(data stored in SCRATCH zone)

SWISSPROT: A8FQP9_SHESH

ID   A8FQP9_SHESH            Unreviewed;       162 AA.
AC   A8FQP9;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   07-JUN-2017, entry version 51.
DE   RecName: Full=Rod shape-determining protein MreD {ECO:0000256|PIRNR:PIRNR018472};
GN   OrderedLocusNames=Ssed_0560 {ECO:0000313|EMBL:ABV35172.1};
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104 {ECO:0000313|EMBL:ABV35172.1, ECO:0000313|Proteomes:UP000002015};
RN   [1] {ECO:0000313|EMBL:ABV35172.1, ECO:0000313|Proteomes:UP000002015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3 {ECO:0000313|EMBL:ABV35172.1,
RC   ECO:0000313|Proteomes:UP000002015};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in formation of the rod shape of the cell. May
CC       also contribute to regulation of formation of penicillin-binding
CC       proteins. {ECO:0000256|PIRNR:PIRNR018472}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000256|PIRNR:PIRNR018472}.
CC   -!- SIMILARITY: Belongs to the MreD family.
CC       {ECO:0000256|PIRNR:PIRNR018472}.
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DR   EMBL; CP000821; ABV35172.1; -; Genomic_DNA.
DR   RefSeq; WP_012140909.1; NC_009831.1.
DR   STRING; 425104.Ssed_0560; -.
DR   EnsemblBacteria; ABV35172; ABV35172; Ssed_0560.
DR   KEGG; sse:Ssed_0560; -.
DR   eggNOG; ENOG4105VQ7; Bacteria.
DR   eggNOG; COG2891; LUCA.
DR   HOGENOM; HOG000266108; -.
DR   KO; K03571; -.
DR   OMA; HRRLLWF; -.
DR   OrthoDB; POG091H05DH; -.
DR   BioCyc; SSED425104:GH7Q-582-MONOMER; -.
DR   Proteomes; UP000002015; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule.
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   Pfam; PF04093; MreD; 1.
DR   PIRSF; PIRSF018472; MreD_proteobac; 1.
DR   TIGRFAMs; TIGR03426; shape_MreD; 1.
PE   3: Inferred from homology;
DR   PRODOM; A8FQP9.
DR   SWISS-2DPAGE; A8FQP9.
KW   Cell inner membrane {ECO:0000256|PIRNR:PIRNR018472};
KW   Cell membrane {ECO:0000256|PIRNR:PIRNR018472};
KW   Cell shape {ECO:0000256|PIRNR:PIRNR018472};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002015};
KW   Membrane {ECO:0000256|PIRNR:PIRNR018472, ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     12     31       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     74     92       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    104    122       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    134    152       Helical. {ECO:0000256|SAM:Phobius}.
SQ   SEQUENCE   162 AA;  19286 MW;  031DA76C0C0685D5 CRC64;
     MSMHIANGRW VVWLSFLVAM LFQIMPLPDL VEPWRPDWLL LVIIYWAMAL PHRYNILSAW
     VLGVLLDIML GAHLGIRALS ISLVVYVVVL HFQRLRNFPM WQQALMISSL ICLYHLVIFW
     VQFVVDTATF DVRLFLPAIS SLIIWPWVFW ILRRVRRLYK VR
//

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