ENVC_ECOLI
ID ENVC_ECOLI Reviewed; 419 AA.
AC P37690; Q2M7S7;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Murein hydrolase activator EnvC;
DE AltName: Full=Septal ring factor;
DE Flags: Precursor;
GN Name=envC; Synonyms=yibP; OrderedLocusNames=b3613, JW5646;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8041620; DOI=10.1093/nar/22.13.2576;
RA Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.;
RT "Analysis of the Escherichia coli genome. V. DNA sequence of the region
RT from 76.0 to 81.5 minutes.";
RL Nucleic Acids Res. 22:2576-2586(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12;
RX PubMed=12113939; DOI=10.1111/j.1574-6968.2002.tb11271.x;
RA Hara H., Narita S., Karibian D., Park J.T., Yamamoto Y., Nishimura Y.;
RT "Identification and characterization of the Escherichia coli envC gene
RT encoding a periplasmic coiled-coil protein with putative peptidase
RT activity.";
RL FEMS Microbiol. Lett. 212:229-236(2002).
RN [5]
RP FUNCTION AS A PROTEASE, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=11976287; DOI=10.1128/jb.184.10.2595-2602.2002;
RA Ichimura T., Yamazoe M., Maeda M., Wada C., Hiraga S.;
RT "Proteolytic activity of YibP protein in Escherichia coli.";
RL J. Bacteriol. 184:2595-2602(2002).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12;
RX PubMed=15165230; DOI=10.1111/j.1365-2958.2004.04063.x;
RA Bernhardt T.G., de Boer P.A.;
RT "Screening for synthetic lethal mutants in Escherichia coli and
RT identification of EnvC (YibP) as a periplasmic septal ring factor with
RT murein hydrolase activity.";
RL Mol. Microbiol. 52:1255-1269(2004).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MG1655 / TB28;
RX PubMed=19525345; DOI=10.1128/jb.00505-09;
RA Uehara T., Dinh T., Bernhardt T.G.;
RT "LytM-domain factors are required for daughter cell separation and rapid
RT ampicillin-induced lysis in Escherichia coli.";
RL J. Bacteriol. 191:5094-5107(2009).
RN [8]
RP FUNCTION AS AN ACTIVATOR, AND DOMAIN.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=20300061; DOI=10.1038/emboj.2010.36;
RA Uehara T., Parzych K.R., Dinh T., Bernhardt T.G.;
RT "Daughter cell separation is controlled by cytokinetic ring-activated cell
RT wall hydrolysis.";
RL EMBO J. 29:1412-1422(2010).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.57 ANGSTROMS) OF 278-419, FUNCTION, AND
RP MUTAGENESIS OF LYS-321; VAL-324; TYR-350; VAL-353; TYR-366; TYR-401 AND
RP ARG-405.
RC STRAIN=K12 / MG1655 / TB28;
RX PubMed=23796240; DOI=10.1111/mmi.12304;
RA Peters N.T., Morlot C., Yang D.C., Uehara T., Vernet T., Bernhardt T.G.;
RT "Structure-function analysis of the LytM domain of EnvC, an activator of
RT cell wall remodelling at the Escherichia coli division site.";
RL Mol. Microbiol. 89:690-701(2013).
CC -!- FUNCTION: Activator of the cell wall hydrolases AmiA and AmiB. Required
CC for septal murein cleavage and daughter cell separation during cell
CC division. In vitro, exhibits weak endoproteolytic activity on beta-
CC casein. {ECO:0000269|PubMed:11976287, ECO:0000269|PubMed:15165230,
CC ECO:0000269|PubMed:19525345, ECO:0000269|PubMed:20300061,
CC ECO:0000269|PubMed:23796240}.
CC -!- INTERACTION:
CC P37690; P0AC30: ftsX; NbExp=2; IntAct=EBI-15948725, EBI-1119111;
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:12113939,
CC ECO:0000269|PubMed:15165230, ECO:0000269|PubMed:19525345}.
CC Note=Localizes at the septal ring.
CC -!- DOMAIN: The coiled-coil domain is necessary and sufficient for
CC recruitment to the divisome. The LytM domain is required for proper
CC septal peptidoglycan splitting. {ECO:0000269|PubMed:20300061}.
CC -!- DISRUPTION PHENOTYPE: Mutants show defects in septation and separation,
CC and form very long filaments (1.5-fold increase). The phenotype is
CC exacerbated when combined with nlpD (over 8-fold longer), more
CC exacerbated with a triple mepM (yebA) or ygeR disruption (15-fold
CC longer) and further yet by the quadruple disruption mutant (envC-nlpD-
CC mepM(yebA)-ygeR, over 21-fold longer). Quadruple mutants are less
CC sensitive to ampicillin lysis. {ECO:0000269|PubMed:11976287,
CC ECO:0000269|PubMed:12113939, ECO:0000269|PubMed:15165230,
CC ECO:0000269|PubMed:19525345}.
CC -!- SIMILARITY: Belongs to the peptidase M23B family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to have murein hydrolase activity.
CC {ECO:0000305|PubMed:15165230}.
CC -!- CAUTION: Unlike many members of this family does not have peptidase
CC activity. {ECO:0000305|PubMed:23796240}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB18590.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U00039; AAB18590.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC76637.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE77679.1; -; Genomic_DNA.
DR RefSeq; NP_418070.6; NC_000913.3.
DR PDB; 4BH5; X-ray; 1.57 A; A/B/C/D=278-419.
DR PDB; 6TPI; X-ray; 2.10 A; A=35-419.
DR PDBsum; 4BH5; -.
DR PDBsum; 6TPI; -.
DR AlphaFoldDB; P37690; -.
DR SMR; P37690; -.
DR BioGRID; 4263303; 372.
DR DIP; DIP-12426N; -.
DR IntAct; P37690; 1.
DR STRING; 511145.b3613; -.
DR MEROPS; M23.950; -.
DR jPOST; P37690; -.
DR PaxDb; P37690; -.
DR PRIDE; P37690; -.
DR DNASU; 948129; -.
DR EnsemblBacteria; AAC76637; AAC76637; b3613.
DR EnsemblBacteria; BAE77679; BAE77679; BAE77679.
DR GeneID; 948129; -.
DR KEGG; ecj:JW5646; -.
DR KEGG; eco:b3613; -.
DR PATRIC; fig|1411691.4.peg.3093; -.
DR EchoBASE; EB2205; -.
DR eggNOG; COG4942; Bacteria.
DR HOGENOM; CLU_029425_4_0_6; -.
DR InParanoid; P37690; -.
DR OMA; SDPAQWC; -.
DR PhylomeDB; P37690; -.
DR BioCyc; EcoCyc:EG12297-MON; -.
DR BioCyc; MetaCyc:EG12297-MON; -.
DR PRO; PR:P37690; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0032153; C:cell division site; IDA:EcoliWiki.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:0042597; C:periplasmic space; IDA:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0016787; F:hydrolase activity; IDA:EcoliWiki.
DR GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0009273; P:peptidoglycan-based cell wall biogenesis; IMP:EcoCyc.
DR GO; GO:0051345; P:positive regulation of hydrolase activity; IDA:EcoCyc.
DR GO; GO:0009314; P:response to radiation; IMP:EcoCyc.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IMP:EcoCyc.
DR GO; GO:0000920; P:septum digestion after cytokinesis; IMP:EcoliWiki.
DR Gene3D; 2.70.70.10; -; 1.
DR InterPro; IPR011055; Dup_hybrid_motif.
DR InterPro; IPR016047; Peptidase_M23.
DR Pfam; PF01551; Peptidase_M23; 1.
DR SUPFAM; SSF51261; SSF51261; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Coiled coil; Periplasm;
KW Reference proteome; Signal.
FT SIGNAL 1..34
FT /evidence="ECO:0000255"
FT CHAIN 35..419
FT /note="Murein hydrolase activator EnvC"
FT /id="PRO_0000169611"
FT REGION 252..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 35..124
FT /evidence="ECO:0000255"
FT COILED 155..271
FT /evidence="ECO:0000255"
FT COMPBIAS 252..277
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 321
FT /note="K->A: Retains AmiA and AmiB activation."
FT /evidence="ECO:0000269|PubMed:23796240"
FT MUTAGEN 321
FT /note="K->E: Loss of AmiA and AmiB activation; does not
FT complement double envC-nlpD disruption, protein localizes
FT normally."
FT /evidence="ECO:0000269|PubMed:23796240"
FT MUTAGEN 324
FT /note="V->A: Retains AmiA and AmiB activation."
FT /evidence="ECO:0000269|PubMed:23796240"
FT MUTAGEN 324
FT /note="V->E: Loss of AmiA and AmiB activation; does not
FT complement double envC-nlpD disruption, protein localizes
FT normally."
FT /evidence="ECO:0000269|PubMed:23796240"
FT MUTAGEN 350
FT /note="Y->A: Loss of AmiA and AmiB activation; does not
FT complement double envC-nlpD disruption, protein localizes
FT normally."
FT /evidence="ECO:0000269|PubMed:23796240"
FT MUTAGEN 353
FT /note="V->A: Loss of AmiA and AmiB activation; does not
FT complement double envC-nlpD disruption, protein localizes
FT normally."
FT /evidence="ECO:0000269|PubMed:23796240"
FT MUTAGEN 366
FT /note="Y->H: Partially unstable, loss of AmiA and AmiB
FT activation."
FT /evidence="ECO:0000269|PubMed:23796240"
FT MUTAGEN 401
FT /note="Y->E: Partially unstable, loss of AmiA and AmiB
FT activation; does not complement double envC-nlpD
FT disruption, protein localizes normally."
FT /evidence="ECO:0000269|PubMed:23796240"
FT MUTAGEN 405
FT /note="R->H: Loss of activation of amidases; does not
FT complement double envC-nlpD disruption, protein localizes
FT normally."
FT /evidence="ECO:0000269|PubMed:23796240"
FT HELIX 41..126
FT /evidence="ECO:0007829|PDB:6TPI"
FT TURN 127..131
FT /evidence="ECO:0007829|PDB:6TPI"
FT HELIX 135..138
FT /evidence="ECO:0007829|PDB:6TPI"
FT HELIX 144..217
FT /evidence="ECO:0007829|PDB:6TPI"
FT HELIX 222..264
FT /evidence="ECO:0007829|PDB:6TPI"
FT HELIX 266..269
FT /evidence="ECO:0007829|PDB:6TPI"
FT TURN 270..272
FT /evidence="ECO:0007829|PDB:6TPI"
FT HELIX 279..288
FT /evidence="ECO:0007829|PDB:6TPI"
FT STRAND 293..296
FT /evidence="ECO:0007829|PDB:4BH5"
FT STRAND 306..308
FT /evidence="ECO:0007829|PDB:4BH5"
FT STRAND 312..315
FT /evidence="ECO:0007829|PDB:4BH5"
FT STRAND 321..326
FT /evidence="ECO:0007829|PDB:4BH5"
FT STRAND 332..334
FT /evidence="ECO:0007829|PDB:4BH5"
FT STRAND 336..346
FT /evidence="ECO:0007829|PDB:4BH5"
FT STRAND 350..359
FT /evidence="ECO:0007829|PDB:4BH5"
FT STRAND 362..374
FT /evidence="ECO:0007829|PDB:4BH5"
FT STRAND 385..390
FT /evidence="ECO:0007829|PDB:4BH5"
FT TURN 392..394
FT /evidence="ECO:0007829|PDB:6TPI"
FT STRAND 399..406
FT /evidence="ECO:0007829|PDB:4BH5"
FT STRAND 409..411
FT /evidence="ECO:0007829|PDB:4BH5"
FT HELIX 414..416
FT /evidence="ECO:0007829|PDB:4BH5"
SQ SEQUENCE 419 AA; 46595 MW; 4C786105C2F95BD5 CRC64;
MTRAVKPRRF AIRPIIYASV LSAGVLLCAF SAHADERDQL KSIQADIAAK ERAVRQKQQQ
RASLLAQLKK QEEAISEATR KLRETQNTLN QLNKQIDEMN ASIAKLEQQK AAQERSLAAQ
LDAAFRQGEH TGIQLILSGE ESQRGQRLQA YFGYLNQARQ ETIAQLKQTR EEVAMQRAEL
EEKQSEQQTL LYEQRAQQAK LTQALNERKK TLAGLESSIQ QGQQQLSELR ANESRLRNSI
ARAEAAAKAR AEREAREAQA VRDRQKEATR KGTTYKPTES EKSLMSRTGG LGAPRGQAFW
PVRGPTLHRY GEQLQGELRW KGMVIGASEG TEVKAIADGR VILADWLQGY GLVVVVEHGK
GDMSLYGYNQ SALVSVGSQV RAGQPIALVG SSGGQGRPSL YFEIRRQGQA VNPQPWLGR
