Reviewed, UniProtKB/Swiss-Prot P20166 (PTG3C_BACSU)

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
Synonyms:	crr, ptsX
Ordered Locus Names:	BSU13890

Organism

Bacillus subtilis [Complete proteome] [HAMAP]

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	699 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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.
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.
Domain	The EIIC domain forms the PTS system translocation channel and contains the specific substrate-binding site. Ref.6 Ref.7 Ref.8 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. Ref.6 Ref.7 Ref.8 The EIIA domain is phosphorylated by phospho-HPr on a histidyl residue. Then, it transfers the phosphoryl group to the EIIB domain. Ref.6 Ref.7 Ref.8
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
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	glucose transport Inferred from electronic annotation. Source: InterPro 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	glucose transmembrane transporter activity Inferred from electronic annotation. Source: InterPro 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 – 699

699

PTS system glucose-specific EIICBA component

PRO_0000186557

Regions

Transmembrane

16 – 36

21

Potential

Transmembrane

66 – 86

21

Potential

Transmembrane

89 – 109

21

Potential

Transmembrane

139 – 159

21

Potential

Transmembrane

180 – 200

21

Potential

Transmembrane

233 – 253

21

Potential

Transmembrane

283 – 303

21

Potential

Transmembrane

313 – 333

21

Potential

Transmembrane

338 – 358

21

Potential

Transmembrane

365 – 385

21

Potential

Transmembrane

388 – 408

21

Potential

Domain

1 – 424

424

PTS EIIC type-1

Domain

439 – 520

82

PTS EIIB type-1

Domain

568 – 672

105

PTS EIIA type-1

Sites

Active site

461

1

Phosphocysteine intermediate; for EIIB activity By similarity

Active site

620

1

Tele-phosphohistidine intermediate; for EIIA activity By similarity

Secondary structure

1

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699

Helix Strand Turn

Details...

Beta strand

555 – 562

8

Helix

563 – 565

3

Beta strand

566 – 568

3

Helix

569 – 572

4

Beta strand

578 – 586

9

Beta strand

588 – 590

3

Beta strand

592 – 600

9

Beta strand

604 – 611

8

Beta strand

616 – 620

5

Beta strand

622 – 624

3

Helix

626 – 628

3

Turn

629 – 632

4

Beta strand

633 – 635

3

Beta strand

648 – 652

5

Helix

654 – 657

4

Helix

658 – 660

3

Beta strand

661 – 663

3

Beta strand

666 – 672

7

Beta strand

678 – 681

4

Beta strand

685 – 687

3

Beta strand

695 – 698

4

Sequences

	Sequence		Length	Mass (Da)
	P20166-1 [UniParc]. Last modified December 1, 1992. Version 2. Checksum: 2A14D3C32EE0A9C5	FASTA	699	75,525
	10 20 30 40 50 60 MFKALFGVLQ KIGRALMLPV AILPAAGILL AIGNAMQNKD MIQVLHFLSN DNVQLVAGVM 70 80 90 100 110 120 ESAGQIVFDN LPLLFAVGVA IGLANGDGVA GIAAIIGYLV MNVSMSAVLL ANGTIPSDSV 130 140 150 160 170 180 ERAKFFTENH PAYVNMLGIP TLATGVFGGI IVGVLAALLF NRFYTIELPQ YLGFFAGKRF 190 200 210 220 230 240 VPIVTSISAL ILGLIMLVIW PPIQHGLNAF STGLVEANPT LAAFIFGVIE RSLIPFGLHH 250 260 270 280 290 300 IFYSPFWYEF FSYKSAAGEI IRGDQRIFMA QIKDGVQLTA GTFMTGKYPF MMFGLPAAAL 310 320 330 340 350 360 AIYHEAKPQN KKLVAGIMGS AALTSFLTGI TEPLEFSFLF VAPVLFAIHC LFAGLSFMVM 370 380 390 400 410 420 QLLNVKIGMT FSGGLIDYFL FGILPNRTAW WLVIPVGLGL AVIYYFGFRF AIRKFNLKTP 430 440 450 460 470 480 GREDAAEETA APGKTGEAGD LPYEILQAMG DQENIKHLDA CITRLRVTVN DQKKVDKDRL 490 500 510 520 530 540 KQLGASGVLE VGNNIQAIFG PRSDGLKTQM QDIIAGRKPR PEPKTSAQEE VGQQVEEVIA 550 560 570 580 590 600 EPLQNEIGEE VFVSPITGEI HPITDVPDQV FSGKMMGDGF AILPSEGIVV SPVRGKILNV 610 620 630 640 650 660 FPTKHAIGLQ SDGGREILIH FGIDTVSLKG EGFTSFVSEG DRVEPGQKLL EVDLDAVKPN 670 680 690 VPSLMTPIVF TNLAEGETVS IKASGSVNRE QEDIVKIEK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and nucleotide sequence of the ptsG gene of Bacillus subtilis." Zagorec M., Postma P.W. Mol. Gen. Genet. 234:325-328(1992) [PubMed: 1508157] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A. Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[3]	"Phosphoenolpyruvate:sugar phosphotransferase system of Bacillus subtilis: nucleotide sequence of ptsX, ptsH and the 5'-end of ptsI and evidence for a ptsHI operon." Gonzy-Treboul G., Zagorec M., Rain-Guion M.-C., Steinmetz M. Mol. Microbiol. 3:103-112(1989) [PubMed: 2497294] [Abstract] Cited for: PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 361-699. Strain: 168.
[4]	"The glucose permease of the phosphotransferase system of Bacillus subtilis: evidence for IIGlc and IIIGlc domains." Gonzy-Treboul G., de Waard J.H., Zagorec M., Postma P.W. Mol. Microbiol. 5:1241-1249(1991) [PubMed: 1956301] [Abstract] Cited for: SEQUENCE REVISION.
[5]	"The glucose permease of Bacillus subtilis is a single polypeptide chain that functions to energize the sucrose permease." Sutrina S.L., Reddy P., Saier M.H. Jr., Reizer J. J. Biol. Chem. 265:18581-18589(1990) [PubMed: 2120236] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 483-558.
[6]	"Structure of the IIA domain of the glucose permease of Bacillus subtilis at 2.2-A resolution." Liao D.-I., Kapadia G., Reddy P., Saier M.H. Jr., Reizer J., Herzberg O. Biochemistry 30:9583-9594(1991) [PubMed: 1911744] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF EIII-GLC DOMAIN.
[7]	"Polypeptide backbone resonance assignments and secondary structure of Bacillus subtilis enzyme IIIglc determined by two-dimensional and three-dimensional heteronuclear NMR spectroscopy." Fairbrother W.J., Cavanagh J., Dyson H.J., Plamer A.G. III, Sutrina S.L., Reizer J., Saier M.H. Jr., Wright P.E. Biochemistry 30:6896-6907(1991) [PubMed: 1906345] [Abstract] Cited for: STRUCTURE BY NMR OF EIIA DOMAIN.
[8]	"High-resolution solution structure of Bacillus subtilis IIAglc." Chen Y., Case D.A., Reizer J., Saier M.H. Jr., Wright P.E. Proteins 31:258-270(1998) [PubMed: 9593197] [Abstract] Cited for: STRUCTURE BY NMR OF EIAA DOMAIN.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

Z11744 Genomic DNA. Translation: CAA77803.1.
AL009126 Genomic DNA. Translation: CAB13262.1.
X12832 Genomic DNA. Translation: CAA31315.1.
M60344 Genomic DNA. Translation: AAA22498.1.

PIR

WQBSGS. S25083.

RefSeq

NP_389272.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AX3	NMR	-	A	539-699	[»]
1GPR	X-ray	1.90	A	539-699	[»]

ModBase

Search...

Protein family/group databases

TCDB

4.A.1.1.9. PTS glucose-glucoside (Glc) family.

Genome annotation databases

GeneID

939255.

GenomeReviews

Gene locus BSU13890 in contig AL009126_GR.

KEGG

bsu:BSU13890.

NMPDR

fig|224308.1.peg.1391.

Organism-specific databases

SubtiList

BG10198. ptsG. [Micado]

CMR

Search...

Phylogenomic databases

HOGENOM

P20166.

OMA

RCASPEN.

Enzyme and pathway databases

BioCyc

BSUB224308:BSU1391-MON.

BRENDA

2.7.1.69. 150.

Family and domain databases

InterPro

IPR018113. PTrfase_EIIB/Cys_phosph_CS.
IPR004719. PTrfase_sys_maltose/Glc-sp_IIC.
IPR001127. PTS_EIIA_1_perm.
IPR001996. PTS_EIIB.
IPR003352. PTS_EIIC.
IPR013013. PTS_EIIC_1.
IPR011535. PTS_Glc-like_IIB_component.
IPR011299. PTS_IIBC_glc.
[Graphical view]

Gene3D

G3DSA:3.30.1360.60. PTS_EIIB. 1 hit.

Pfam

PF00358. PTS_EIIA_1. 1 hit.
PF00367. PTS_EIIB. 1 hit.
PF02378. PTS_EIIC. 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.
TIGR00852. pts-Glc. 1 hit.
TIGR02002. PTS-II-BC-glcB. 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. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

PTG3C_BACSU

Accession

Primary (citable) accession number: P20166
Secondary accession number(s): P08875

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	December 1, 1992
Last modified:	November 3, 2009
This is version 100 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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