Q9ZAD8 (PT1_LACLC) 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

Organism

Lactococcus lactis subsp. cremoris (Streptococcus cremoris)

Taxonomic identifier

1359 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Lactobacillales › Streptococcaceae › Lactococcus

Protein attributes

Sequence length	575 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).
Catalytic activity	Phosphoenolpyruvate + protein L-histidine = pyruvate + protein N(pi)-phospho-L-histidine.
Cofactor	Magnesium 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
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 – 575	575	Phosphoenolpyruvate-protein phosphotransferase		PRO_0000147071
Sites
	Active site	191	1	Tele-phosphohistidine intermediate By similarity
	Active site	506	1	Proton donor By similarity
	Metal binding	435	1	Magnesium By similarity
	Metal binding	459	1	Magnesium By similarity
	Binding site	298	1	Substrate By similarity
	Binding site	334	1	Substrate By similarity
	Binding site	435	1	Substrate By similarity
	Binding site	456	1	Substrate; via carbonyl oxygen By similarity
	Binding site	457	1	Substrate; via amide nitrogen By similarity
	Binding site	458	1	Substrate By similarity
	Binding site	459	1	Substrate; via amide nitrogen By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9ZAD8 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: 3737EED048498B11	FASTA	575	62,577
	10 20 30 40 50 60 MTTMLKGIAA SSGVAVAKAY LLVQPDLSFE TKTIADTANE EARLDAALAT SQSELQLIKD 70 80 90 100 110 120 KAVTTLGEEA ASVFDAHMMV LADPDMTAQI KAVINDKKVN AESALKEVTD MFIGIFEGMT 130 140 150 160 170 180 DNAYMQERAA DIKDVTKRVL AHLLGVKLPS PALIDEEVII VAEDLTPSDT AQLDKKFVKA 190 200 210 220 230 240 FVTNIGGRTS HSAIMARTLE IPAVLGTNNI TELVSEGQLL AVSGLTGEVI LDPSTEQQSE 250 260 270 280 290 300 FHKAGDAYAA QKAEWAALKD AETVTADGRH YELAANIGTP KDVEGVNDNG AEAIGLYRTE 310 320 330 340 350 360 FLYMDAQDFP TEDDQYEAYK AVLEGMNGKP VVVRTMDIGG DKTLPYFDLP KEMNPFLGWR 370 380 390 400 410 420 ALRISLSTAG DGMFRTQLRA LLRASVHGQL RIMFPMVALV TEFRAAKKIY DEEKSKLIAE 430 440 450 460 470 480 GVPVAEGIEV GIMIEIPAAA MLADQFAKEV DFFSIGTNDL IQYTMAADRM NEQVSYLYQP 490 500 510 520 530 540 YNPSILRLIN NVIKAAHAEG KWAGMCGEMA GDQTAVPLLM GMGLDEFSMS ATSVLQTRSL 550 560 570 MKRLDSKKME ELSSKALSEC ATMEEVIALV EEYTK

References

[1]	"Molecular characterization of the Lactococcus lactis ptsHI operon and analysis of the regulatory role of HPr." Luesink E.J., Beumer C.M.A., Kuipers O.P., de Vos W.M. J. Bacteriol. 181:764-771(1999) [PubMed: 9922238] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z97203 Genomic DNA. Translation: CAB10077.1.
3D structure databases
ProteinModelPortal	Q9ZAD8.
SMR	Q9ZAD8. Positions 5-575.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
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.
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_LACLC

Accession

Primary (citable) accession number: Q9ZAD8

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	May 1, 1999
Last modified:	October 19, 2011
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program