Q8KA50 (PT1_BUCAP) Reviewed, UniProtKB/Swiss-Prot

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
Ordered Locus Names:	BUsg_061

Organism

Buchnera aphidicola subsp. Schizaphis graminum (strain Sg) [Complete proteome] [HAMAP]

Taxonomic identifier

198804 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera

Protein attributes

Sequence length	570 AA.
Sequence status	Complete.
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.
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm.
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
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	phosphoenolpyruvate-dependent sugar phosphotransferase system Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	kinase activity Inferred from electronic annotation. Source: UniProtKB-KW metal 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 – 570	570	Phosphoenolpyruvate-protein phosphotransferase		PRO_0000147062
Sites
	Active site	189	1	Tele-phosphohistidine intermediate By similarity
	Active site	502	1	Proton donor By similarity
	Metal binding	431	1	Magnesium By similarity
	Metal binding	455	1	Magnesium By similarity
	Binding site	296	1	Substrate By similarity
	Binding site	332	1	Substrate By similarity
	Binding site	431	1	Substrate By similarity
	Binding site	452	1	Substrate; via carbonyl oxygen By similarity
	Binding site	453	1	Substrate; via amide nitrogen By similarity
	Binding site	454	1	Substrate By similarity
	Binding site	455	1	Substrate; via amide nitrogen By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8KA50 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: 3E8F880BDAF024BD	FASTA	570	64,357
	10 20 30 40 50 60 MISGILASPG IAFGNVLLLK KEEIVINRQN ISTENIKTEI NKFFNGRKKS VKQLTEIKIA 70 80 90 100 110 120 TGEKFGKKKE GIFEGHIMLL EDEELEKEII NLITEKKISA AEATKFIIEG QAKALEKIKD 130 140 150 160 170 180 EYLKNRAIDV RDIGSRLLKN ILNISIVDLN NIKNQVILIS KDLTPSETAQ INLKYILGFI 190 200 210 220 230 240 TDLGGPTSHT SIMARSLEIP AIVGTVNITK KVKNNDFIIL DSLNNEIIIN PSDQIINEKK 250 260 270 280 290 300 QVERKYFFKK ENLKKLRNLY ATTTDGHNIK IGSNIGNIQD IYSAKKNGAE CIGLYRTEFL 310 320 330 340 350 360 FMGRNALPTE NEQFQAYKEI AESMENKPVI IRTMDIGGDK DLPYMNLPKE ENPFLGWRAI 370 380 390 400 410 420 RISMDRKEIL HAQLRAILRA SAFGKIYILF PMIISVEEIR TLKIEVHKLQ IQLKKEHLVF 430 440 450 460 470 480 DENIKIGIMI ETPASAIIAD HLIKEVDFFS IGTNDLTQYT LAVDRGNDLI SHLYNPISPS 490 500 510 520 530 540 VIQLIKQVID ISHLHGKWTG MCGELAGDER VTTLLLGMGL DEFSMSSTSI PKIKEIIRKT 550 560 570 SFSKSQELAK KVLKAATTKE ILDLLNKFII

References

[1]	"50 million years of genomic stasis in endosymbiotic bacteria." Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E. Science 296:2376-2379(2002) [PubMed: 12089438] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Sg.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE013218 Genomic DNA. Translation: AAM67632.1.
RefSeq	NP_660421.1. NC_004061.1.
3D structure databases
ProteinModelPortal	Q8KA50.
SMR	Q8KA50. Positions 2-569.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBUCT00000000168; EBBUCP00000000168; EBBUCG00000000168.
GeneID	1005877.
GenomeReviews	Gene locus BUsg_061 in contig AE013218_GR.
KEGG	bas:BUsg061.
PATRIC	21246887. VBIBucAph100086_0061.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000007917.
HOGENOM	HBG456539.
OMA	IFRASHY.
ProtClustDB	PRK11177.
Enzyme and pathway databases
BioCyc	BAPH198804:BUSG061-MONOMER.
Family and domain databases
InterPro	IPR008279. PEP-util_enz_mobile_dom. IPR018274. PEP_util_AS. IPR000121. PEP_util_C. IPR023151. PEP_util_CS. IPR006318. PEP_util_enz. IPR024692. PTS_enz_I. IPR008731. PTS_PEP_utilis_N. IPR015813. Pyrv/PenolPyrv_Kinase. [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.
KO	K08483.
PANTHER	PTHR22931:SF10. PTHR22931:SF10. 1 hit.
Pfam	PF05524. PEP-utilisers_N. 1 hit. PF00391. PEP-utilizers. 1 hit. PF02896. PEP-utilizers_C. 1 hit. [Graphical view]
PIRSF	PIRSF000732. PTS_enzyme_I. 1 hit.
PRINTS	PR01736. PHPHTRNFRASE.
SUPFAM	SSF47831. PEP-utilisers_N. 1 hit. SSF52009. PEP_mobile. 1 hit. SSF51621. Pyrv/PenolPyrv_Kinase_cat. 1 hit.
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_BUCAP

Accession

Primary (citable) accession number: Q8KA50

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 15, 2002
Last sequence update:	October 1, 2002
Last modified:	January 25, 2012
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program