ID   A0A1H9BXH9_9GAMM        Unreviewed;       163 AA.
AC   A0A1H9BXH9;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=Rod shape-determining protein MreD {ECO:0000256|PIRNR:PIRNR018472};
GN   ORFNames=SAMN04488038_102270 {ECO:0000313|EMBL:SEP93696.1};
OS   Solimonas aquatica.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Nevskiales; Nevskiaceae;
OC   Solimonas.
OX   NCBI_TaxID=489703 {ECO:0000313|EMBL:SEP93696.1, ECO:0000313|Proteomes:UP000199233};
RN   [1] {ECO:0000313|EMBL:SEP93696.1, ECO:0000313|Proteomes:UP000199233}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 25927 {ECO:0000313|EMBL:SEP93696.1,
RC   ECO:0000313|Proteomes:UP000199233};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; FOFS01000002; SEP93696.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H9BXH9; -.
DR   STRING; 489703.SAMN04488038_102270; -.
DR   OrthoDB; 6647425at2; -.
DR   Proteomes; UP000199233; 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   Reference proteome {ECO:0000313|Proteomes:UP000199233};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        54..72
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        79..98
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        104..122
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   163 AA;  18506 MW;  A13C0CDD964344CA CRC64;
     MSRPSTRATW TAYLLSLLLG LVLQIVQLPE SLAAARPLLP AMLLAYWALR EPQLPMLLPA
     FLIGLLMDVL LGTPMGQHAI GLLVLIYLVV SLRSFFIVFP LWQATLALIP AWVIYCFLMY
     WIDGATHHTA DRWLRWLPAL STSLSWPLLW SVMELIRQPG EEE
//