PTS system glucoside-specific EIICBA component - Staphylococcus aureus (strain N315)

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Q7A3G4 (PTU3C_STAAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 71. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
PTS system glucoside-specific EIICBA component

Including the following 3 domains:

Glucoside permease IIC component
Alternative name(s):
PTS system glucoside-specific EIIC component
Glucoside-specific phosphotransferase enzyme IIB component
EC=2.7.1.69
Alternative name(s):
PTS system glucoside-specific EIIB component
Glucoside-specific phosphotransferase enzyme IIA component
EC=2.7.1.-
Alternative name(s):
PTS system glucoside-specific EIIA component

Gene names

Name:	glcB
Ordered Locus Names:	SA2326

Organism

Staphylococcus aureus (strain N315) [Complete proteome] [HAMAP]

Taxonomic identifier

158879 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacilli › Bacillales › Staphylococcus ›

Protein attributes

Sequence length	688 AA.
Sequence status	Complete.
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 alpha- and beta-glucoside transport By similarity.
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.
Subcellular location	Cell membrane; Multi-pass membrane protein By similarity.
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 Transmembrane helix
Molecular function	Kinase Transferase
Technical term	Complete proteome
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-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
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 – 688

688

PTS system glucoside-specific EIICBA component

PRO_0000351414

Regions

Transmembrane

12 – 32

Helical; Potential

Transmembrane

81 – 101

Helical; Potential

Transmembrane

137 – 157

Helical; Potential

Transmembrane

182 – 202

Helical; Potential

Transmembrane

223 – 243

Helical; Potential

Transmembrane

284 – 304

Helical; Potential

Transmembrane

315 – 335

Helical; Potential

Transmembrane

340 – 360

Helical; Potential

Transmembrane

364 – 384

Helical; Potential

Transmembrane

395 – 415

Helical; Potential

Domain

3 – 427

425

PTS EIIC type-1

Domain

438 – 519

PTS EIIB type-1

Domain

560 – 664

105

PTS EIIA type-1

Sites

Active site

460

Phosphocysteine intermediate; for EIIB activity By similarity

Active site

612

Tele-phosphohistidine intermediate; for EIIA activity By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q7A3G4 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 11D5C824835AFD21
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FASTA

688

74,430

        10         20         30         40         50         60 
MFKKLFGQLQ RIGKALMLPV AILPAAGILL AFGNAMHNEQ LVEIAPWLKN DIIVMISSVM 

        70         80         90        100        110        120 
EAAGQVVFDN LPLLFAVGTA LGLAGGDGVA ALAALVGYLI MNATMGKVLH ITIDDIFSYA 

       130        140        150        160        170        180 
KGAKELSQAA KEPAHALVLG IPTLQTGVFG GIIMGALAAW CYNKFYNITL PPFLGFFAGK 

       190        200        210        220        230        240 
RFVPIVTSVV AIATGVLLSF AWPPIQDGLN SLSNFLLNKN LTLTTFIFGI IERSLIPFGL 

       250        260        270        280        290        300 
HHIFYSPFWF EFGSYTNHAG ELVRGDQRIW MAQLKDGVPF TAGAFTTGKY PFMMFGLPAA 

       310        320        330        340        350        360 
AFAIYKNARP ERKKVVGGLM LSAGLTAFLT GITEPLEFSF LFVAPVLYGI HVLLAGTSFL 

       370        380        390        400        410        420 
VMHLLGVKIG MTFSGGFIDY ILYGLLNWDR SHALLVIPVG IVYAIVYYFL FDFAIRKFKL 

       430        440        450        460        470        480 
KTPGREDEET EIRNSSVAKL PFDVLDAMGG KENIKHLDAC ITRLRVEVVD KSKVDVAGIK 

       490        500        510        520        530        540 
ALGASGVLEV GNNMQAIFGP KSDQIKHDMA KIMSGEITKP SETTVTEEMS DEPVHVEALG 

       550        560        570        580        590        600 
TTDIYAPGVG QIIPLSEVPD QVFAGKMMGD GIGFIPEKGE IVAPFDGTVK TIFPTKHAIG 

       610        620        630        640        650        660 
LESESGVEVL IHIGIDTVKL NGEGFESLIN VDEKVTQAQP LMKVNLAYLK AHAPSIVTPM 

       670        680 
IITNLENKEL VIEDVQDADP GKLIMTVK

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References

[1]

"Whole genome sequencing of meticillin-resistant Staphylococcus aureus."
Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L., Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M., Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.

Hiramatsu K.
Lancet 357:1225-1240(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: N315.

[2]

"Shotgun proteomic analysis of total and membrane protein extracts of S. aureus strain N315."
Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F.
Submitted (OCT-2007) to UniProtKB
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: N315.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000018 Genomic DNA. Translation: BAB43629.1.
PIR	C90058.
RefSeq	NP_375650.1. NC_002745.2.
3D structure databases
HSSP	HSSP built from PDB template 1IBA based on UniProtKB P69786.
ProteinModelPortal	Q7A3G4.
SMR	Q7A3G4. Positions 447-509, 532-671.
ModBase	Search...
Protein-protein interaction databases
STRING	158879.SA2326.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	BAB43629; BAB43629; BAB43629.
GeneID	1125253.
KEGG	sau:SA2326.
PATRIC	19577210. VBIStaAur116463_2523.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1263.
HOGENOM	HOG000250993.
KO	K02763. K02764. K02765.
OMA	FSDWAAH.
ProtClustDB	CLSK872840.
Enzyme and pathway databases
BioCyc	SAUR158879:GJCB-2487-MONOMER.
Family and domain databases
Gene3D	3.30.1360.60. 1 hit.
InterPro	IPR011055. Dup_hybrid_motif. IPR018113. PTrfase_EIIB/Cys_phosph_CS. IPR001127. PTS_EIIA_1_perm. IPR001996. PTS_EIIB_1. IPR003352. PTS_EIIC. IPR013013. PTS_EIIC_1. IPR011535. PTS_Glc-like_IIB_component. IPR011299. PTS_IIBC_glc. [Graphical view]
Pfam	PF00358. PTS_EIIA_1. 1 hit. PF00367. PTS_EIIB. 1 hit. PF02378. PTS_EIIC. 1 hit. [Graphical view]
SUPFAM	SSF51261. Dup_hybrid_motif. 1 hit. SSF55604. PTS_EIIB. 1 hit.
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...

Entry information

Entry name

PTU3C_STAAN

Accession

Primary (citable) accession number: Q7A3G4

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 14, 2008
Last sequence update:	July 5, 2004
Last modified:	May 1, 2013
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Including the following 3 domains:

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents