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Protein

Murein hydrolase activator EnvC

Gene

envC

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Activator of the cell wall hydrolases AmiA and AmiB. Required for septal murein cleavage and daughter cell separation during cell division. In vitro, exhibits weak endoproteolytic activity on beta-casein.5 Publications

GO - Molecular functioni

  • hydrolase activity Source: EcoliWiki

GO - Biological processi

  • autolysis Source: EcoliWiki
  • cell cycle Source: UniProtKB-KW
  • cell separation after cytokinesis Source: EcoliWiki
  • peptidoglycan-based cell wall biogenesis Source: EcoCyc
  • positive regulation of hydrolase activity Source: EcoCyc
  • response to drug Source: EcoCyc
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division

Enzyme and pathway databases

BioCyciEcoCyc:EG12297-MONOMER.
ECOL316407:JW5646-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Murein hydrolase activator EnvC
Alternative name(s):
Septal ring factor
Gene namesi
Name:envC
Synonyms:yibP
Ordered Locus Names:b3613, JW5646
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12297. envC.

Subcellular locationi

GO - Cellular componenti

  • cell division site Source: EcoliWiki
  • outer membrane-bounded periplasmic space Source: EcoCyc
  • periplasmic space Source: EcoCyc
  • plasma membrane Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Periplasm

Pathology & Biotechi

Disruption phenotypei

Mutants show defects in septation and separation, and form very long filaments (1.5-fold increase). The phenotype is exacerbated when combined with nlpD (over 8-fold longer), more exacerbated with a triple mepM (yebA) or ygeR disruption (15-fold longer) and further yet by the quadruple disruption mutant (envC-nlpD-mepM(yebA)-ygeR, over 21-fold longer). Quadruple mutants are less sensitive to ampicillin lysis.4 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi321 – 3211K → A: Retains AmiA and AmiB activation. 1 Publication
Mutagenesisi321 – 3211K → E: Loss of AmiA and AmiB activation; does not complement double envC-nlpD disruption, protein localizes normally. 1 Publication
Mutagenesisi324 – 3241V → A: Retains AmiA and AmiB activation. 1 Publication
Mutagenesisi324 – 3241V → E: Loss of AmiA and AmiB activation; does not complement double envC-nlpD disruption, protein localizes normally. 1 Publication
Mutagenesisi350 – 3501Y → A: Loss of AmiA and AmiB activation; does not complement double envC-nlpD disruption, protein localizes normally. 1 Publication
Mutagenesisi353 – 3531V → A: Loss of AmiA and AmiB activation; does not complement double envC-nlpD disruption, protein localizes normally. 1 Publication
Mutagenesisi366 – 3661Y → H: Partially unstable, loss of AmiA and AmiB activation. 1 Publication
Mutagenesisi401 – 4011Y → E: Partially unstable, loss of AmiA and AmiB activation; does not complement double envC-nlpD disruption, protein localizes normally. 1 Publication
Mutagenesisi405 – 4051R → H: Loss of activation of amidases; does not complement double envC-nlpD disruption, protein localizes normally. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3434Sequence analysisAdd
BLAST
Chaini35 – 419385Murein hydrolase activator EnvCPRO_0000169611Add
BLAST

Proteomic databases

PaxDbiP37690.
PRIDEiP37690.

Interactioni

Protein-protein interaction databases

BioGridi4263303. 365 interactions.
DIPiDIP-12426N.
STRINGi511145.b3613.

Structurei

Secondary structure

1
419
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi293 – 2964Combined sources
Beta strandi306 – 3083Combined sources
Beta strandi312 – 3154Combined sources
Beta strandi321 – 3266Combined sources
Beta strandi332 – 3343Combined sources
Beta strandi336 – 34611Combined sources
Beta strandi350 – 35910Combined sources
Beta strandi362 – 37413Combined sources
Beta strandi385 – 3906Combined sources
Beta strandi399 – 4068Combined sources
Beta strandi409 – 4113Combined sources
Helixi414 – 4163Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4BH5X-ray1.57A/B/C/D278-419[»]
ProteinModelPortaliP37690.
SMRiP37690. Positions 290-419.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili35 – 12490Sequence analysisAdd
BLAST
Coiled coili155 – 271117Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi56 – 225170Gln-richAdd
BLAST

Domaini

The coiled-coil domain is necessary and sufficient for recruitment to the divisome. The LytM domain is required for proper septal peptidoglycan splitting.1 Publication

Sequence similaritiesi

Belongs to the peptidase M23B family.Curated

Keywords - Domaini

Coiled coil, Signal

Phylogenomic databases

eggNOGiENOG41063SB. Bacteria.
COG4942. LUCA.
HOGENOMiHOG000270189.
InParanoidiP37690.
OMAiPEKFART.
OrthoDBiEOG61ZTBJ.
PhylomeDBiP37690.

Family and domain databases

InterProiIPR011055. Dup_hybrid_motif.
IPR016047. Peptidase_M23.
[Graphical view]
PfamiPF01551. Peptidase_M23. 1 hit.
[Graphical view]
SUPFAMiSSF51261. SSF51261. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P37690-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTRAVKPRRF AIRPIIYASV LSAGVLLCAF SAHADERDQL KSIQADIAAK
60 70 80 90 100
ERAVRQKQQQ RASLLAQLKK QEEAISEATR KLRETQNTLN QLNKQIDEMN
110 120 130 140 150
ASIAKLEQQK AAQERSLAAQ LDAAFRQGEH TGIQLILSGE ESQRGQRLQA
160 170 180 190 200
YFGYLNQARQ ETIAQLKQTR EEVAMQRAEL EEKQSEQQTL LYEQRAQQAK
210 220 230 240 250
LTQALNERKK TLAGLESSIQ QGQQQLSELR ANESRLRNSI ARAEAAAKAR
260 270 280 290 300
AEREAREAQA VRDRQKEATR KGTTYKPTES EKSLMSRTGG LGAPRGQAFW
310 320 330 340 350
PVRGPTLHRY GEQLQGELRW KGMVIGASEG TEVKAIADGR VILADWLQGY
360 370 380 390 400
GLVVVVEHGK GDMSLYGYNQ SALVSVGSQV RAGQPIALVG SSGGQGRPSL
410
YFEIRRQGQA VNPQPWLGR
Length:419
Mass (Da):46,595
Last modified:December 15, 1998 - v2
Checksum:i4C786105C2F95BD5
GO

Sequence cautioni

The sequence AAB18590.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00039 Genomic DNA. Translation: AAB18590.1. Different initiation.
U00096 Genomic DNA. Translation: AAC76637.2.
AP009048 Genomic DNA. Translation: BAE77679.1.
RefSeqiNP_418070.6. NC_000913.3.

Genome annotation databases

EnsemblBacteriaiAAC76637; AAC76637; b3613.
BAE77679; BAE77679; BAE77679.
GeneIDi948129.
KEGGiecj:JW5646.
eco:b3613.
PATRICi32122713. VBIEscCol129921_3733.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00039 Genomic DNA. Translation: AAB18590.1. Different initiation.
U00096 Genomic DNA. Translation: AAC76637.2.
AP009048 Genomic DNA. Translation: BAE77679.1.
RefSeqiNP_418070.6. NC_000913.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4BH5X-ray1.57A/B/C/D278-419[»]
ProteinModelPortaliP37690.
SMRiP37690. Positions 290-419.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263303. 365 interactions.
DIPiDIP-12426N.
STRINGi511145.b3613.

Proteomic databases

PaxDbiP37690.
PRIDEiP37690.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76637; AAC76637; b3613.
BAE77679; BAE77679; BAE77679.
GeneIDi948129.
KEGGiecj:JW5646.
eco:b3613.
PATRICi32122713. VBIEscCol129921_3733.

Organism-specific databases

EchoBASEiEB2205.
EcoGeneiEG12297. envC.

Phylogenomic databases

eggNOGiENOG41063SB. Bacteria.
COG4942. LUCA.
HOGENOMiHOG000270189.
InParanoidiP37690.
OMAiPEKFART.
OrthoDBiEOG61ZTBJ.
PhylomeDBiP37690.

Enzyme and pathway databases

BioCyciEcoCyc:EG12297-MONOMER.
ECOL316407:JW5646-MONOMER.

Miscellaneous databases

PROiP37690.

Family and domain databases

InterProiIPR011055. Dup_hybrid_motif.
IPR016047. Peptidase_M23.
[Graphical view]
PfamiPF01551. Peptidase_M23. 1 hit.
[Graphical view]
SUPFAMiSSF51261. SSF51261. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Analysis of the Escherichia coli genome. V. DNA sequence of the region from 76.0 to 81.5 minutes."
    Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.
    Nucleic Acids Res. 22:2576-2586(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  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 and characterization of the Escherichia coli envC gene encoding a periplasmic coiled-coil protein with putative peptidase activity."
    Hara H., Narita S., Karibian D., Park J.T., Yamamoto Y., Nishimura Y.
    FEMS Microbiol. Lett. 212:229-236(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
    Strain: K12.
  5. "Proteolytic activity of YibP protein in Escherichia coli."
    Ichimura T., Yamazoe M., Maeda M., Wada C., Hiraga S.
    J. Bacteriol. 184:2595-2602(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A PROTEASE, DISRUPTION PHENOTYPE.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  6. "Screening for synthetic lethal mutants in Escherichia coli and identification of EnvC (YibP) as a periplasmic septal ring factor with murein hydrolase activity."
    Bernhardt T.G., de Boer P.A.
    Mol. Microbiol. 52:1255-1269(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
    Strain: K12.
  7. "LytM-domain factors are required for daughter cell separation and rapid ampicillin-induced lysis in Escherichia coli."
    Uehara T., Dinh T., Bernhardt T.G.
    J. Bacteriol. 191:5094-5107(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
    Strain: K12 / MG1655 / TB28.
  8. "Daughter cell separation is controlled by cytokinetic ring-activated cell wall hydrolysis."
    Uehara T., Parzych K.R., Dinh T., Bernhardt T.G.
    EMBO J. 29:1412-1422(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS AN ACTIVATOR, DOMAIN.
    Strain: K12 / MG1655 / ATCC 47076.
  9. "Structure-function analysis of the LytM domain of EnvC, an activator of cell wall remodelling at the Escherichia coli division site."
    Peters N.T., Morlot C., Yang D.C., Uehara T., Vernet T., Bernhardt T.G.
    Mol. Microbiol. 89:690-701(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.57 ANGSTROMS) OF 278-419, FUNCTION, MUTAGENESIS OF LYS-321; VAL-324; TYR-350; VAL-353; TYR-366; TYR-401 AND ARG-405.
    Strain: K12 / MG1655 / TB28.

Entry informationi

Entry nameiENVC_ECOLI
AccessioniPrimary (citable) accession number: P37690
Secondary accession number(s): Q2M7S7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: December 15, 1998
Last modified: April 13, 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

Caution

Was originally thought to have murein hydrolase activity.1 Publication
Unlike many members of this family does not have peptidase activity.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Peptidase families
    Classification of peptidase families and list of entries
  4. 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.