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Database: UniProt
Entry: E1SFN2_PANVC
LinkDB: E1SFN2_PANVC
Original site: E1SFN2_PANVC 
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
//
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