P37178 (PT1P_SALTY) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Phosphoenolpyruvate-protein phosphotransferase ptsP
EC=2.7.3.9

Alternative name(s):
Enzyme I-Ntr
Phosphotransferase system, enzyme I

Gene names

Name:	ptsP
Ordered Locus Names:	STM3003

Organism

Salmonella typhimurium

Taxonomic identifier

90371 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella

Protein attributes

Sequence length	748 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Component of the phosphoenolpyruvate-dependent nitrogen-metabolic phosphotransferase system (nitrogen-metabolic PTS), that seems to be involved in regulating nitrogen metabolism. Enzyme I-Ntr transfers the phosphoryl group from phosphoenolpyruvate (PEP) to the phosphoryl carrier protein (NPr). Could function in the transcriptional regulation of sigma-54 dependent operons in conjunction with the NPr (ptsO) and EIIA-Ntr (ptsN) proteins By similarity.
Catalytic activity	Phosphoenolpyruvate + protein L-histidine = pyruvate + protein N(pi)-phospho-L-histidine.
Cofactor	Magnesium By similarity.
Subcellular location	Cytoplasm Probable.
Domain	The GAF domain is an important site of signal perception in prokaryotes and eukaryotes. The EI 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. Contains 1 GAF domain.

Ontologies

Keywords
Biological process	Phosphotransferase system Sugar transport Transport
Cellular component	Cytoplasm
Ligand	Magnesium Metal-binding
Molecular function	Kinase Transferase
Technical term	Complete proteome Reference 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 – 748	748	Phosphoenolpyruvate-protein phosphotransferase ptsP		PRO_0000147096
Regions
	Domain	1 – 127	127	GAF
	Region	128 – 170	43	Linker
	Region	171 – 748	578	PTS EI
Sites
	Active site	356	1	Tele-phosphohistidine intermediate By similarity
	Active site	668	1	Proton donor By similarity
	Metal binding	597	1	Magnesium By similarity
	Metal binding	621	1	Magnesium By similarity
	Binding site	462	1	Substrate By similarity
	Binding site	498	1	Substrate By similarity
	Binding site	597	1	Substrate By similarity
	Binding site	618	1	Substrate; via carbonyl oxygen By similarity
	Binding site	619	1	Substrate; via amide nitrogen By similarity
	Binding site	620	1	Substrate By similarity
	Binding site	621	1	Substrate; via amide nitrogen By similarity

Sequences

	Sequence		Length	Mass (Da)
	P37178 [UniParc]. Last modified December 13, 2001. Version 2. Checksum: 46799C4447B75189	FASTA	748	83,627
	10 20 30 40 50 60 MLTRLREIVE KVASAPRLNE ALNILVTDIC LAMDTEVCSV YLADHDRRCY YLMATRGLKK 70 80 90 100 110 120 PRGRTVALAF DEGIVGLVGR LAEPINLADA QKHPSFKYIP SVKEERFRAF LGVPIIQRRQ 130 140 150 160 170 180 LLGVLVVQQR ELRQYDESEE SFLVTLATQM AAILSQSQVT ALFGQYRQTR IRALPAAPGV 190 200 210 220 230 240 AIATGWQDAT MPLMEQVYEA STLDTSLERE RLTGALEEAA NEFRRYSKRF AAGAQKETAA 250 260 270 280 290 300 IFDLYSHLLS DARLRRELFA EVDKGAVAEW AVKKIIEKFA EQFAALTDNY LKERAGDLRT 310 320 330 340 350 360 LGQRLLFHLD DSVQGPNAWP ERFILVADEL SATTLAELPQ DRLAGVVVRD GAANSHAAIM 370 380 390 400 410 420 VRALGIPTVM GADIQPSVLH RRTLVVDGYR GELLVDPEPV LIQEYQRLIS EEIELSRLAE 430 440 450 460 470 480 DDVNLPAQLK SGERVKVMLN AGLSPEHEEK LGSRIDGIGL YRTEIPFMLQ SGFPSEEEQV 490 500 510 520 530 540 AQYQGMLQMF NDKPVTLRTL DVGADKQLPY MPISEENPCL GWRGIRITLD QPEIFLIQVR 550 560 570 580 590 600 AMLRANAATG NLSILLPMVT SIDEVDEARR LIERAGREVE EMIGYAIPKP RIGIMLEVPS 610 620 630 640 650 660 MVFMLPHLAN RIDFISVGTN DLTQYILAVD RNNTRVASIY DSLHPAMLRA LSMIAQEAEK 670 680 690 700 710 720 HGLDLRLCGE MAGDPMCVAI LIGLGYRHLS MNGRSVARVK YLLRHIDFED AQTLARRSLE 730 740 AQMATEVRHQ VAAFMERRGM GGLIRGGL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2." McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K. Nature 413:852-856(2001) [PubMed: 11677609] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: LT2 / SGSC1412 / ATCC 700720.
[2]	"Isolation and characterization of a temperature-sensitive mutant of Salmonella typhimurium defective in prolipoprotein modification." Gan K., Gupta S.D., Sankaran K., Schmid M.B., Wu H.C. J. Biol. Chem. 268:16544-16550(1993) [PubMed: 8344935] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 664-748. Strain: LT2.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE006468 Genomic DNA. Translation: AAL21879.1. L13259 Genomic DNA. Translation: AAA20895.1.
PIR	B47354.
RefSeq	NP_461920.1. NC_003197.1.
3D structure databases
ProteinModelPortal	P37178.
ModBase	Search...
Proteomic databases
PRIDE	P37178.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1254526.
GenomeReviews	Gene locus STM3003 in contig AE006468_GR.
KEGG	stm:STM3003.
NMPDR	fig|99287.1.peg.2896.
PATRIC	32384737. VBISalEnt20916_3178.
Phylogenomic databases
HOGENOM	HBG456539.
OMA	IFLIQLR.
ProtClustDB	PRK11061.
Enzyme and pathway databases
BioCyc	STYP99287:STM3003-MONOMER.
Family and domain databases
InterPro	IPR003018. GAF. IPR008279. PEP-util_enz_mobile_dom. IPR018274. PEP_util_AS. IPR000121. PEP_util_C. IPR023151. PEP_util_CS. IPR006318. PEP_util_enz. 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	K08484.
PANTHER	PTHR22931:SF10. PTHR22931:SF10. 1 hit.
Pfam	PF01590. GAF. 1 hit. PF05524. PEP-utilisers_N. 1 hit. PF00391. PEP-utilizers. 1 hit. PF02896. PEP-utilizers_C. 1 hit. [Graphical view]
PRINTS	PR01736. PHPHTRNFRASE.
SMART	SM00065. GAF. 1 hit. [Graphical view]
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

PT1P_SALTY

Accession

Primary (citable) accession number: P37178

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	December 13, 2001
Last modified:	January 25, 2012
This is version 93 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program