ID E1SFN2_PANVC Unreviewed; 162 AA.
AC E1SFN2;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=Rod shape-determining protein MreD {ECO:0000256|PIRNR:PIRNR018472};
GN Name=mreD {ECO:0000313|EMBL:ADO10978.1};
GN OrderedLocusNames=Pvag_2822 {ECO:0000313|EMBL:ADO10978.1};
OS Pantoea vagans (strain C9-1) (Pantoea agglomerans (strain C9-1)).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Pantoea.
OX NCBI_TaxID=712898 {ECO:0000313|EMBL:ADO10978.1, ECO:0000313|Proteomes:UP000006631};
RN [1] {ECO:0000313|EMBL:ADO10978.1, ECO:0000313|Proteomes:UP000006631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C9-1 {ECO:0000313|EMBL:ADO10978.1,
RC ECO:0000313|Proteomes:UP000006631};
RX PubMed=20952567; DOI=10.1128/JB.01122-10;
RA Smits T.H., Rezzonico F., Kamber T., Goesmann A., Ishimaru C.A.,
RA Stockwell V.O., Frey J.E., Duffy B.;
RT "The genome sequence of the biocontrol agent Pantoea vagans strain C9-1.";
RL J. Bacteriol. 192:6486-6487(2010).
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; CP002206; ADO10978.1; -; Genomic_DNA.
DR RefSeq; WP_013359205.1; NC_014562.1.
DR AlphaFoldDB; E1SFN2; -.
DR GeneID; 58736664; -.
DR KEGG; pva:Pvag_2822; -.
DR eggNOG; COG2891; Bacteria.
DR HOGENOM; CLU_119315_0_1_6; -.
DR OrthoDB; 6647425at2; -.
DR Proteomes; UP000006631; Chromosome.
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 6..25
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 37..54
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..128
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 134..152
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 162 AA; 18982 MW; 1E8F39C77DB38717 CRC64;
MSRYRSQGRW VIWLSFLVAL VLQIMPWPDE IYMFRPSWLL LILIYWVLAL PHRVNVGSGF
MLGAIMDLIA GSTLGVRALA LSIIAYLIAF KFQLFRNLAL WQQALMVMVL SLAMDVIVFW
AEFLVINVSF RPEIFWSSVV DGILWPWLFL LMRKIRRQFA VQ
//