ID   MREC_CERSP              Reviewed;         300 AA.
AC   Q70AN6;
DT   11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 47.
DE   RecName: Full=Cell shape-determining protein MreC {ECO:0000250|UniProtKB:P16926};
DE   AltName: Full=Cell shape protein MreC {ECO:0000250|UniProtKB:P16926};
DE   AltName: Full=Rod shape-determining protein MreC {ECO:0000250|UniProtKB:P16926};
GN   Name=mreC {ECO:0000312|EMBL:CAE53833.1};
OS   Cereibacter sphaeroides (Rhodobacter sphaeroides).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Cereibacter.
OX   NCBI_TaxID=1063;
RN   [1] {ECO:0000312|EMBL:CAE53833.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=WS8N {ECO:0000312|EMBL:CAE53833.1};
RX   PubMed=15601688; DOI=10.1128/jb.187.1.54-64.2005;
RA   Slovak P.M., Wadhams G.H., Armitage J.P.;
RT   "Localization of MreB in Rhodobacter sphaeroides under conditions causing
RT   changes in cell shape and membrane structure.";
RL   J. Bacteriol. 187:54-64(2005).
RN   [2] {ECO:0000305}
RP   SUBCELLULAR LOCATION.
RC   STRAIN=WS8N;
RX   PubMed=16484180; DOI=10.1128/jb.188.5.1691-1700.2006;
RA   Slovak P.M., Porter S.L., Armitage J.P.;
RT   "Differential localization of Mre proteins with PBP2 in Rhodobacter
RT   sphaeroides.";
RL   J. Bacteriol. 188:1691-1700(2006).
CC   -!- FUNCTION: Involved in formation and maintenance of cell shape.
CC       {ECO:0000250|UniProtKB:P16926}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000305|PubMed:16484180}; Single-pass membrane protein
CC       {ECO:0000305|PubMed:16484180}. Note=Colocalizes with penicillin-binding
CC       protein PBP2 throughout the cell cycle. In newly formed and elongating
CC       cells, the foci form bands across the cell, which are predominately
CC       located at or near midcell. In cells undergoing septation, the foci are
CC       not observed at the site of septation but are positioned close to the
CC       midcell of the nascent or forming daughter cells.
CC   -!- SIMILARITY: Belongs to the MreC family. {ECO:0000305}.
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DR   EMBL; AJ605582; CAE53833.1; -; Genomic_RNA.
DR   RefSeq; WP_002719491.1; NZ_WTFI01000014.1.
DR   AlphaFoldDB; Q70AN6; -.
DR   SMR; Q70AN6; -.
DR   OrthoDB; 837894at2; -.
DR   GO; GO:0009276; C:Gram-negative-bacterium-type cell wall; IDA:UniProtKB.
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   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   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Cell shape; Coiled coil; Membrane;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..300
FT                   /note="Cell shape-determining protein MreC"
FT                   /id="PRO_0000418059"
FT   TOPO_DOM        1..17
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P16926, ECO:0000255"
FT   TRANSMEM        18..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P16926, ECO:0000255"
FT   TOPO_DOM        39..300
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P16926, ECO:0000255"
FT   REGION          277..300
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          74..117
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   300 AA;  33103 MW;  54D3346F981D0839 CRC64;
     MARDRTRPED FTRPLRRILV GGLVLLLLGI FLIWRIDSPR VEQFRAALID RVVPSFEWLM
     TPMTKVAGMV ENFQSYTRIY EQNQELRREL QQMKAWKEAA LQLEQKNARL LDLNQVRLDP
     KLTHVTGVVL ADSGSPFRQS VLLNVGARDG IRDGWATMDG IGLVGRISGV GRTTSRVILL
     TDTSSRIPVT VQPSGQRALL TGDNSPSPPL EFLDKPDLVR PGDRVVTSGD GGVFPADLLV
     GQVAQGPDRR LRVRLAADYG RLEFLRVLRS HELEPISDPG KLVAEPPAPP APAAVEGADG