Reviewed, UniProtKB/Swiss-Prot P23387 (PTF3E_RHOCA)

Names and origin

Protein names

Recommended name:
    PTS system fructose-specific EIIBBC component
Alternative name(s):
    EIIBBC-Fru
Including the following 2 domains:
    1- Recommended name:
            Fructose-specific phosphotransferase enzyme IIB component
              EC=2.7.1.69
        Alternative name(s):
            PTS system fructose-specific EIIB component
            EIII-Fru
    2- Recommended name:
            Fructose permease IIC component
        Alternative name(s):
            PTS system fructose-specific EIIC component

Gene names

Name:

fruA

Organism

Rhodobacter capsulatus (Rhodopseudomonas capsulata)

Taxonomic identifier

1061 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Rhodobacter

Protein attributes

Sequence length	578 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Predicted.

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 fructose transport.
Catalytic activity	Protein EIIB N(pi)-phospho-L-histidine/cysteine + sugar = protein EIIB + sugar phosphate.
Subcellular location	Cell membrane; Multi-pass membrane protein.
Domain	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 EIIC domain forms the PTS system translocation channel and contains the specific substrate-binding site.
Sequence similarities	Contains 2 PTS EIIB type-2 domains. Contains 1 PTS EIIC type-2 domain.
Caution	Only one of the two EIIB domains may be active since the first domain lacks the active site and is probably unable to bind and transfer a phosphate group.

Ontologies

Keywords
Biological process	Phosphotransferase system Sugar transport Transport
Cellular component	Cell membrane Membrane
Domain	Repeat 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 – 578	578	PTS system fructose-specific EIIBBC component		PRO_0000186513
Regions
	Transmembrane	251 – 271	21	Potential
	Transmembrane	284 – 304	21	Potential
	Transmembrane	319 – 339	21	Potential
	Transmembrane	364 – 384	21	Potential
	Transmembrane	405 – 425	21	Potential
	Transmembrane	428 – 450	23	Potential
	Transmembrane	477 – 497	21	Potential
	Transmembrane	518 – 538	21	Potential
	Transmembrane	545 – 565	21	Potential
	Domain	1 – 99	99	PTS EIIB type-2 1
	Domain	119 – 214	96	PTS EIIB type-2 2
	Domain	241 – 576	336	PTS EIIC type-2
Sites
	Active site	125	1	Phosphocysteine intermediate; for EIIB activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	P23387-1 [UniParc]. Last modified November 1, 1991. Version 1. Checksum: 87793E5AAA608E4E	FASTA	578	58,576
	10 20 30 40 50 60 MSKIVAVTAG AKGVAHTHLA AEALSATAQA LGHQIRVERH SAEGVEAPLQ GAEIAAADVV 70 80 90 100 110 120 LIAADLRIED VRFVTKPVYR TSTARAVTQT AAVLAEALAL TGEETPQMTT DTGQRPLRVV 130 140 150 160 170 180 AITSCPTGIA HTFMAADALK KTAAARGWEI AVETQGSVGS QNALSAAQIQ AADLVVIAAD 190 200 210 220 230 240 THVDDSRFAG KKVYKTSVGA AVKGAAKVLD AALAEGVVLG TNLADTVDAL KAQRAATRSG 250 260 270 280 290 300 PYMHLLTGVS YMLPLVVAGG LLIALSFVFG IKAFEVEGTL PAALMAIGGG AAFKLMVPVL 310 320 330 340 350 360 AGFIAYSIAD RPGLTPGLIG GMLAVNLNAG FLGGIVAGFL AGYVARWLRD AIKLPRTLEG 370 380 390 400 410 420 LKPVLILPLL STAITGLIMV YVVGTPVAAI LAAMTAFLQG LGTTNAVVLG LILGGMMAVD 430 440 450 460 470 480 MGGPINKAAY TFAVGLLTSS TYAPMAAVMA AGMTPPLGLA LATLVAKNRF TAEEREAGGA 490 500 510 520 530 540 AAVLGLSFIT EGAIPFAAKD PARVIPSIIV GSAITGALSM ALGCLLVAPH GGIFVLAIPH 550 560 570 AVTNLGLYAL SIVVGTLVTT GLLIALKKPI PAEERARS

References

[1]

"Nucleotide sequence of the fruA gene, encoding the fructose permease of the Rhodobacter capsulatus phosphotransferase system, and analyses of the deduced protein sequence." Wu L.-F., Saier M.H. Jr. J. Bacteriol. 172:7167-7178(1990) [PubMed: 2254279] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: DSM 938 / 37b4.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X53150 Genomic DNA. Translation: CAA37303.1.
PIR	B37852.
3D structure databases
ModBase	Search...
Enzyme and pathway databases
BRENDA	2.7.1.69. 567.
Family and domain databases
InterPro	IPR013011. PTS_EIIB_2. IPR003352. PTS_EIIC. IPR013014. PTS_EIIC_2. IPR003353. PTS_IIB_fruc. IPR006327. PTS_IIC_fruc. [Graphical view]
Pfam	PF02378. PTS_EIIC. 1 hit. PF02379. PTS_IIB_fruc. 2 hits. [Graphical view]
TIGRFAMs	TIGR00829. FRU. 1 hit. TIGR01427. PTS_IIC_fructo. 1 hit.
PROSITE	PS51099. PTS_EIIB_TYPE_2. 2 hits. PS51104. PTS_EIIC_TYPE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PTF3E_RHOCA

Accession

Primary (citable) accession number: P23387

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1991
Last sequence update:	November 1, 1991
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)