mrcB:Gene Product(s)

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Nomenclature Function Interactions Localization Sequence Domains Structure Resources Accessions Links References Suggestions

Nomenclature

See Help:Product_nomenclature for help entering or editing information in this section of EcoliWiki.

Standard name

MrcB

Synonyms

fused glycosyl transferase[1], transpeptidase[1], B0149[2][1], PonB[2][1], PbpF[2][1], MrcB[2][1], PBP1B[2][1] , ECK0148, JW0145, pbpF, ponB, b0149

Product description

MrcB[2][3];

Component of penicillin-binding protein 1B[3]

Murein polymerase, PBP1B; bifunctional murein transglycosylase and transpeptidase; penicillin-binding protein 1B; dimeric[4]

EC number (for enzymes)

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Notes

Function

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<protect> Gene Ontology
See Help:Gene_ontology for help entering or editing GO terms and GO annotations in EcoliWiki.

Qualifier GO ID GO term name Reference Evidence Code with/from Aspect Notes Status
GO:0005887

integral to plasma membrane

C

Seeded from Riley et al 2006 [1].

Missing: evidence, reference

GO:0005886

plasma membrane

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0997

C

Seeded from EcoCyc (v14.0)

complete

GO:0005886

plasma membrane

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-1003

C

Seeded from EcoCyc (v14.0)

complete

GO:0008955

peptidoglycan glycosyltransferase activity

PMID:6389538[5]

IDA: Inferred from Direct Assay

F

complete

GO:0051518

positive regulation of bipolar cell growth

PMID:330236[6]

IDA: Inferred from Direct Assay

P

Cephaloridine has a high affinity for PBP1B. When this happens, cell elongation is inhibited, causing the cell to lyse.

complete

GO:0009002

serine-type D-Ala-D-Ala carboxypeptidase activity

PMID:6389538[5]

IDA: Inferred from Direct Assay

F

complete

GO:0008658

penicillin binding

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR001460

F

Seeded from EcoCyc (v14.0)

complete

GO:0008955

peptidoglycan glycosyltransferase activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR011813

F

Seeded from EcoCyc (v14.0)

complete

GO:0008955

peptidoglycan glycosyltransferase activity

GOA:spec
GO_REF:0000003

IEA: Inferred from Electronic Annotation

EC:2.4.1.129

F

Seeded from EcoCyc (v14.0)

complete

GO:0009252

peptidoglycan biosynthetic process

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR001264

P

Seeded from EcoCyc (v14.0)

complete

GO:0009252

peptidoglycan biosynthetic process

PMID:16569861[7]

IMP: Inferred from Mutant Phenotype

P

Table 1 shows a PBP1B deficient strain produce lipid II instead of peptidoglycan.

complete

GO:0009252

peptidoglycan biosynthetic process

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0573

P

Seeded from EcoCyc (v14.0)

complete

GO:0009274

peptidoglycan-based cell wall

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR001264

C

Seeded from EcoCyc (v14.0)

complete

GO:0009274

peptidoglycan-based cell wall

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR011813

C

Seeded from EcoCyc (v14.0)

complete

GO:0016020

membrane

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0472

C

Seeded from EcoCyc (v14.0)

complete

GO:0016020

membrane

PMID:16858726[8]

IDA: Inferred from Direct Assay

C

Seeded from EcoCyc (v14.0)

complete

GO:0016021

integral to membrane

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0812

C

Seeded from EcoCyc (v14.0)

complete

GO:0016021

integral to membrane

GO_REF:0000023

IEA: Inferred from Electronic Annotation

SP_SL:SL-9906

C

Seeded from EcoCyc (v14.0)

complete

GO:0046677

response to antibiotic

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR011813

P

Seeded from EcoCyc (v14.0)

complete

GO:0046677

response to antibiotic

PMID:371539[9]

IDA: Inferred from Direct Assay

SP_KW:KW-0046


P

Table 1 shows Cephalosporin Beta-Lactams exhibit high affinity for PBP1B.

complete

Interactions See Help:Product_interactions for help entering or editing information about gene product interactions in this section of EcoliWiki.

Partner Type Partner Notes References Evidence

Protein

Subunits of penicillin-binding protein 1B

could be indirect

Protein

talB

PMID:19402753[10]

LCMS(ID Probability):99.6

Protein

hupA

PMID:19402753[10]

LCMS(ID Probability):99.6

Protein

hemB

PMID:19402753[10]

LCMS(ID Probability):99.6

Protein

ppsA

PMID:19402753[10]

LCMS(ID Probability):99.6

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Notes

Localization

See Help:Product_localization for how to add or edit information in this section of EcoliWiki.

Compartment Description Evidence Reference/Source Notes

plasma membrane


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Notes

Structure and Physical Properties

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<protect> Physical Properties See Help:Product_physical_properties for help entering or editing information about the physical properties of this gene product.

Name
Sequence

at EcoCyc

MAGNDREPIG RKGKPTRPVK QKVSRRRYED DDDYDDYDDY EDEEPMPRKG KGKGKGRKPR
GKRGWLWLLL KLAIVFAVLI AIYGVYLDQK IRSRIDGKVW QLPAAVYGRM VNLEPDMTIS
KNEMVKLLEA TQYRQVSKMT RPGEFTVQAN SIEMIRRPFD FPDSKEGQVR ARLTFDGDHL
ATIVNMENNR QFGFFRLDPR LITMISSPNG EQRLFVPRSG FPDLLVDTLL ATEDRHFYEH
DGISLYSIGR AVLANLTAGR TVQGASTLTQ QLVKNLFLSS ERSYWRKANE AYMALIMDAR
YSKDRILELY MNEVYLGQSG DNEIRGFPLA SLYYFGRPVE ELSLDQQALL VGMVKGASIY
NPWRNPKLAL ERRNLVLRLL QQQQIIDQEL YDMLSARPLG VQPRGGVISP QPAFMQLVRQ
ELQAKLGDKV KDLSGVKIFT TFDSVAQDAA EKAAVEGIPA LKKQRKLSDL ETAIVVVDRF
SGEVRAMVGG SEPQFAGYNR AMQARRSIGS LAKPATYLTA LSQPKIYRLN TWIADAPIAL
RQPNGQVWSP QNDDRRYSES GRVMLVDALT RSMNVPTVNL GMALGLPAVT ETWIKLGVPK
DQLHPVPAML LGALNLTPIE VAQAFQTIAS GGNRAPLSAL RSVIAEDGKV LYQSFPQAER
AVPAQAAYLT LWTMQQVVQR GTGRQLGAKY PNLHLAGKTG TTNNNVDTWF AGIDGSTVTI
TWVGRDNNQP TKLYGASGAM SIYQRYLANQ TPTPLNLVPP EDIADMGVDY DGNFVCSGGM
RILPVWTSDP QSLCQQSEMQ QQPSGNPFDQ SSQPQQQPQQ QPAQQEQKDS DGVAGWIKDM FGSN
Length

844

Mol. Wt

94.294 kDa

pI

9.5 (calculated)

Extinction coefficient

116,200 - 116,450 (calc based on 30 Y, 13 W, and 2 C residues)


Domains/Motifs/Modification Sites

See Help:Product_domains_motifs for help entering or editing information in this section of EcoliWiki.

Type Residues Description Notes References

Domain

472..744

PF00905 Penicillin binding protein transpeptidase domain

PMID:19920124[11]

Domain

198..381

PF00912 Transglycosylase

PMID:19920124[11]

<motif_map/>

Structure
See Help:Product_structure for help entering or editing information in this section of EcoliWiki.

Structures

<beststructure> gene=mrcB taxon=562,83333 </beststructure>

Models

View models at:

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Structure figures

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Notes

Gene Product Resources

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See Help:Product_resources for help with entering or editing information in this section of EcoliWiki.

Resource type Source Notes/Reference

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Notes

Accessions in Other Databases

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See Help:Gene_accessions for help with entering information into the Gene Accessions table.

Database Accession Notes

NCBI (Protein) (EcoliWiki Page)

GI:16128142

Escherichia coli str. K-12 substr. MG1655

NCBI (Protein) (EcoliWiki Page)

GeneID:944843

Escherichia coli str. K-12 substr. MG1655

ASAP

ASAP:ABE-0000516

Escherichia coli str. K-12 substr. MG1655

UniProt (EcoliWiki Page)

UniProtKB/Swiss-Prot:P02919

Escherichia coli str. K-12 substr. MG1655

EcoCyc

EcoCyc:EG10605

Escherichia coli str. K-12 substr. MG1655

EcoGene

EcoGene:EG10605

Escherichia coli str. K-12 substr. MG1655

NCBI (Gene) (EcoliWiki Page)

GeneID:944843

Escherichia coli str. K-12 substr. MG1655

RegulonDB

RegulonDB:ECK120000598

Escherichia coli str. K-12 substr. MG1655

EchoBASE

EchoBASE:EB0600

Escherichia coli str. K-12 substr. MG1655

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Notes

Links

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References

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See Help:References for how to manage references in EcoliWiki.

  1. 1.0 1.1 1.2 1.3 1.4 1.5 1.6 1.7 1.8 1.9 Riley, M. et al. (2006) Nucleic Acids Res 34:1-6 (corrected supplemental data from B. Wanner)
  2. 2.0 2.1 2.2 2.3 2.4 2.5 EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  3. 3.0 3.1 EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  4. EcoGene: Rudd, KE (2000) EcoGene: a genome sequence database for Escherichia coli K-12. Nucleic Acids Res 28:60-4.
  5. 5.0 5.1 Nakagawa, J et al. (1984) Functional biosynthesis of cell wall peptidoglycan by polymorphic bifunctional polypeptides. Penicillin-binding protein 1Bs of Escherichia coli with activities of transglycosylase and transpeptidase. J. Biol. Chem. 259 13937-46 PubMed
  6. Spratt, BG & Jobanputra, V (1977) Mutants of Escherichia coli which lack a component of penicillin-binding protein 1 are viable. FEBS Lett. 79 374-8 PubMed
  7. Ramachandran, V et al. (2006) Screen for inhibitors of the coupled transglycosylase-transpeptidase of peptidoglycan biosynthesis in Escherichia coli. Antimicrob. Agents Chemother. 50 1425-32 PubMed
  8. Lasserre, JP et al. (2006) A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis. Electrophoresis 27 3306-21 PubMed
  9. Nozaki, Y et al. (1979) SCE-963, a new potent cephalosporin with high affinity for penicillin-binding proteins 1 and 3 of Escherichia coli. Antimicrob. Agents Chemother. 15 20-7 PubMed
  10. 10.0 10.1 10.2 10.3 Hu, P et al. (2009) Global functional atlas of Escherichia coli encompassing previously uncharacterized proteins. PLoS Biol. 7 e96 PubMed
  11. 11.0 11.1 Finn, RD et al. (2010) The Pfam protein families database. Nucleic Acids Res. 38 D211-22 PubMed

Categories

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