Reviewed, UniProtKB/Swiss-Prot P71012 (PTF3A_BACSU)

Names and origin

Protein names

Recommended name:
    PTS system fructose-specific EIIABC component
Alternative name(s):
    EIIABC-Fru
Including the following 3 domains:
    1- Recommended name:
            Fructose-specific phosphotransferase enzyme IIA component
              EC=2.7.1.-
        Alternative name(s):
            PTS system fructose-specific EIIA component
            EII-Fru
    2- Recommended name:
            Fructose-specific phosphotransferase enzyme IIB component
              EC=2.7.1.69
        Alternative name(s):
            PTS system fructose-specific EIIB component
            EIII-Fru
    3- Recommended name:
            Fructose permease IIC component
        Alternative name(s):
            PTS system fructose-specific EIIC component

Gene names

Name:	fruA
Ordered Locus Names:	BSU14400

Organism

Bacillus subtilis [Complete proteome] [HAMAP]

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	635 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 fructose transport By similarity.
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 Potential.
Domain	The EIIA domain is phosphorylated by phospho-HPr on a histidyl residue. Then, it transfers the phosphoryl group to the EIIB 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 1 PTS EIIA type-2 domain. Contains 1 PTS EIIB type-2 domain. Contains 1 PTS EIIC type-2 domain.

Ontologies

Keywords
Biological process	Phosphotransferase system Sugar transport Transport
Cellular component	Cell membrane Membrane
Domain	Transmembrane
Molecular function	Transferase
PTM	Phosphoprotein
Technical term	3D-structure 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-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	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 – 635

635

PTS system fructose-specific EIIABC component

PRO_0000360665

Regions

Transmembrane

312 – 332

21

Potential

Transmembrane

350 – 370

21

Potential

Transmembrane

392 – 412

21

Potential

Transmembrane

428 – 448

21

Potential

Transmembrane

470 – 490

21

Potential

Transmembrane

511 – 531

21

Potential

Transmembrane

544 – 564

21

Potential

Transmembrane

569 – 589

21

Potential

Transmembrane

608 – 628

21

Potential

Domain

5 – 149

145

PTS EIIA type-2

Domain

172 – 267

96

PTS EIIB type-2

Domain

301 – 635

335

PTS EIIC type-2

Sites

Active site

67

1

Tele-phosphohistidine intermediate; for EIIA activity By similarity

Active site

178

1

Phosphocysteine intermediate; for EIIB activity By similarity

Secondary structure

1

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635

Helix Strand Turn

Details...

Beta strand

172 – 177

6

Helix

185 – 198

14

Beta strand

203 – 208

6

Helix

219 – 224

6

Beta strand

228 – 234

7

Helix

239 – 241

3

Beta strand

245 – 249

5

Helix

258 – 266

9

Sequences

	Sequence		Length	Mass (Da)
	P71012-1 [UniParc]. Last modified June 1, 1998. Version 2. Checksum: 753F12C2AFDD7F84	FASTA	635	67,184
	10 20 30 40 50 60 MKITELLTKH TIKLNIESKE KENVIDEMVT VLDKAGKLND RQAYKEAILN RESQSSTGIG 70 80 90 100 110 120 EGIAIPHAKT ASVINPAIAF GRSKDGVDYE SLDGQPAHLV FMIAATEGAN NTHLEALSRL 130 140 150 160 170 180 STLLMREEIR KQLLEAESED AIIDIINQHD KDDDEEEEEE EAAPAPAGKG KILAVTACPT 190 200 210 220 230 240 GIAHTFMAAD ALKEKAKELG VEIKVETNGS SGIKHKLTAQ EIEDAPAIIV AADKQVEMER 250 260 270 280 290 300 FKGKRVLQVP VTAGIRRPQE LIEKAMNQDA PIYQGSGGGS AASNDDEEAK GKSGSGIGNT 310 320 330 340 350 360 FYKHLMSGVS NMLPFVVGGG ILVAISFFWG IHSADPNDPS YNTFAAALNF IGGDNALKLI 370 380 390 400 410 420 VAVLAGFIAM SIADRPGFAP GMVGGFMATQ ANAGFLGGLI AGFLAGYVVI LLKKVFTFIP 430 440 450 460 470 480 QSLDGLKPVL IYPLFGIFIT GVLMQFVVNT PVAAFMNFLT NWLESLGTGN LVLMGIILGG 490 500 510 520 530 540 MMAIDMGGPL NKAAFTFGIA MIDAGNYAPH AAIMAGGMVP PLGIALATTI FRNKFTQRDR 550 560 570 580 590 600 EAGITCYFMG AAFVTEGAIP FAAADPLRVI PAAVVGAAVA GGLTEFFRVT LPAPHGGVFV 610 620 630 AFITNHPMLY LLSIVIGAVV MAIILGIVKK PVTEK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence analysis of the mobA-ampS region of the Bacillus subtilis chromosome." Caldwell R.M., Ferrari E. Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168.
[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]	"The structure of a domain of fruA from Bacillus subtilis." Midwest center for structural genomics (MCSG) Submitted (SEP-2007) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 171-273.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AF012285 Genomic DNA. Translation: AAC24915.1.
AL009126 Genomic DNA. Translation: CAB13313.1.

PIR

H69626.

RefSeq

NP_389323.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2R4Q	X-ray	1.60	A	171-273	[»]

ModBase

Search...

Protein family/group databases

TCDB

4.A.2.1.4. PTS fructose-mannitol (Fru) family.

Genome annotation databases

GeneID

938757.

GenomeReviews

Gene locus BSU14400 in contig AL009126_GR.

KEGG

bsu:BSU14400.

NMPDR

fig|224308.1.peg.1442.

Organism-specific databases

SubtiList

BG11938. fruA. [Micado]

CMR

Search...

Phylogenomic databases

HOGENOM

P71012.

OMA

GANATHL.

Enzyme and pathway databases

BioCyc

BSUB224308:BSU1442-MON.

Family and domain databases

InterPro

IPR002178. PTS_EIIA_2.
IPR013011. PTS_EIIB_2.
IPR003352. PTS_EIIC.
IPR013014. PTS_EIIC_2.
IPR004715. PTS_IIA_fruc.
IPR003353. PTS_IIB_fruc.
IPR006327. PTS_IIC_fruc.
[Graphical view]

Gene3D

G3DSA:3.40.930.10. PTS_EIIA_2. 1 hit.

Pfam

PF00359. PTS_EIIA_2. 1 hit.
PF02378. PTS_EIIC. 1 hit.
PF02379. PTS_IIB_fruc. 1 hit.
[Graphical view]

ProDom

PD001689. PTS_EIIA_2. 1 hit.
[Graphical view] [Entries sharing at least one domain]

TIGRFAMs

TIGR00829. FRU. 1 hit.
TIGR00848. fruA. 1 hit.
TIGR01427. PTS_IIC_fructo. 1 hit.

PROSITE

PS51094. PTS_EIIA_TYPE_2. 1 hit.
PS00372. PTS_EIIA_TYPE_2_HIS. 1 hit.
PS51099. PTS_EIIB_TYPE_2. 1 hit.
PS51104. PTS_EIIC_TYPE_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

PTF3A_BACSU

Accession

Primary (citable) accession number: P71012
Secondary accession number(s): Q7BVR6

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 20, 2009
Last sequence update:	June 1, 1998
Last modified:	November 3, 2009
This is version 64 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)