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Protein

PTS system glucose-specific EIICBA component

Gene

ptsG

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

Protein EIIA N(pi)-phospho-L-histidine + protein EIIB = protein EIIA + protein EIIB N(pi)-phospho-L-histidine/cysteine.PROSITE-ProRule annotation
Protein EIIB N(pi)-phospho-L-histidine/cysteine + sugar = protein EIIB + sugar phosphate.PROSITE-ProRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei461 – 4611Phosphocysteine intermediate; for EIIB activityPROSITE-ProRule annotation
Active sitei620 – 6201Tele-phosphohistidine intermediate; for EIIA activityPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Phosphotransferase system, Sugar transport, Transport

Enzyme and pathway databases

BioCyciBSUB:BSU13890-MONOMER.

Protein family/group databases

TCDBi4.A.1.1.9. the pts glucose-glucoside (glc) family.

Names & Taxonomyi

Protein namesi
Recommended name:
PTS system glucose-specific EIICBA component
Alternative name(s):
EII-Glc/EIII-Glc
EIICBA-Glc
Including the following 3 domains:
Glucose permease IIC component
Alternative name(s):
PTS system glucose-specific EIIC component
Glucose-specific phosphotransferase enzyme IIB component (EC:2.7.1.69)
Alternative name(s):
PTS system glucose-specific EIIB component
Glucose-specific phosphotransferase enzyme IIA component (EC:2.7.1.-)
Alternative name(s):
PTS system glucose-specific EIIA component
Gene namesi
Name:ptsG
Synonyms:crr, ptsX
Ordered Locus Names:BSU13890
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570 Componenti: Chromosome

Organism-specific databases

GenoListiBSU13890. [Micado]

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei16 – 3621HelicalPROSITE-ProRule annotationAdd
BLAST
Transmembranei66 – 8621HelicalPROSITE-ProRule annotationAdd
BLAST
Transmembranei89 – 10921HelicalPROSITE-ProRule annotationAdd
BLAST
Transmembranei139 – 15921HelicalPROSITE-ProRule annotationAdd
BLAST
Transmembranei180 – 20021HelicalPROSITE-ProRule annotationAdd
BLAST
Transmembranei233 – 25321HelicalPROSITE-ProRule annotationAdd
BLAST
Transmembranei283 – 30321HelicalPROSITE-ProRule annotationAdd
BLAST
Transmembranei313 – 33321HelicalPROSITE-ProRule annotationAdd
BLAST
Transmembranei338 – 35821HelicalPROSITE-ProRule annotationAdd
BLAST
Transmembranei365 – 38521HelicalPROSITE-ProRule annotationAdd
BLAST
Transmembranei388 – 40821HelicalPROSITE-ProRule annotationAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 699699PTS system glucose-specific EIICBA componentPRO_0000186557Add
BLAST

Proteomic databases

PaxDbiP20166.

Interactioni

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100007711.

Structurei

Secondary structure

1
699
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi557 – 5626Combined sources
Helixi563 – 5653Combined sources
Beta strandi566 – 5683Combined sources
Helixi569 – 5724Combined sources
Beta strandi577 – 5848Combined sources
Beta strandi586 – 5927Combined sources
Beta strandi595 – 5995Combined sources
Beta strandi602 – 61413Combined sources
Beta strandi616 – 6205Combined sources
Beta strandi622 – 6243Combined sources
Turni625 – 6328Combined sources
Beta strandi633 – 6364Combined sources
Beta strandi641 – 6433Combined sources
Beta strandi645 – 6528Combined sources
Helixi654 – 6574Combined sources
Helixi658 – 6603Combined sources
Beta strandi666 – 6727Combined sources
Helixi673 – 6753Combined sources
Beta strandi678 – 6814Combined sources
Beta strandi685 – 6873Combined sources
Beta strandi692 – 6987Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AX3NMR-A539-699[»]
1GPRX-ray1.90A539-699[»]
ProteinModelPortaliP20166.
SMRiP20166. Positions 438-516, 541-698.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP20166.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 424424PTS EIIC type-1PROSITE-ProRule annotationAdd
BLAST
Domaini439 – 52082PTS EIIB type-1PROSITE-ProRule annotationAdd
BLAST
Domaini568 – 672105PTS EIIA type-1PROSITE-ProRule annotationAdd
BLAST

Domaini

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 similaritiesi

Contains 1 PTS EIIA type-1 domain.PROSITE-ProRule annotation
Contains 1 PTS EIIB type-1 domain.PROSITE-ProRule annotation
Contains 1 PTS EIIC type-1 domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1263.
HOGENOMiHOG000250993.
InParanoidiP20166.
KOiK02763.
K02764.
K02765.
OMAiSFNGYQT.
OrthoDBiEOG6FFS9V.
PhylomeDBiP20166.

Family and domain databases

Gene3Di3.30.1360.60. 1 hit.
InterProiIPR011055. Dup_hybrid_motif.
IPR018113. PTrfase_EIIB_Cys.
IPR001127. PTS_EIIA_1_perm.
IPR003352. PTS_EIIC.
IPR013013. PTS_EIIC_1.
IPR001996. PTS_IIB_1.
IPR011299. PTS_IIBC_glc.
IPR004719. PTS_maltose/Glc_sub_IIC.
[Graphical view]
PfamiPF00358. PTS_EIIA_1. 1 hit.
PF00367. PTS_EIIB. 1 hit.
PF02378. PTS_EIIC. 1 hit.
[Graphical view]
SUPFAMiSSF51261. SSF51261. 1 hit.
SSF55604. SSF55604. 1 hit.
TIGRFAMsiTIGR00826. EIIB_glc. 1 hit.
TIGR00830. PTBA. 1 hit.
TIGR00852. pts-Glc. 1 hit.
TIGR02002. PTS-II-BC-glcB. 1 hit.
PROSITEiPS51093. 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]

Sequencei

Sequence statusi: Complete.

P20166-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFKALFGVLQ KIGRALMLPV AILPAAGILL AIGNAMQNKD MIQVLHFLSN
60 70 80 90 100
DNVQLVAGVM ESAGQIVFDN LPLLFAVGVA IGLANGDGVA GIAAIIGYLV
110 120 130 140 150
MNVSMSAVLL ANGTIPSDSV ERAKFFTENH PAYVNMLGIP TLATGVFGGI
160 170 180 190 200
IVGVLAALLF NRFYTIELPQ YLGFFAGKRF VPIVTSISAL ILGLIMLVIW
210 220 230 240 250
PPIQHGLNAF STGLVEANPT LAAFIFGVIE RSLIPFGLHH IFYSPFWYEF
260 270 280 290 300
FSYKSAAGEI IRGDQRIFMA QIKDGVQLTA GTFMTGKYPF MMFGLPAAAL
310 320 330 340 350
AIYHEAKPQN KKLVAGIMGS AALTSFLTGI TEPLEFSFLF VAPVLFAIHC
360 370 380 390 400
LFAGLSFMVM QLLNVKIGMT FSGGLIDYFL FGILPNRTAW WLVIPVGLGL
410 420 430 440 450
AVIYYFGFRF AIRKFNLKTP GREDAAEETA APGKTGEAGD LPYEILQAMG
460 470 480 490 500
DQENIKHLDA CITRLRVTVN DQKKVDKDRL KQLGASGVLE VGNNIQAIFG
510 520 530 540 550
PRSDGLKTQM QDIIAGRKPR PEPKTSAQEE VGQQVEEVIA EPLQNEIGEE
560 570 580 590 600
VFVSPITGEI HPITDVPDQV FSGKMMGDGF AILPSEGIVV SPVRGKILNV
610 620 630 640 650
FPTKHAIGLQ SDGGREILIH FGIDTVSLKG EGFTSFVSEG DRVEPGQKLL
660 670 680 690
EVDLDAVKPN VPSLMTPIVF TNLAEGETVS IKASGSVNRE QEDIVKIEK
Length:699
Mass (Da):75,525
Last modified:December 1, 1992 - v2
Checksum:i2A14D3C32EE0A9C5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z11744 Genomic DNA. Translation: CAA77803.1.
AL009126 Genomic DNA. Translation: CAB13262.1.
X12832 Genomic DNA. Translation: CAA31315.1.
M60344 Genomic DNA. Translation: AAA22498.1.
PIRiS25083. WQBSGS.
RefSeqiNP_389272.1. NC_000964.3.
WP_003244661.1. NZ_JNCM01000035.1.

Genome annotation databases

EnsemblBacteriaiCAB13262; CAB13262; BSU13890.
GeneIDi939255.
KEGGibsu:BSU13890.
PATRICi18974561. VBIBacSub10457_1472.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z11744 Genomic DNA. Translation: CAA77803.1.
AL009126 Genomic DNA. Translation: CAB13262.1.
X12832 Genomic DNA. Translation: CAA31315.1.
M60344 Genomic DNA. Translation: AAA22498.1.
PIRiS25083. WQBSGS.
RefSeqiNP_389272.1. NC_000964.3.
WP_003244661.1. NZ_JNCM01000035.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AX3NMR-A539-699[»]
1GPRX-ray1.90A539-699[»]
ProteinModelPortaliP20166.
SMRiP20166. Positions 438-516, 541-698.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100007711.

Protein family/group databases

TCDBi4.A.1.1.9. the pts glucose-glucoside (glc) family.

Proteomic databases

PaxDbiP20166.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB13262; CAB13262; BSU13890.
GeneIDi939255.
KEGGibsu:BSU13890.
PATRICi18974561. VBIBacSub10457_1472.

Organism-specific databases

GenoListiBSU13890. [Micado]

Phylogenomic databases

eggNOGiCOG1263.
HOGENOMiHOG000250993.
InParanoidiP20166.
KOiK02763.
K02764.
K02765.
OMAiSFNGYQT.
OrthoDBiEOG6FFS9V.
PhylomeDBiP20166.

Enzyme and pathway databases

BioCyciBSUB:BSU13890-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP20166.

Family and domain databases

Gene3Di3.30.1360.60. 1 hit.
InterProiIPR011055. Dup_hybrid_motif.
IPR018113. PTrfase_EIIB_Cys.
IPR001127. PTS_EIIA_1_perm.
IPR003352. PTS_EIIC.
IPR013013. PTS_EIIC_1.
IPR001996. PTS_IIB_1.
IPR011299. PTS_IIBC_glc.
IPR004719. PTS_maltose/Glc_sub_IIC.
[Graphical view]
PfamiPF00358. PTS_EIIA_1. 1 hit.
PF00367. PTS_EIIB. 1 hit.
PF02378. PTS_EIIC. 1 hit.
[Graphical view]
SUPFAMiSSF51261. SSF51261. 1 hit.
SSF55604. SSF55604. 1 hit.
TIGRFAMsiTIGR00826. EIIB_glc. 1 hit.
TIGR00830. PTBA. 1 hit.
TIGR00852. pts-Glc. 1 hit.
TIGR02002. PTS-II-BC-glcB. 1 hit.
PROSITEiPS51093. 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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF EIAA DOMAIN.

Entry informationi

Entry nameiPTG3C_BACSU
AccessioniPrimary (citable) accession number: P20166
Secondary accession number(s): P08875
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: December 1, 1992
Last modified: June 24, 2015
This is version 141 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.