PTS system glucose-specific EIICBA component - Staphylococcus carnosus (strain TM300)

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Reviewed, UniProtKB/Swiss-Prot Q57071 (PTG3C_STACT)

Last modified October 13, 2009. Version 60. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    PTS system glucose-specific EIICBA component
Alternative name(s):
    EIICBA-Glc
      Short name=EII-Glc
    EIICBA-Glc 1
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:	glcA
Ordered Locus Names:	Sca_0999

Organism

Staphylococcus carnosus (strain TM300) [Complete proteome] [HAMAP]

Taxonomic identifier

396513 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Staphylococcus

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Protein attributes

Sequence length	675 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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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. Can not transport galactose, fructose, mannose, cellobiose, sucrose, maltose, lactose, melibiose and trehalose, as well as N-acetylglucosamine. Ref.3
Catalytic activity	Protein EIIB N(pi)-phospho-L-histidine/cysteine + sugar = protein EIIB + sugar phosphate. Protein EIIA N(pi)-phospho-L-histidine + protein EIIB = protein EIIA + protein EIIB N(pi)-phospho-L-histidine/cysteine.
Enzyme regulation	Inhibited by 2-deoxyglucose and methyl beta-D-glucoside, but not by methyl alpha-D-glucoside, p-nitrophenyl alpha-D-glucoside, o-nitrophenyl beta-D-glucoside and salicin. Ref.3
Subcellular location	Cell membrane; Multi-pass membrane protein. Ref.3
Induction	Up-regulated by the antiterminator protein glcT. Ref.4
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.
Biophysicochemical properties	Kinetic parameters: K_M=12 µM for glucose K_M=30.5 µM for glucose (in the presence of Triton X-100)

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Ontologies

Keywords
Biological process	Phosphotransferase system Sugar transport Transport
Cellular component	Cell membrane Membrane
Domain	Transmembrane
Molecular function	Kinase Transferase
Technical term	Complete proteome Direct protein sequencing
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...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 675

675

PTS system glucose-specific EIICBA component

PRO_0000351401

Regions

Transmembrane

16 – 36

Potential

Transmembrane

63 – 83

Potential

Transmembrane

89 – 109

Potential

Transmembrane

126 – 146

Potential

Transmembrane

170 – 190

Potential

Transmembrane

199 – 219

Potential

Transmembrane

273 – 293

Potential

Transmembrane

303 – 323

Potential

Transmembrane

329 – 349

Potential

Transmembrane

355 – 375

Potential

Transmembrane

383 – 403

Potential

Domain

3 – 414

412

PTS EIIC type-1

Domain

425 – 506

PTS EIIB type-1

Domain

547 – 651

105

PTS EIIA type-1

Sites

Active site

447

Phosphocysteine intermediate; for EIIB activity By similarity

Active site

599

Tele-phosphohistidine intermediate; for EIIA activity By similarity

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Sequences

Sequence

Length

Mass (Da)

Tools

Q57071-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 523BAF4EF362B7E2
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FASTA

675

73,111

        10         20         30         40         50         60 
MWKKFFGQLQ RIGKALMLPV AILPAAGLLL ALGNAFQGDA LQSLMPFIKA EGFQNVAKMM 

        70         80         90        100        110        120 
EGAGGIIFDN LAIIFALGVA IGLASGDGVA AIAAFVGFIV LNKTMGMFLG VTPEKAADAA 

       130        140        150        160        170        180 
TGFANVLGIP TLQTGVFGGI IIGALAAWCY NKFYNISLPS YLGFFAGKRF VPIMMATCSF 

       190        200        210        220        230        240 
ILAFPMAIIW PSIQGGLNAF SEGLLASNTG LAVFLFGFIK RLLIPFGLHH IFHAPFWFEF 

       250        260        270        280        290        300 
GSYKNAAGQI IHGDQRIFIE QIRDNVPLTA GKFMQGEFPV MMFGLPAAAL AIYQTAKKEN 

       310        320        330        340        350        360 
KKVVAGLMLS GALTSFLTGI TEPLEFSFLF VAPLLFFIHA VLDGLSFLIL YLLDLHLGYT 

       370        380        390        400        410        420 
FSGGFIDFFL LGILPNKTQW WLVIPVGLVY AAIYYIIFRF LIVKFNFKTP GREDKEVKSS 

       430        440        450        460        470        480 
NVAASELPFK VLDAMGGKAN IKHLDACITR LRVEVNDKAK VDVQELKDLG ASGVLEVGNN 

       490        500        510        520        530        540 
MQAIFGPKSD QIKHDMQQIM DGKITSPEET TVTEEGDKET AEIAAAGGGV VYAPIKGEVV 

       550        560        570        580        590        600 
DISEVPDKVF SEKMMGDGIA IKPETGEVVA PFDGVVKMVF PTKHAIGLES KDGIELLIHF 

       610        620        630        640        650        660 
GLETVKLEGK GFDILVKEND NIVLGQPLMK VDLDYIKEHA DSTITPIVVT NLNGRTMEVL 

       670 
QHGEVKQGDK VILVK

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and sequencing of two genes from Staphylococcus carnosus coding for glucose-specific PTS and their expression in Escherichia coli K-12." Christiansen I., Hengstenberg W. Mol. Gen. Genet. 250:375-379(1996) [PubMed: 8602153] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Genome analysis of the meat starter culture bacterium Staphylococcus carnosus TM300." Rosenstein R., Nerz C., Biswas L., Resch A., Raddatz G., Schuster S.C., Goetz F. Appl. Environ. Microbiol. 75:811-822(2009) [PubMed: 19060169] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"Staphylococcal phosphoenolpyruvate-dependent phosphotransferase system -- two highly similar glucose permeases in Staphylococcus carnosus with different glucoside specificity: protein engineering in vivo?" Christiansen I., Hengstenberg W. Microbiology 145:2881-2889(1999) [PubMed: 10537210] [Abstract] Cited for: PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION, SUBSTRATE SPECIFICITY, ENZYME REGULATION, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES.
[4]	"Regulation of the glucose-specific phosphotransferase system (PTS) of Staphylococcus carnosus by the antiterminator protein GlcT." Knezevic I., Bachem S., Sickmann A., Meyer H.E., Stuelke J., Hengstenberg W. Microbiology 146:2333-2342(2000) [PubMed: 10974121] [Abstract] Cited for: INDUCTION BY GLCT.

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Cross-references

Sequence databases
	X93360 Genomic DNA. Translation: CAA63742.1. AM295250 Genomic DNA. Translation: CAL27907.1.
PIR	S46952.
RefSeq	YP_002634092.1.
3D structure databases
HSSP	HSSP built from PDB template 1O2F based on UniProtKB P05053.
ModBase	Search...
Genome annotation databases
GeneID	7551632.
GenomeReviews	Gene locus Sca_0999 in contig AM295250_GR.
KEGG	sca:Sca_0999.
Organism-specific databases
CMR	Search...
Family and domain databases
InterPro	IPR018113. PTrfase_EIIB/Cys_phosph_CS. 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. 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...

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Entry information

Entry name

PTG3C_STACT

Accession

Primary (citable) accession number: Q57071
Secondary accession number(s): B9DP62

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 14, 2008
Last sequence update:	November 1, 1996
Last modified:	October 13, 2009
This is version 60 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)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Genome annotation databases

Organism-specific databases

Family and domain databases

Entry information

Relevant documents