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Protein

PTS system mannose-specific EIIBCA component

Gene

manP

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: -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)DescriptionActionsGraphical viewLength
Active sitei9Phosphocysteine intermediate; for EIIB activityBy similarity1
Active sitei566Tele-phosphohistidine intermediate; for EIIA activityPROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionKinase, Transferase
Biological processPhosphotransferase 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)DescriptionActionsGraphical viewLength
Transmembranei133 – 153HelicalPROSITE-ProRule annotationAdd BLAST21
Transmembranei174 – 194HelicalPROSITE-ProRule annotationAdd BLAST21
Transmembranei199 – 219HelicalPROSITE-ProRule annotationAdd BLAST21
Transmembranei221 – 241HelicalPROSITE-ProRule annotationAdd BLAST21
Transmembranei256 – 276HelicalPROSITE-ProRule annotationAdd BLAST21
Transmembranei297 – 317HelicalPROSITE-ProRule annotationAdd BLAST21
Transmembranei336 – 356HelicalPROSITE-ProRule annotationAdd BLAST21
Transmembranei369 – 389HelicalPROSITE-ProRule annotationAdd BLAST21
Transmembranei396 – 416HelicalPROSITE-ProRule annotationAdd BLAST21
Transmembranei436 – 456HelicalPROSITE-ProRule annotationAdd BLAST21

GO - Cellular componenti

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)DescriptionActionsGraphical viewLength
Mutagenesisi9C → 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 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003713131 – 650PTS system mannose-specific EIIBCA componentAdd BLAST650

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei365Phosphoserine1 Publication1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiO31645
PRIDEiO31645

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

1650
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 8Combined sources7
Helixi14 – 30Combined sources17
Beta strandi33 – 40Combined sources8
Beta strandi43 – 46Combined sources4
Helixi50 – 55Combined sources6
Beta strandi57 – 65Combined sources9
Helixi70 – 72Combined sources3
Beta strandi75 – 80Combined sources6
Helixi82 – 87Combined sources6
Helixi89 – 98Combined sources10

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiO31645

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 98PTS EIIB type-2PROSITE-ProRule annotationAdd BLAST98
Domaini123 – 456PTS EIIC type-2PROSITE-ProRule annotationAdd BLAST334
Domaini504 – 649PTS EIIA type-2PROSITE-ProRule annotationAdd BLAST146

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

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
InterProiView protein in InterPro
IPR016152 PTrfase/Anion_transptr
IPR002178 PTS_EIIA_type-2_dom
IPR036095 PTS_EIIB-like_sf
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
PfamiView protein in Pfam
PF00359 PTS_EIIA_2, 1 hit
PF02378 PTS_EIIC, 1 hit
PF02302 PTS_IIB, 1 hit
SUPFAMiSSF52794 SSF52794, 1 hit
SSF55804 SSF55804, 1 hit
TIGRFAMsiTIGR00829 FRU, 1 hit
TIGR00848 fruA, 1 hit
TIGR01427 PTS_IIC_fructo, 1 hit
PROSITEiView protein in 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

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
PATRICifig|224308.179.peg.1296

Entry informationi

Entry nameiPTN3B_BACSU
AccessioniPrimary (citable) accession number: O31645
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: May 5, 2009
Last modified: May 23, 2018
This is version 120 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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