ID   MRED_ECOL6              Reviewed;         162 AA.
AC   P0ABH5; P16927;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Rod shape-determining protein MreD;
GN   Name=mreD; OrderedLocusNames=c4003;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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; AE014075; AAN82443.1; -; Genomic_DNA.
DR   RefSeq; WP_000179409.1; NC_004431.1.
DR   AlphaFoldDB; P0ABH5; -.
DR   SMR; P0ABH5; -.
DR   STRING; 199310.c4003; -.
DR   EnsemblBacteria; AAN82443; AAN82443; c4003.
DR   GeneID; 66672856; -.
DR   KEGG; ecc:c4003; -.
DR   eggNOG; COG2891; Bacteria.
DR   HOGENOM; CLU_119315_0_1_6; -.
DR   OMA; YWAMALP; -.
DR   BioCyc; ECOL199310:C4003-MON; -.
DR   Proteomes; UP000001410; 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; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..162
FT                   /note="Rod shape-determining protein MreD"
FT                   /id="PRO_0000062772"
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