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Protein

PTS system N-acetylmuramic acid-specific EIIBC component

Gene

murP

Organism
Escherichia coli (strain K12)
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 N-acetylmuramic acid (MurNAc) transport, yielding cytoplasmic MurNAc-6-P. Is responsible for growth on MurNAc as the sole source of carbon and energy. Is also able to take up anhydro-N-acetylmuramic acid (anhMurNAc), but cannot phosphorylate the carbon 6, probably because of the 1,6-anhydro ring.2 Publications

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei29 – 291Phosphocysteine intermediate; for EIIB activityPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

  • carbohydrate transmembrane transport Source: EcoCyc
  • phosphoenolpyruvate-dependent sugar phosphotransferase system Source: EcoCyc
  • regulation of carbohydrate utilization Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Phosphotransferase system, Sugar transport, Transport

Enzyme and pathway databases

BioCyciEcoCyc:MONOMER0-5.
ECOL316407:JW2422-MONOMER.
MetaCyc:MONOMER0-5.

Protein family/group databases

TCDBi4.A.1.2.7. the pts glucose-glucoside (glc) family.

Names & Taxonomyi

Protein namesi
Recommended name:
PTS system N-acetylmuramic acid-specific EIIBC component
Alternative name(s):
EIIBC-MurNAc
Including the following 2 domains:
N-acetylmuramic acid-specific phosphotransferase enzyme IIB component (EC:2.7.1.1921 Publication)
Alternative name(s):
PTS system N-acetylmuramic acid-specific EIIB component
N-acetylmuramic acid permease IIC component
Alternative name(s):
PTS system N-acetylmuramic acid-specific EIIC component
Gene namesi
Name:murP
Synonyms:yfeV
Ordered Locus Names:b2429, JW2422
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG14163. murP.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 123123CytoplasmicSequence analysisAdd
BLAST
Transmembranei124 – 14421HelicalPROSITE-ProRule annotationAdd
BLAST
Topological domaini145 – 15713PeriplasmicSequence analysisAdd
BLAST
Transmembranei158 – 17821HelicalPROSITE-ProRule annotationAdd
BLAST
Topological domaini179 – 1802CytoplasmicSequence analysis
Transmembranei181 – 20121HelicalPROSITE-ProRule annotationAdd
BLAST
Topological domaini202 – 21716PeriplasmicSequence analysisAdd
BLAST
Transmembranei218 – 23821HelicalPROSITE-ProRule annotationAdd
BLAST
Topological domaini239 – 26022CytoplasmicSequence analysisAdd
BLAST
Transmembranei261 – 28121HelicalPROSITE-ProRule annotationAdd
BLAST
Topological domaini282 – 30120PeriplasmicSequence analysisAdd
BLAST
Transmembranei302 – 32221HelicalPROSITE-ProRule annotationAdd
BLAST
Topological domaini323 – 33412CytoplasmicSequence analysisAdd
BLAST
Transmembranei335 – 35521HelicalPROSITE-ProRule annotationAdd
BLAST
Topological domaini356 – 36813PeriplasmicSequence analysisAdd
BLAST
Transmembranei369 – 38921HelicalPROSITE-ProRule annotationAdd
BLAST
Topological domaini390 – 3934CytoplasmicSequence analysis
Transmembranei394 – 41421HelicalPROSITE-ProRule annotationAdd
BLAST
Topological domaini415 – 44026PeriplasmicSequence analysisAdd
BLAST
Transmembranei441 – 46121HelicalPROSITE-ProRule annotationAdd
BLAST
Topological domaini462 – 47413CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • integral component of plasma membrane Source: EcoCyc
  • membrane Source: EcoCyc
  • plasma membrane Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 474474PTS system N-acetylmuramic acid-specific EIIBC componentPRO_0000186709Add
BLAST

Proteomic databases

PaxDbiP77272.
PRIDEiP77272.

Expressioni

Inductioni

Induced by MurNAc 6-phosphate that releases the repressor MurR from the DNA. Also up-regulated by the cAMP receptor protein crp via the binding of crp-cAMP to a class I site upstream of the murQ promoter. Repressed by MurR in the absence of MurNAc 6-phosphate.1 Publication

Interactioni

Protein-protein interaction databases

BioGridi4260573. 11 interactions.
STRINGi511145.b2429.

Structurei

3D structure databases

ProteinModelPortaliP77272.
SMRiP77272. Positions 6-84.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 8989PTS EIIB type-1PROSITE-ProRule annotationAdd
BLAST
Domaini115 – 474360PTS EIIC type-1PROSITE-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 EIIC domain forms the PTS system translocation channel and contains the specific substrate-binding site.

Sequence similaritiesi

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

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105C5Y. Bacteria.
COG2190. LUCA.
HOGENOMiHOG000102024.
InParanoidiP77272.
KOiK11191.
K11192.
OMAiGKVMLYL.
OrthoDBiEOG6MPWQX.
PhylomeDBiP77272.

Family and domain databases

Gene3Di3.30.1360.60. 1 hit.
InterProiIPR018113. PTrfase_EIIB_Cys.
IPR003352. PTS_EIIC.
IPR013013. PTS_EIIC_1.
IPR001996. PTS_IIB_1.
[Graphical view]
PfamiPF00367. PTS_EIIB. 1 hit.
PF02378. PTS_EIIC. 1 hit.
[Graphical view]
SUPFAMiSSF55604. SSF55604. 1 hit.
PROSITEiPS51098. PTS_EIIB_TYPE_1. 1 hit.
PS01035. PTS_EIIB_TYPE_1_CYS. 1 hit.
PS51103. PTS_EIIC_TYPE_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P77272-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKEISSELL NTILTRVGGP GNIASCGNCM TRLRLGVHDS SLVDPNIKTL
60 70 80 90 100
EGVKGVILTS DQVQVVFGPG KAHRAAKAMS ELLGEAPVQD AAEIAAQNKR
110 120 130 140 150
QLKAKQTSGV QQFLAKFATI FTPLIPGFIA AGLLLGIATL IATVMHVPAD
160 170 180 190 200
AQGTLPDALN FMKVFSKGLF TFLVILVGYN AAQAFGGTGV NGAIIAALFL
210 220 230 240 250
LGYNPAATTG YYAGFHDFFG LPIDPRGNII GVLIAAWACA RIEGMVRRFM
260 270 280 290 300
PDDLDMLLTS LITLLITATL AYLIIMPLGG WLFEGMSWLF MHLNSNPFGC
310 320 330 340 350
AVLAGLFLIA VVFGVHQGFI PVYLALMDSQ GFNSLFPILS MAGAGQVGAA
360 370 380 390 400
LALYWRAQPH SALRSQVRGA IIPGLLGVGE PLIYGVTLPR MKPFVTACLG
410 420 430 440 450
GAAGGLFIGL IAWWGLPMGL NSAFGPSGLV ALPLMTSAQG ILPAMAVYAG
460 470
GILVAWVCGF IFTTLFGCRN VNLD
Length:474
Mass (Da):49,802
Last modified:February 1, 1997 - v1
Checksum:iEA5D8849A303737C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC75482.1.
AP009048 Genomic DNA. Translation: BAA16313.1.
PIRiD65017.
RefSeqiNP_416924.1. NC_000913.3.
WP_001040483.1. NZ_CP014272.1.

Genome annotation databases

EnsemblBacteriaiAAC75482; AAC75482; b2429.
BAA16313; BAA16313; BAA16313.
GeneIDi946894.
KEGGiecj:JW2422.
eco:b2429.
PATRICi32120243. VBIEscCol129921_2524.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC75482.1.
AP009048 Genomic DNA. Translation: BAA16313.1.
PIRiD65017.
RefSeqiNP_416924.1. NC_000913.3.
WP_001040483.1. NZ_CP014272.1.

3D structure databases

ProteinModelPortaliP77272.
SMRiP77272. Positions 6-84.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260573. 11 interactions.
STRINGi511145.b2429.

Protein family/group databases

TCDBi4.A.1.2.7. the pts glucose-glucoside (glc) family.

Proteomic databases

PaxDbiP77272.
PRIDEiP77272.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75482; AAC75482; b2429.
BAA16313; BAA16313; BAA16313.
GeneIDi946894.
KEGGiecj:JW2422.
eco:b2429.
PATRICi32120243. VBIEscCol129921_2524.

Organism-specific databases

EchoBASEiEB3915.
EcoGeneiEG14163. murP.

Phylogenomic databases

eggNOGiENOG4105C5Y. Bacteria.
COG2190. LUCA.
HOGENOMiHOG000102024.
InParanoidiP77272.
KOiK11191.
K11192.
OMAiGKVMLYL.
OrthoDBiEOG6MPWQX.
PhylomeDBiP77272.

Enzyme and pathway databases

BioCyciEcoCyc:MONOMER0-5.
ECOL316407:JW2422-MONOMER.
MetaCyc:MONOMER0-5.

Miscellaneous databases

PROiP77272.

Family and domain databases

Gene3Di3.30.1360.60. 1 hit.
InterProiIPR018113. PTrfase_EIIB_Cys.
IPR003352. PTS_EIIC.
IPR013013. PTS_EIIC_1.
IPR001996. PTS_IIB_1.
[Graphical view]
PfamiPF00367. PTS_EIIB. 1 hit.
PF02378. PTS_EIIC. 1 hit.
[Graphical view]
SUPFAMiSSF55604. SSF55604. 1 hit.
PROSITEiPS51098. PTS_EIIB_TYPE_1. 1 hit.
PS01035. PTS_EIIB_TYPE_1_CYS. 1 hit.
PS51103. PTS_EIIC_TYPE_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features."
    Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T.
    , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.
    DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. "Identification of a phosphotransferase system of Escherichia coli required for growth on N-acetylmuramic acid."
    Dahl U., Jaeger T., Nguyen B.T., Sattler J.M., Mayer C.
    J. Bacteriol. 186:2385-2392(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN MURNAC UPTAKE, CATALYTIC ACTIVITY.
  5. "Global topology analysis of the Escherichia coli inner membrane proteome."
    Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.
    Science 308:1321-1323(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
    Strain: K12 / MG1655 / ATCC 47076.
  6. "MurQ etherase is required by Escherichia coli in order to metabolize anhydro-N-acetylmuramic acid obtained either from the environment or from its own cell wall."
    Uehara T., Suefuji K., Jaeger T., Mayer C., Park J.T.
    J. Bacteriol. 188:1660-1662(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ANHMURNAC UPTAKE.
  7. "The transcriptional factors MurR and catabolite activator protein regulate N-acetylmuramic acid catabolism in Escherichia coli."
    Jaeger T., Mayer C.
    J. Bacteriol. 190:6598-6608(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
    Strain: K12 / MG1655 / ATCC 47076.

Entry informationi

Entry nameiPTYBC_ECOLI
AccessioniPrimary (citable) accession number: P77272
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: February 1, 1997
Last modified: June 8, 2016
This is version 135 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The PTS domain EIIA required for activity was shown to be the crr-encoded enzyme IIA-glucose, EIIA-Glc.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. 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.