similarity.
Subcellular location	Cytoplasm By similarity.
Domain	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.
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.
Sequence similarities	Belongs to the PEP-utilizing enzyme family.

Ontologies

Keywords
Biological process	Phosphotransferase system Sugar transport Transport
Cellular component	Cytoplasm
Ligand	Magnesium Metal-binding
Molecular function	Kinase Transferase
Gene Ontology (GO)
Biological process	phosphoenolpyruvate-dependent sugar phosphotransferase system Inferred from electronic annotation. Source: UniProtKB-KW phosphorylation Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	kinase activity Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW phosphoenolpyruvate-protein phosphotransferase activity Inferred from electronic annotation. Source: EC sugar:hydrogen symporter activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 574	574	Phosphoenolpyruvate-protein phosphotransferase		PRO_0000147072
Sites
	Active site	190	1	Tele-phosphohistidine intermediate By similarity
	Active site	503	1	Proton donor By similarity
	Metal binding	432	1	Magnesium By similarity
	Metal binding	456	1	Magnesium By similarity
	Binding site	297	1	Substrate By similarity
	Binding site	333	1	Substrate By similarity
	Binding site	432	1	Substrate By similarity
	Binding site	453	1	Substrate; via carbonyl oxygen By similarity
	Binding site	454	1	Substrate; via amide nitrogen By similarity
	Binding site	455	1	Substrate By similarity
	Binding site	456	1	Substrate; via amide nitrogen By similarity

Sequences

	Sequence		Length	Mass (Da)
	O07126-1 [UniParc]. Last modified July 1, 1997. Version 1. Checksum: 5544473E7292DBF1	FASTA	574	63,009
	10 20 30 40 50 60 MTKLRGIAAS DGIATAKAYM LVQPDLSFSK STISDSEKEI NRLHKALQDS TSDLETIRKI 70 80 90 100 110 120 AAESLGEEEA QVFDAHMMIL ADPEFTGAIE GKINDDKVNA EQALKEVADL FVATFESMTN 130 140 150 160 170 180 NAYMQERAAD IKDVTKRVLS HLLGVTLPNP ALIDEEVIVI AHDLTPSDTA QLNGKFVKAF 190 200 210 220 230 240 VTDVGGRTSH SAIMARSLEI PAIVGTETVT QDVKAGDLLI VDGINGDVVL DPTDADIAEY 250 260 270 280 290 300 DVKAQAFADQ KAEWEKLKNE KSVTKDGKTF TVAANIGTPK DLAGVLENGS EAIGLYRTEF 310 320 330 340 350 360 LYMDSAELPS EDDQFEAYKS VLEGMDGKPV VVRTMDIGGD KKLPYLPLPE EMNPFLGYRA 370 380 390 400 410 420 IRISLDRDDI FRTQLRALLR ASNYGKLRIM FPMIATVAEF RQAKGILEDE KAKLIAAGQT 430 440 450 460 470 480 VSDDLQVGMM VEIPASAVLA NQFAKEVDFF SIGTNDLIQY TMAADRMNER VSYLYQPYNP 490 500 510 520 530 540 AILRLIKNVI DASHKEGKWT GMCGEAAGDS IMAPLLVGMG LDEFSMSATS VLRVRSLMKR 550 560 570 LDTTELTDLV ETAVNVNTSN EENQKLVEDF MKDR

References

[1]	"Molecular cloning and analysis of the ptsHI operon in Lactobacillus sake." Stentz R., Lauret R., Ehrlich S.D., Morel-Deville F., Zagorec M. Appl. Environ. Microbiol. 63:2111-2116(1997) [PubMed: 9172326] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 160*1.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U82366 Genomic DNA. Translation: AAC45391.1.
3D structure databases
HSSP	HSSP built from PDB template 1EZC based on UniProtKB P08839.
ModBase	Search...
Enzyme and pathway databases
BRENDA	2.7.3.9. 273663.
Family and domain databases
InterPro	IPR008279. PEP_mobile. IPR018274. PEP_mobile_CS. IPR006318. PEP_P_trans. IPR000121. PEP_utilizers. IPR008731. PTS_PEP_utilis_N. IPR015813. Pyrv/PenolPyrv_Kinase_cat. [Graphical view]
Gene3D	G3DSA:3.50.30.10. PEP_mobile. 1 hit. G3DSA:1.10.274.10. PTS_PEP_utilis_N. 1 hit. G3DSA:3.20.20.60. Pyrv/PenolPyrv_Kinase_cat. 1 hit.
Pfam	PF05524. PEP-utilisers_N. 1 hit. PF00391. PEP-utilizers. 1 hit. PF02896. PEP-utilizers_C. 1 hit. [Graphical view]
PRINTS	PR01736. PHPHTRNFRASE.
ProDom	PD000940. PEP_utilizers. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR01417. PTS_I_fam. 1 hit.
PROSITE	PS00742. PEP_ENZYMES_2. 1 hit. PS00370. PEP_ENZYMES_PHOS_SITE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PT1_LACSK

Accession

Primary (citable) accession number: O07126

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	July 1, 1997
Last modified:	September 22, 2009
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)