Reviewed, UniProtKB/Swiss-Prot P42015 (PTG3C_BACST)

Names and origin

Protein names

Recommended name:
    PTS system glucose-specific EIICBA component
Alternative name(s):
    EIICBA-Glc
    EII-Glc/EIII-Glc
Including the following 3 domains:
    1- Recommended name:
            Glucose permease IIC component
        Alternative name(s):
            PTS system glucose-specific EIIC component
    2- Recommended name:
            Glucose-specific phosphotransferase enzyme IIB component
              EC=2.7.1.69
        Alternative name(s):
            PTS system glucose-specific EIIB component
    3- Recommended name:
            Glucose-specific phosphotransferase enzyme IIA component
              EC=2.7.1.-
        Alternative name(s):
            PTS system glucose-specific EIIA component

Gene names

Name:

ptsG

Organism

Bacillus stearothermophilus (Geobacillus stearothermophilus)

Taxonomic identifier

1422 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Geobacillus

Protein attributes

Sequence length	324 AA.
Sequence status	Fragment.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active -transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. This system is involved in glucose transport By similarity.
Catalytic activity	Protein EIIA N(pi)-phospho-L-histidine + protein EIIB = protein EIIA + protein EIIB N(pi)-phospho-L-histidine/cysteine. Protein EIIB N(pi)-phospho-L-histidine/cysteine + sugar = protein EIIB + sugar phosphate.
Subcellular location	Cell membrane; Multi-pass membrane protein Potential.
Domain	The EIIC domain forms the PTS system translocation channel and contains the specific substrate-binding site. The EIIB domain is phosphorylated by phospho-EIIA on a cysteinyl or histidyl residue, depending on the transported sugar. Then, it transfers the phosphoryl group to the sugar substrate concomitantly with the sugar uptake processed by the EIIC domain. The EIIA domain is phosphorylated by phospho-HPr on a histidyl residue. Then, it transfers the phosphoryl group to the EIIB domain.
Sequence similarities	Contains 1 PTS EIIA type-1 domain. Contains 1 PTS EIIB type-1 domain. Contains 1 PTS EIIC type-1 domain.

Ontologies

Keywords
Biological process	Phosphotransferase system Sugar transport Transport
Cellular component	Cell membrane Membrane
Domain	Transmembrane
Molecular function	Kinase Transferase
Gene Ontology (GO)
Biological process	phosphoenolpyruvate-dependent sugar phosphotransferase system Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	kinase activity Inferred from electronic annotation. Source: UniProtKB-KW protein-N(PI)-phosphohistidine-sugar 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 – 324	›324	PTS system glucose-specific EIICBA component		PRO_0000186556
Regions
	Transmembrane	5 – 25	21	Potential
	Transmembrane	28 – 48	21	Potential
	Domain	‹1 – 63	›63	PTS EIIC type-1
	Domain	78 – 159	82	PTS EIIB type-1
	Domain	194 – 298	105	PTS EIIA type-1
Sites
	Active site	100	1	Phosphocysteine intermediate; for EIIB activity By similarity
	Active site	246	1	Tele-phosphohistidine intermediate; for EIIA activity By similarity
Experimental info
	Non-terminal residue	1	1

Sequences

	Sequence		Length	Mass (Da)
	P42015-1 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 89B712E6A6624F3F	FASTA	324	34,674
	10 20 30 40 50 60 HLLNVKIGMT FSGGVIDFLL FGVLPNRTAW WLVIPVGLVF AVIYYFGFRF AIRKWDLATP 70 80 90 100 110 120 GREKTVEEAP KAEAAAAGDL PYEVLAALGG KENIEHLDAC ITRLRVSVHD IGRVDKDRLK 130 140 150 160 170 180 ALGAAGVLEV GNNVQAIFGP KSDMLKGQIQ DIMQGKAPAR AEEKPKTAAS EAAESETIAS 190 200 210 220 230 240 PMSGEIVPLA EVPDQVFSQK MMGDGFAVMP TDGTVVSPVD GKIINVFPTK HAIGIQSAGG 250 260 270 280 290 300 HEILIHVGID TVKLNGQGFE ALVKEGDEVK KGQPILRVDL DYVKQNAPSI VTPVIFTNLQ 310 320 AGETVHVNKQ GPVARGEDAV VTIR

References

[1]	"Discovery of a ptsHI operon, which includes a third gene (ptsT), in the thermophile Bacillus stearothermophilus." Lai X., Ingram L.O. Microbiology 141:1443-1449(1995) [PubMed: 7670643] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: XL-65-6.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U12340 Genomic DNA. Translation: AAA86047.1.
3D structure databases
HSSP	HSSP built from PDB template 1GPR based on UniProtKB P20166.
ModBase	Search...
Enzyme and pathway databases
BRENDA	2.7.1.69. 266715.
Family and domain databases
InterPro	IPR018113. PTrfase_EIIB/Cys_phosph_CS. IPR001127. PTS_EIIA_1_perm. IPR001996. PTS_EIIB. IPR011535. PTS_Glc-like_IIB_component. [Graphical view]
Pfam	PF00358. PTS_EIIA_1. 1 hit. PF00367. PTS_EIIB. 1 hit. [Graphical view]
ProDom	PD002243. PTS_EIIA. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR00826. EIIB_glc. 1 hit. TIGR00830. PTBA. 1 hit.
PROSITE	PS51093. PTS_EIIA_TYPE_1. 1 hit. PS00371. PTS_EIIA_TYPE_1_HIS. 1 hit. PS51098. PTS_EIIB_TYPE_1. 1 hit. PS01035. PTS_EIIB_TYPE_1_CYS. 1 hit. PS51103. PTS_EIIC_TYPE_1. Partial match. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PTG3C_BACST

Accession

Primary (citable) accession number: P42015

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	October 13, 2009
This is version 68 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)