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]

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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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(s) Evidence Code with/from Aspect Notes Status
GO:0005624

membrane fraction

PMID:16858726[5]

IDA: Inferred from Direct Assay

C

Seeded from EcoCyc [6]

complete

GO:0003824

catalytic activity

GO_REF:0000002
GO_REF:0000004

IEA: Inferred from Electronic Annotation

InterPro:IPR001264
SP_KW:KW-0511

F

Seeded from EcoCyc [6]

complete

GO:0007047

cell wall organization

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0961

P

Seeded from EcoCyc 12.5 [7]

complete

GO:0008233

peptidase activity

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR011813

F

Seeded from EcoCyc [6]

complete

GO:0008360

regulation of cell shape

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0133

P

Seeded from EcoCyc [6]

complete

GO:0008658

penicillin binding

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR001460

F

Seeded from EcoCyc 12.5 [7]

complete

GO:0008955

peptidoglycan glycosyltransferase activity

GO_REF:0000002
GO_REF:0000003

IEA: Inferred from Electronic Annotation

InterPro:IPR011813
EC:2.4.1.129

F

Seeded from EcoCyc 12.5 [7]

complete

GO:0009252

peptidoglycan biosynthetic process

GO_REF:0000002
GO_REF:0000002
GO_REF:0000004

IEA: Inferred from Electronic Annotation

InterPro:IPR001264
InterPro:IPR011813
SP_KW:KW-0573

P

Seeded from EcoCyc [6]

complete

GO:0009273

peptidoglycan-based cell wall biogenesis

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR001460

P

Seeded from EcoCyc [6]

complete

GO:0009274

peptidoglycan-based cell wall

GO_REF:0000002
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR001264
InterPro:IPR011813

C

Seeded from EcoCyc [6]

complete

GO:0016020

membrane

GO_REF:0000004
GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0397
SP_KW:KW-0472

C

Seeded from EcoCyc 12.5 [7]

complete

GO:0016021

integral to membrane

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0812

C

Seeded from EcoCyc [6]

complete

GO:0016740

transferase activity

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0808

F

Seeded from EcoCyc [6]

complete

GO:0016757

transferase activity, transferring glycosyl groups

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0328

F

Seeded from EcoCyc [6]

complete

GO:0016787

hydrolase activity

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0378

F

Seeded from EcoCyc [6]

complete

GO:0046677

response to antibiotic

GO_REF:0000002
GO_REF:0000004

IEA: Inferred from Electronic Annotation

InterPro:IPR011813
SP_KW:KW-0046

P

Seeded from EcoCyc [6]

complete

GO:0005887

integral to plasma membrane

C

Seeded from Riley et al 2006 [1].

required field missing

GO:0005739

mitochondrion

PMID:16858726[5]

IDA: Inferred from Direct Assay

C

Seeded from EcoCyc [6]

complete

GO:0005886

plasma membrane

GO_REF:0000004
GO_REF:0000004
GO_REF:0000023

IEA: Inferred from Electronic Annotation

SP_KW:KW-0997
SP_KW:KW-1003
SP_SL:SL-0037

C

Seeded from EcoCyc [6]

complete

GO:0008144

drug binding

PMID:10564478[8]
PMID:11933234[9]
PMID:12325012[10]
PMID:365089[11]
PMID:371539[12]
PMID:6268122[13]
PMID:6373702[14]
PMID:6376452[15]
PMID:6427167[16]
PMID:6448021[17]
PMID:6448573[18]
PMID:6941742[19]
PMID:7018389[20]
PMID:7049076[21]

IDA: Inferred from Direct Assay














F

Seeded from EcoCyc [6]

complete

GO:0046349

amino sugar biosynthetic process

P

Seeded from EcoCyc 11.1[3].

required fields missing

GO:0042493

response to drug

P

Seeded from EcoCyc 11.1[3].

required fields missing

GO:0000910

cytokinesis

P

Seeded from EcoCyc 11.1[3].

required fields missing

GO:0008955

peptidoglycan glycosyltransferase activity

PMID:6389538[22]

IDA: Inferred from Direct Assay

F

complete

GO:0009002

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

PMID:6389538[22]

IDA: Inferred from Direct Assay

F

complete

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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


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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 Notes

plasma membrane


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Notes

Structure and Physical Properties

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

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)

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Domains/Motifs/Modification Sites

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

Type Residues Description Notes
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<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

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

EcoCyc (EcoliWiki Page)

EcoCyc:EG10605-MONOMER

UniProt (EcoliWiki Page)

UniProt:P02919

PFAM (EcoliWiki Page)

PFAM:PF00912

RefSeq (EcoliWiki Page)

RefSeq:NP_414691

ECOO157CYC (EcoliWiki Page)

ECOO157CYC:MRCB-MONOMER


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Notes

Links

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Name URL Comments
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References

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

  1. ↑ 1.00 1.01 1.02 1.03 1.04 1.05 1.06 1.07 1.08 1.09 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 3.2 3.3 3.4 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 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
  6. ↑ 6.00 6.01 6.02 6.03 6.04 6.05 6.06 6.07 6.08 6.09 6.10 6.11 6.12 6.13 6.14 EcoCyc (release 13.0; 2009) Keseler, IM et al. (2009) Nucleic Acids Res. 37(Database issue):D464-70
  7. ↑ 7.0 7.1 7.2 7.3 EcoCyc (release 12.5; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  8. ↑ Terrak, M et al. (1999) The catalytic, glycosyl transferase and acyl transferase modules of the cell wall peptidoglycan-polymerizing penicillin-binding protein 1b of Escherichia coli. Mol Microbiol 34 350-64 PubMed
  9. ↑ Stembera, K et al. (2002) Moenomycin-mediated affinity purification of penicillin-binding protein 1b. Chembiochem 3 332-40 PubMed
  10. ↑ Stembera, K et al. (2002) A surface plasmon resonance analysis of the interaction between the antibiotic moenomycin A and penicillin-binding protein 1b. Chembiochem 3 559-65 PubMed
  11. ↑ Ohya, S et al. (1978) New cephamycin antibiotic, CS-1170: binding affinity to penicillin-binding proteins and inhibition of peptidoglycan cross-linking reactions in Escherichia coli. Antimicrob Agents Chemother 14 780-5 PubMed
  12. ↑ 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
  13. ↑ Masuyoshi, S et al. (1981) Cefotaxime: binding affinity to penicillin-binding proteins and morphological changes of Escherichia coli and Pseudomonas aeruginosa. Arzneimittelforschung 31 1070-2 PubMed
  14. ↑ Rojo, F et al. (1984) Binding of 125I-labeled beta-lactam antibiotics to the penicillin binding proteins of Escherichia coli. J Antibiot (Tokyo) 37 389-93 PubMed
  15. ↑ Rake, JB et al. (1984) Affinity of cefonicid, a long-acting cephalosporin, for the penicillin-binding proteins of Escherichia coli K-12. J Antibiot (Tokyo) 37 572-6 PubMed
  16. ↑ Hashizume, T et al. (1984) Studies on the mechanism of action of imipenem (N-formimidoylthienamycin) in vitro: binding to the penicillin-binding proteins (PBPs) in Escherichia coli and Pseudomonas aeruginosa, and inhibition of enzyme activities due to the PBPs in E. coli. J Antibiot (Tokyo) 37 394-400 PubMed
  17. ↑ Matsubara, N et al. (1980) Affinity of cefoperazone for penicillin-binding proteins. Antimicrob Agents Chemother 18 195-9 PubMed
  18. ↑ Komatsu, Y & Nishikawa, T (1980) Moxalactam (6059-S), a new 1-oxa-beta-lactam: binding affinity for penicillin-binding proteins of Escherichia coli K-12. Antimicrob Agents Chemother 17 316-21 PubMed
  19. ↑ Tsuchiya, K et al. (1981) Cefmenoxime (SCE-1365), a novel broad-spectrum cephalosporin: in vitro and in vivo antibacterial activities. Antimicrob Agents Chemother 19 56-65 PubMed
  20. ↑ Shigi, Y et al. (1981) Differences between ceftizoxime and its stereoisomer in antibacterial activity and affinity for penicillin-binding proteins. Antimicrob Agents Chemother 19 393-6 PubMed
  21. ↑ Ohya, S et al. (1982) Penem derivatives: beta-lactamase stability and affinity for penicillin-binding proteins in Escherichia coli. Antimicrob Agents Chemother 21 492-7 PubMed
  22. ↑ 22.0 22.1 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

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