MREC_ECOLI
ID MREC_ECOLI Reviewed; 367 AA.
AC P16926; P13028; Q2M8W4;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Cell shape-determining protein MreC;
DE AltName: Full=Cell shape protein MreC;
DE AltName: Full=Rod shape-determining protein MreC;
GN Name=mreC; OrderedLocusNames=b3250, JW3219;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=K12 / JM109 / ATCC 53323;
RX PubMed=2687239; DOI=10.1128/jb.171.12.6511-6516.1989;
RA Wachi M., Doi M., Okada Y., Matsuhashi M.;
RT "New mre genes mreC and mreD, responsible for formation of the rod shape of
RT Escherichia coli cells.";
RL J. Bacteriol. 171:6511-6516(1989).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-128.
RC STRAIN=K12 / JM109 / ATCC 53323;
RX PubMed=3049542; DOI=10.1128/jb.170.10.4619-4624.1988;
RA Doi M., Wachi M., Ishino F., Tomioka S., Ito M., Sakagami Y., Suzuki A.,
RA Matsuhashi M.;
RT "Determinations of the DNA sequence of the mreB gene and of the gene
RT products of the mre region that function in formation of the rod shape of
RT Escherichia coli cells.";
RL J. Bacteriol. 170:4619-4624(1988).
RN [5]
RP FUNCTION, SELF-ASSOCIATION, INTERACTION WITH MREB AND MRED, SUBCELLULAR
RP LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=15612918; DOI=10.1111/j.1365-2958.2004.04367.x;
RA Kruse T., Bork-Jensen J., Gerdes K.;
RT "The morphogenetic MreBCD proteins of Escherichia coli form an essential
RT membrane-bound complex.";
RL Mol. Microbiol. 55:78-89(2005).
CC -!- FUNCTION: Involved in formation and maintenance of cell shape.
CC Responsible for formation of rod shape. May also contribute to
CC regulation of formation of penicillin-binding proteins.
CC {ECO:0000269|PubMed:15612918, ECO:0000269|PubMed:2687239}.
CC -!- SUBUNIT: Self-associates. Interacts with MreB and MreD.
CC {ECO:0000269|PubMed:15612918}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:15612918}; Single-pass membrane protein
CC {ECO:0000269|PubMed:15612918}.
CC -!- DISRUPTION PHENOTYPE: Reduction in growth rate and ultimately cell
CC lysis. Growth arrest is associated with remarkable change in cell
CC morphology from the normal rod-shape to enlarged, spherical cells. Many
CC of the large spherical cells lyse at a later stage.
CC {ECO:0000269|PubMed:15612918}.
CC -!- SIMILARITY: Belongs to the MreC family. {ECO:0000305}.
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DR EMBL; M31792; AAA24155.1; -; Genomic_DNA.
DR EMBL; U18997; AAA58053.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76282.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77292.1; -; Genomic_DNA.
DR EMBL; M22055; AAA83892.1; -; Genomic_DNA.
DR PIR; JV0059; JV0059.
DR RefSeq; NP_417716.1; NC_000913.3.
DR RefSeq; WP_000802511.1; NZ_SSZK01000034.1.
DR AlphaFoldDB; P16926; -.
DR SMR; P16926; -.
DR BioGRID; 4261941; 266.
DR ComplexPortal; CPX-5718; Elongasome complex.
DR DIP; DIP-10256N; -.
DR IntAct; P16926; 5.
DR MINT; P16926; -.
DR STRING; 511145.b3250; -.
DR ChEMBL; CHEMBL3309012; -.
DR TCDB; 9.B.157.1.3; the cell shape-determining mrebcd (mrebcd) family.
DR jPOST; P16926; -.
DR PaxDb; P16926; -.
DR PRIDE; P16926; -.
DR EnsemblBacteria; AAC76282; AAC76282; b3250.
DR EnsemblBacteria; BAE77292; BAE77292; BAE77292.
DR GeneID; 947655; -.
DR KEGG; ecj:JW3219; -.
DR KEGG; eco:b3250; -.
DR PATRIC; fig|1411691.4.peg.3479; -.
DR EchoBASE; EB0604; -.
DR eggNOG; COG1792; Bacteria.
DR HOGENOM; CLU_042663_2_0_6; -.
DR InParanoid; P16926; -.
DR OMA; NPFTHRI; -.
DR PhylomeDB; P16926; -.
DR BioCyc; EcoCyc:EG10609-MON; -.
DR PRO; PR:P16926; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; ISM:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0043621; F:protein self-association; IPI:UniProtKB.
DR GO; GO:0071963; P:establishment or maintenance of cell polarity regulating cell shape; IMP:UniProtKB.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IC:ComplexPortal.
DR GO; GO:0008360; P:regulation of cell shape; IMP:EcoCyc.
DR Gene3D; 2.40.10.340; -; 1.
DR Gene3D; 2.40.10.350; -; 1.
DR InterPro; IPR042177; Cell/Rod_1.
DR InterPro; IPR042175; Cell/Rod_MreC_2.
DR InterPro; IPR007221; MreC.
DR PANTHER; PTHR34138; PTHR34138; 1.
DR Pfam; PF04085; MreC; 1.
DR TIGRFAMs; TIGR00219; mreC; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Cell shape; Coiled coil; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..367
FT /note="Cell shape-determining protein MreC"
FT /id="PRO_0000062767"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 13..35
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 36..367
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT REGION 300..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 63..92
FT /evidence="ECO:0000255"
FT COMPBIAS 318..352
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 367 AA; 39530 MW; 1BAA7C5EF9E84C92 CRC64;
MKPIFSRGPS LQIRLILAVL VALGIIIADS RLGTFSQIRT YMDTAVSPFY FVSNAPRELL
DGVSQTLASR DQLELENRAL RQELLLKNSE LLMLGQYKQE NARLRELLGS PLRQDEQKMV
TQVISTVNDP YSDQVVIDKG SVNGVYEGQP VISDKGVVGQ VVAVAKLTSR VLLICDATHA
LPIQVLRNDI RVIAAGNGCT DDLQLEHLPA NTDIRVGDVL VTSGLGGRFP EGYPVAVVSS
VKLDTQRAYT VIQARPTAGL QRLRYLLLLW GADRNGANPM TPEEVHRVAN ERLMQMMPQV
LPSPDAMGPK LPEPATGIAQ PTPQQPATGN AATAPAAPTQ PAANRSPQRA TPPQSGAQPP
ARAPGGQ
