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Database: UniProt
Entry: A0A0F5ZWA3_9GAMM
LinkDB: A0A0F5ZWA3_9GAMM
Original site: A0A0F5ZWA3_9GAMM 
ID   A0A0F5ZWA3_9GAMM        Unreviewed;       162 AA.
AC   A0A0F5ZWA3;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Rod shape-determining protein MreD {ECO:0000256|PIRNR:PIRNR018472};
GN   ORFNames=RN22_12910 {ECO:0000313|EMBL:KKD60031.1};
OS   Grimontia sp. AD028.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Grimontia.
OX   NCBI_TaxID=1581149 {ECO:0000313|EMBL:KKD60031.1, ECO:0000313|Proteomes:UP000033732};
RN   [1] {ECO:0000313|EMBL:KKD60031.1, ECO:0000313|Proteomes:UP000033732}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AD028 {ECO:0000313|EMBL:KKD60031.1,
RC   ECO:0000313|Proteomes:UP000033732};
RA   Adrian T.-G.-S., Chan K.-G.;
RT   "Genome sequencing of Grimontia sp. AD028.";
RL   Submitted (APR-2015) 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:KKD60031.1}.
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DR   EMBL; LASY01000055; KKD60031.1; -; Genomic_DNA.
DR   RefSeq; WP_039849728.1; NZ_LASY01000055.1.
DR   AlphaFoldDB; A0A0F5ZWA3; -.
DR   PATRIC; fig|1581149.3.peg.3389; -.
DR   OrthoDB; 6647425at2; -.
DR   Proteomes; UP000033732; 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        74..92
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        133..152
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   162 AA;  18511 MW;  E61B0F7ADCE9A817 CRC64;
     MANSSMRGRA LIWLSFIIAL ILQAAPWPGE LAPFRPSWVL LVAFYWVLAL PHRVNVGTAL
     VVGLLWDLML GSTLGVRGLM MSVLVYIVAL NFQMLRNMSL WQQAALLSLL TLAGKVLEFW
     AEYLVSNVQF DPAQLWAGLL NFLLWPWLFL LLRRVRRQFS IK
//
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