MRED_STRR6
ID MRED_STRR6 Reviewed; 164 AA.
AC Q8DMY3;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Cell shape-determining protein MreD;
GN Name=mreD; OrderedLocusNames=spr2022;
OS Streptococcus pneumoniae (strain ATCC BAA-255 / R6).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=171101;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-255 / R6;
RX PubMed=11544234; DOI=10.1128/jb.183.19.5709-5717.2001;
RA Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S.,
RA DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C.,
RA Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., LeBlanc D.J.,
RA Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., McAhren S.M., McHenney M.,
RA McLeaster K., Mundy C.W., Nicas T.I., Norris F.H., O'Gara M., Peery R.B.,
RA Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y.,
RA Young-Bellido M., Zhao G., Zook C.A., Baltz R.H., Jaskunas S.R.,
RA Rosteck P.R. Jr., Skatrud P.L., Glass J.I.;
RT "Genome of the bacterium Streptococcus pneumoniae strain R6.";
RL J. Bacteriol. 183:5709-5717(2001).
RN [2]
RP SUBUNIT.
RC STRAIN=R6 / R704;
RX PubMed=28710862; DOI=10.1111/mmi.13748;
RA Stamsaas G.A., Straume D., Ruud Winther A., Kjos M., Frantzen C.A.,
RA Haavarstein L.S.;
RT "Identification of EloR (Spr1851) as a regulator of cell elongation in
RT Streptococcus pneumoniae.";
RL Mol. Microbiol. 105:954-967(2017).
CC -!- FUNCTION: Involved in formation and maintenance of cell shape, probably
CC part of the elongasome which synthesizes peripheral peptidogylcan (PG).
CC {ECO:0000305|PubMed:28710862}.
CC -!- SUBUNIT: Interacts with MreC in the elongasome; interaction requires
CC the 90 C-terminal residues of MreC. {ECO:0000269|PubMed:28710862}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the MreD family. {ECO:0000305}.
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DR EMBL; AE007317; AAL00824.1; -; Genomic_DNA.
DR PIR; C98124; C98124.
DR PIR; H95258; H95258.
DR RefSeq; NP_359613.1; NC_003098.1.
DR RefSeq; WP_001249454.1; NC_003098.1.
DR AlphaFoldDB; Q8DMY3; -.
DR STRING; 171101.spr2022; -.
DR EnsemblBacteria; AAL00824; AAL00824; spr2022.
DR GeneID; 60234265; -.
DR GeneID; 66807288; -.
DR KEGG; spr:spr2022; -.
DR PATRIC; fig|171101.6.peg.2188; -.
DR eggNOG; COG2891; Bacteria.
DR HOGENOM; CLU_121959_2_0_9; -.
DR OMA; VCVLEFY; -.
DR Proteomes; UP000000586; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR InterPro; IPR007227; Cell_shape_determining_MreD.
DR Pfam; PF04093; MreD; 1.
DR TIGRFAMs; TIGR03426; shape_MreD; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell shape; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..164
FT /note="Cell shape-determining protein MreD"
FT /id="PRO_0000454548"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 106..126
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 135..155
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 164 AA; 19324 MW; 1080F41C8643E366 CRC64;
MRQLKRVGVF LLLPFFVLID AHISQLLGSF FPHVHLASHF LFLFLLFETI EVSEYLYLVY
CFVIGLVYDV YFFHLIGITT LLFILLGAFL HKLNSVILLN RWTRMLAMIV LTFLFEMGSY
LLAFMVGLTV DSMSIFIVYS LVPTMILNFL WITVFQFIFE KYYL