ID A0A1H8VD28_9GAMM Unreviewed; 162 AA.
AC A0A1H8VD28;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=Rod shape-determining protein MreD {ECO:0000256|PIRNR:PIRNR018472};
GN ORFNames=SAMN04488052_11165 {ECO:0000313|EMBL:SEP13124.1};
OS Aquisalimonas asiatica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Aquisalimonas.
OX NCBI_TaxID=406100 {ECO:0000313|EMBL:SEP13124.1, ECO:0000313|Proteomes:UP000199657};
RN [1] {ECO:0000313|EMBL:SEP13124.1, ECO:0000313|Proteomes:UP000199657}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.6291 {ECO:0000313|EMBL:SEP13124.1,
RC ECO:0000313|Proteomes:UP000199657};
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; FOEG01000011; SEP13124.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H8VD28; -.
DR STRING; 406100.SAMN04488052_11165; -.
DR OrthoDB; 6647425at2; -.
DR Proteomes; UP000199657; 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:UP000199657};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..25
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 37..62
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 74..92
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 104..121
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; 18018 MW; 0D41265BB96A0463 CRC64;
MAFAGRQGGG VIFVSIIVAY ALTIMPLPEW AQPARPAWAA LVLIYWCMAV PHRVGVVFAW
LVGLGQDALQ ATLLGQHALA YALMAYLVLH LHQRIRVYPL PQQAAIVLLL LLLVHVVQAW
ISGLVDRPAP GLVYWLPPLV GTLLWPWVFV VMRGVRRRFS VQ
//
