ID W0LBN5_9GAMM Unreviewed; 162 AA.
AC W0LBN5;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=Rod shape-determining protein MreD {ECO:0000256|PIRNR:PIRNR018472};
GN ORFNames=Z042_09370 {ECO:0000313|EMBL:AHG19809.1};
OS Chania multitudinisentens RB-25.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Chania.
OX NCBI_TaxID=1441930 {ECO:0000313|EMBL:AHG19809.1, ECO:0000313|Proteomes:UP000019030};
RN [1] {ECO:0000313|EMBL:AHG19809.1, ECO:0000313|Proteomes:UP000019030}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RB-25 {ECO:0000313|EMBL:AHG19809.1,
RC ECO:0000313|Proteomes:UP000019030};
RA Robson E.H.J.;
RT "Isolation of Serratia multitudinisentens RB-25 from Ex-Landfill site.";
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AHG19809.1, ECO:0000313|Proteomes:UP000019030}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RB-25 {ECO:0000313|EMBL:AHG19809.1,
RC ECO:0000313|Proteomes:UP000019030};
RA Chan K.-G.;
RL Submitted (MAR-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}.
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DR EMBL; CP007044; AHG19809.1; -; Genomic_DNA.
DR RefSeq; WP_024913299.1; NZ_JAJC01000024.1.
DR AlphaFoldDB; W0LBN5; -.
DR STRING; 1441930.Z042_09370; -.
DR KEGG; sfo:Z042_09370; -.
DR PATRIC; fig|1441930.4.peg.1870; -.
DR eggNOG; COG2891; Bacteria.
DR HOGENOM; CLU_119315_0_1_6; -.
DR OrthoDB; 6647425at2; -.
DR Proteomes; UP000019030; 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 Reference proteome {ECO:0000313|Proteomes:UP000019030};
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 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; 19013 MW; 4CFD7548FF9CFE04 CRC64;
MNRYRSNGRW IIWLSFLVAL VLQIMPWPEQ IYMFRPSWLL LILTYWVMAL PHRVNVGTGF
VLGLVMDLVF GSTLGVRALA MGIIAYLVAF KFQLFRNMAL WQQALIVVLL SLAMDVVVFW
AEFLVINVSF RPEVFWSSVV NGVLWPWLFL LMRKIRRQFA VQ
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