MRED_ECOLI
ID MRED_ECOLI Reviewed; 162 AA.
AC P0ABH4; P16927; Q2M8W5;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Rod shape-determining protein MreD;
GN Name=mreD; OrderedLocusNames=b3249, JW3218;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
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 153-162.
RC STRAIN=K12;
RX PubMed=1937035; DOI=10.1016/0378-1119(91)90578-y;
RA Wachi M., Doi M., Ueda T., Ueki M., Tsuritani K., Nagai K., Matsuhashi M.;
RT "Sequence of the downstream flanking region of the shape-determining genes
RT mreBCD of Escherichia coli.";
RL Gene 106:135-136(1991).
RN [5]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
CC -!- FUNCTION: Involved in formation of the rod shape of the cell. May also
CC contribute to regulation of formation of penicillin-binding proteins.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the MreD family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M31792; AAA24156.1; -; Genomic_DNA.
DR EMBL; U18997; AAA58052.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76281.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77291.1; -; Genomic_DNA.
DR EMBL; X57166; CAA40455.1; -; Genomic_DNA.
DR PIR; JV0060; JV0060.
DR RefSeq; NP_417715.1; NC_000913.3.
DR RefSeq; WP_000179409.1; NZ_STEB01000012.1.
DR AlphaFoldDB; P0ABH4; -.
DR SMR; P0ABH4; -.
DR BioGRID; 4262449; 394.
DR ComplexPortal; CPX-5718; Elongasome complex.
DR DIP; DIP-10257N; -.
DR STRING; 511145.b3249; -.
DR TCDB; 9.B.157.1.3; the cell shape-determining mrebcd (mrebcd) family.
DR PaxDb; P0ABH4; -.
DR PRIDE; P0ABH4; -.
DR EnsemblBacteria; AAC76281; AAC76281; b3249.
DR EnsemblBacteria; BAE77291; BAE77291; BAE77291.
DR GeneID; 66672856; -.
DR GeneID; 947756; -.
DR KEGG; ecj:JW3218; -.
DR KEGG; eco:b3249; -.
DR PATRIC; fig|1411691.4.peg.3480; -.
DR EchoBASE; EB0605; -.
DR eggNOG; COG2891; Bacteria.
DR HOGENOM; CLU_119315_0_1_6; -.
DR InParanoid; P0ABH4; -.
DR OMA; YWAMALP; -.
DR PhylomeDB; P0ABH4; -.
DR BioCyc; EcoCyc:EG10610-MON; -.
DR PRO; PR:P0ABH4; -.
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:EcoCyc.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IC:ComplexPortal.
DR GO; GO:0008360; P:regulation of cell shape; IMP:EcoCyc.
DR InterPro; IPR007227; Cell_shape_determining_MreD.
DR InterPro; IPR026034; MreD_proteobac.
DR PANTHER; PTHR37484; PTHR37484; 1.
DR Pfam; PF04093; MreD; 1.
DR PIRSF; PIRSF018472; MreD_proteobac; 1.
DR TIGRFAMs; TIGR03426; shape_MreD; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Cell shape; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..162
FT /note="Rod shape-determining protein MreD"
FT /id="PRO_0000062770"
FT TOPO_DOM 1..9
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 31..51
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 52..55
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 56..76
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 77..105
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 106..126
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 127..131
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 153..162
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 162 AA; 18788 MW; 4D9DEAE3F38F99C8 CRC64;
MASYRSQGRW VIWLSFLIAL LLQIMPWPDN LIVFRPNWVL LILLYWILAL PHRVNVGTGF
VMGAILDLIS GSTLGVRVLA MSIIAYLVAL KYQLFRNLAL WQQALVVMLL SLVVDIIVFW
AEFLVINVSF RPEVFWSSVV NGVLWPWIFL LMRKVRQQFA VQ
