ID   MRED_ECO57              Reviewed;         162 AA.
AC   P0ABH6; P16927;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Rod shape-determining protein MreD;
GN   Name=mreD; OrderedLocusNames=Z4607, ECs4121;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
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       (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the MreD family. {ECO:0000305}.
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DR   EMBL; AE005174; AAG58376.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB37544.1; -; Genomic_DNA.
DR   PIR; A91144; A91144.
DR   PIR; D85989; D85989.
DR   RefSeq; NP_312148.1; NC_002695.1.
DR   RefSeq; WP_000179409.1; NZ_SWKA01000005.1.
DR   AlphaFoldDB; P0ABH6; -.
DR   SMR; P0ABH6; -.
DR   STRING; 155864.EDL933_4470; -.
DR   EnsemblBacteria; AAG58376; AAG58376; Z4607.
DR   EnsemblBacteria; BAB37544; BAB37544; ECs_4121.
DR   GeneID; 66672856; -.
DR   GeneID; 916032; -.
DR   KEGG; ece:Z4607; -.
DR   KEGG; ecs:ECs_4121; -.
DR   PATRIC; fig|386585.9.peg.4302; -.
DR   eggNOG; COG2891; Bacteria.
DR   HOGENOM; CLU_119315_0_1_6; -.
DR   OMA; YWAMALP; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
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   3: Inferred from homology;
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_0000062771"
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