ID G2DVM1_9GAMM Unreviewed; 163 AA.
AC G2DVM1;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=Rod shape-determining protein MreD {ECO:0000256|PIRNR:PIRNR018472};
GN ORFNames=ThidrDRAFT_0191 {ECO:0000313|EMBL:EGV34036.1};
OS Thiorhodococcus drewsii AZ1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Thiorhodococcus.
OX NCBI_TaxID=765913 {ECO:0000313|EMBL:EGV34036.1, ECO:0000313|Proteomes:UP000004200};
RN [1] {ECO:0000313|EMBL:EGV34036.1, ECO:0000313|Proteomes:UP000004200}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AZ1 {ECO:0000313|EMBL:EGV34036.1,
RC ECO:0000313|Proteomes:UP000004200};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Land M.L., Hauser L., Vogl K., Liu Z., Imhoff J., Thiel V.,
RA Frigaard N.-U., Bryant D.A., Woyke T.J.;
RT "The draft genome of Thiorhodococcus drewsii AZ1.";
RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
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 {ECO:0000256|PIRNR:PIRNR018472}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|PIRNR:PIRNR018472}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the MreD family. {ECO:0000256|ARBA:ARBA00007776,
CC ECO:0000256|PIRNR:PIRNR018472}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGV34036.1}.
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DR EMBL; AFWT01000001; EGV34036.1; -; Genomic_DNA.
DR RefSeq; WP_007038907.1; NZ_AFWT01000001.1.
DR AlphaFoldDB; G2DVM1; -.
DR STRING; 765913.ThidrDRAFT_0191; -.
DR eggNOG; COG2891; Bacteria.
DR Proteomes; UP000004200; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-UniRule.
DR InterPro; IPR007227; Cell_shape_determining_MreD.
DR InterPro; IPR026034; MreD_proteobac.
DR NCBIfam; TIGR03426; shape_MreD; 1.
DR PANTHER; PTHR37484; ROD SHAPE-DETERMINING PROTEIN MRED; 1.
DR PANTHER; PTHR37484:SF1; ROD SHAPE-DETERMINING PROTEIN MRED; 1.
DR Pfam; PF04093; MreD; 1.
DR PIRSF; PIRSF018472; MreD_proteobac; 1.
PE 3: Inferred from homology;
KW Cell inner membrane {ECO:0000256|PIRNR:PIRNR018472};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW ECO:0000256|PIRNR:PIRNR018472};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|PIRNR:PIRNR018472};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR018472};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 35..50
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 106..127
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 133..153
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 163 AA; 18462 MW; 042F1E00473F1B99 CRC64;
MKRARRPLRL WPVVLSLVLA MLLTILPLPE SIGDYRPQWV TLAIIFWCLA MPQRIGVFWA
FFAGLTLDVL TGSLLGEHAL GLSVVAYLTG MLRSGILLFP LWQQAFFIWV LLLVERLLSL
WVIGATGQPM PPLSYWSATF GSLLVWPWLF LVLRITGRRI GSD
//