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Protein

PTS system mannose-specific EIIBCA component

Gene

manP

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 5 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 mannose transport.

Catalytic activityi

[Protein]-N(pi)-phospho-L-histidine + D-mannose(Side 1) = [protein]-L-histidine + D-mannose 6-phosphate(Side 2).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei9 – 91Phosphocysteine intermediate; for EIIB activityBy similarity
Active sitei566 – 5661Tele-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:BSU12010-MONOMER.

Protein family/group databases

TCDBi4.A.2.1.6. the pts fructose-mannitol (fru) family.

Names & Taxonomyi

Protein namesi
Recommended name:
PTS system mannose-specific EIIBCA component
Alternative name(s):
EIIBCA-Man
Short name:
EII-Man
Including the following 3 domains:
Mannose-specific phosphotransferase enzyme IIB component (EC:2.7.1.191)
Alternative name(s):
PTS system mannose-specific EIIB component
Mannose permease IIC component
Alternative name(s):
PTS system mannose-specific EIIC component
Mannose-specific phosphotransferase enzyme IIA component
Alternative name(s):
PTS system mannose-specific EIIA component
Gene namesi
Name:manP
Synonyms:yjdD
Ordered Locus Names:BSU12010
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

  • Cell membrane PROSITE-ProRule annotation; Multi-pass membrane protein PROSITE-ProRule annotation

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei133 – 15321HelicalPROSITE-ProRule annotationAdd
BLAST
Transmembranei174 – 19421HelicalPROSITE-ProRule annotationAdd
BLAST
Transmembranei199 – 21921HelicalPROSITE-ProRule annotationAdd
BLAST
Transmembranei221 – 24121HelicalPROSITE-ProRule annotationAdd
BLAST
Transmembranei256 – 27621HelicalPROSITE-ProRule annotationAdd
BLAST
Transmembranei297 – 31721HelicalPROSITE-ProRule annotationAdd
BLAST
Transmembranei336 – 35621HelicalPROSITE-ProRule annotationAdd
BLAST
Transmembranei369 – 38921HelicalPROSITE-ProRule annotationAdd
BLAST
Transmembranei396 – 41621HelicalPROSITE-ProRule annotationAdd
BLAST
Transmembranei436 – 45621HelicalPROSITE-ProRule annotationAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

Cells lacking this gene are unable to grow with mannose as the sole carbon source. Deletion of manP results in constitutive expression from both the manP and manR promoters, indicating that the phosphotransferase system (PTS) component EII-Man has a negative effect on regulation of the mannose operon and manR.2 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi9 – 91C → A: Appears to be unable to inactivate ManR, since ManR does not show any decrease in its DNA-binding activity in the presence of this mutant. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 650650PTS system mannose-specific EIIBCA componentPRO_0000371313Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei365 – 3651Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiO31645.

PTM databases

iPTMnetiO31645.

Expressioni

Inductioni

Up-regulated by mannose. Is under the control of ManR. Is subject to carbon catabolite repression (CCR) by glucose. Forms part of an operon with manA and yjdF.1 Publication

Interactioni

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100006641.

Structurei

Secondary structure

1
650
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 87Combined sources
Helixi14 – 3017Combined sources
Beta strandi33 – 408Combined sources
Beta strandi43 – 464Combined sources
Helixi50 – 556Combined sources
Beta strandi57 – 659Combined sources
Helixi70 – 723Combined sources
Beta strandi75 – 806Combined sources
Helixi82 – 876Combined sources
Helixi89 – 9810Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2R48X-ray1.80A2-104[»]
ProteinModelPortaliO31645.
SMRiO31645. Positions 2-104, 502-647.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO31645.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 9898PTS EIIB type-2PROSITE-ProRule annotationAdd
BLAST
Domaini123 – 456334PTS EIIC type-2PROSITE-ProRule annotationAdd
BLAST
Domaini504 – 649146PTS EIIA type-2PROSITE-ProRule annotationAdd
BLAST

Domaini

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 EIIB domain is also able to transfer its phosphoryl group to a specific histidine residue in ManR, which leads to its inactivation.PROSITE-ProRule annotation1 Publication
The EIIC domain forms the PTS system translocation channel and contains the specific substrate-binding site.PROSITE-ProRule annotation1 Publication
The EIIA domain is phosphorylated by phospho-HPr on a histidyl residue. Then, it transfers the phosphoryl group to the EIIB domain.PROSITE-ProRule annotation1 Publication

Sequence similaritiesi

Contains 1 PTS EIIA type-2 domain.PROSITE-ProRule annotation
Contains 1 PTS EIIB type-2 domain.PROSITE-ProRule annotation
Contains 1 PTS EIIC type-2 domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105DM4. Bacteria.
COG1299. LUCA.
COG1445. LUCA.
COG1762. LUCA.
HOGENOMiHOG000227677.
InParanoidiO31645.
KOiK02768.
K02769.
K02770.
OMAiQPIMPII.
PhylomeDBiO31645.

Family and domain databases

CDDicd05569. PTS_IIB_fructose. 1 hit.
Gene3Di3.40.930.10. 1 hit.
InterProiIPR016152. PTrfase/Anion_transptr.
IPR002178. PTS_EIIA_type-2_dom.
IPR013011. PTS_EIIB_2.
IPR003501. PTS_EIIB_2/3.
IPR003352. PTS_EIIC.
IPR013014. PTS_EIIC_2.
IPR004715. PTS_IIA_fruc.
IPR003353. PTS_IIB_fruc.
IPR006327. PTS_IIC_fruc.
[Graphical view]
PfamiPF00359. PTS_EIIA_2. 1 hit.
PF02378. PTS_EIIC. 1 hit.
PF02302. PTS_IIB. 1 hit.
[Graphical view]
SUPFAMiSSF52794. SSF52794. 1 hit.
SSF55804. SSF55804. 1 hit.
TIGRFAMsiTIGR00829. FRU. 1 hit.
TIGR00848. fruA. 1 hit.
TIGR01427. PTS_IIC_fructo. 1 hit.
PROSITEiPS51094. 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]

Sequencei

Sequence statusi: Complete.

O31645-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLLAITSCP NGIAHTYMAA ENLQKAADRL GVSIKVETQG GIGVENKLTE
60 70 80 90 100
EEIREADAII IAADRSVNKD RFIGKKLLSV GVQDGIRKPE ELIQKALNGD
110 120 130 140 150
IPVYRSATKS ESGNHQEKKQ NPIYRHLMNG VSFMVPFIVV GGLLIAVALT
160 170 180 190 200
LGGEKTPKGL VIPDDSFWKT IEQIGSASFS FMIPILAGYI AYSIADKPGL
210 220 230 240 250
VPGMIGGYIA ATGSFYDSAS GAGFLGGIIA GFLAGYAALW IKKLKVPKAI
260 270 280 290 300
QPIMPIIIIP VFASLIVGLA FVFLIGAPVA QIFASLTVWL AGMKGSSSIL
310 320 330 340 350
LALILGAMIS FDMGGPVNKV AFLFGSAMIG EGNYEIMGPI AVAICIPPIG
360 370 380 390 400
LGIATFLGKR KFEASQREMG KAAFTMGLFG ITEGAIPFAA QDPLRVIPSI
410 420 430 440 450
MAGSMTGSVI AMIGNVGDRV AHGGPIVAVL GAVDHVLMFF IAVIAGSLVT
460 470 480 490 500
ALFVNVLKKD ITASPVLSET APTSAPSEAA AANEIKQPIQ SQKAEMSEFK
510 520 530 540 550
KLTDIISPEL IEPNLSGETS DDIIDELIQK LSRRGALLSE SGFKQAILNR
560 570 580 590 600
EQQGTTAIGM NIAIPHGKSE AVREPSVAFG IKRSGVDWNS LDGSEAKLIF
610 620 630 640 650
MIAVPKESGG NQHLKILQML SRKLMDDNYR ERLLSVQTTE EAYKLLEEIE
Length:650
Mass (Da):69,026
Last modified:May 5, 2009 - v2
Checksum:iBF92BA1E5E7EBE5F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL009126 Genomic DNA. Translation: CAB13058.2.
PIRiG69848.
RefSeqiNP_389083.2. NC_000964.3.
WP_003245781.1. NZ_JNCM01000035.1.

Genome annotation databases

EnsemblBacteriaiCAB13058; CAB13058; BSU12010.
GeneIDi936437.
KEGGibsu:BSU12010.
PATRICi18974131. VBIBacSub10457_1258.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL009126 Genomic DNA. Translation: CAB13058.2.
PIRiG69848.
RefSeqiNP_389083.2. NC_000964.3.
WP_003245781.1. NZ_JNCM01000035.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2R48X-ray1.80A2-104[»]
ProteinModelPortaliO31645.
SMRiO31645. Positions 2-104, 502-647.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100006641.

Protein family/group databases

TCDBi4.A.2.1.6. the pts fructose-mannitol (fru) family.

PTM databases

iPTMnetiO31645.

Proteomic databases

PaxDbiO31645.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB13058; CAB13058; BSU12010.
GeneIDi936437.
KEGGibsu:BSU12010.
PATRICi18974131. VBIBacSub10457_1258.

Phylogenomic databases

eggNOGiENOG4105DM4. Bacteria.
COG1299. LUCA.
COG1445. LUCA.
COG1762. LUCA.
HOGENOMiHOG000227677.
InParanoidiO31645.
KOiK02768.
K02769.
K02770.
OMAiQPIMPII.
PhylomeDBiO31645.

Enzyme and pathway databases

BioCyciBSUB:BSU12010-MONOMER.

Miscellaneous databases

EvolutionaryTraceiO31645.

Family and domain databases

CDDicd05569. PTS_IIB_fructose. 1 hit.
Gene3Di3.40.930.10. 1 hit.
InterProiIPR016152. PTrfase/Anion_transptr.
IPR002178. PTS_EIIA_type-2_dom.
IPR013011. PTS_EIIB_2.
IPR003501. PTS_EIIB_2/3.
IPR003352. PTS_EIIC.
IPR013014. PTS_EIIC_2.
IPR004715. PTS_IIA_fruc.
IPR003353. PTS_IIB_fruc.
IPR006327. PTS_IIC_fruc.
[Graphical view]
PfamiPF00359. PTS_EIIA_2. 1 hit.
PF02378. PTS_EIIC. 1 hit.
PF02302. PTS_IIB. 1 hit.
[Graphical view]
SUPFAMiSSF52794. SSF52794. 1 hit.
SSF55804. SSF55804. 1 hit.
TIGRFAMsiTIGR00829. FRU. 1 hit.
TIGR00848. fruA. 1 hit.
TIGR01427. PTS_IIC_fructo. 1 hit.
PROSITEiPS51094. 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]
ProtoNetiSearch...

Entry informationi

Entry nameiPTN3B_BACSU
AccessioniPrimary (citable) accession number: O31645
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: May 5, 2009
Last modified: September 7, 2016
This is version 112 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

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 one 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.