ID   MREC_STRR6              Reviewed;         272 AA.
AC   Q8DMY2;
DT   11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Cell shape-determining protein MreC {ECO:0000303|PubMed:17707860, ECO:0000312|EMBL:AAL00825.1};
DE   AltName: Full=Cell shape protein MreC {ECO:0000250|UniProtKB:Q01466};
GN   Name=mreC {ECO:0000312|EMBL:AAL00825.1}; OrderedLocusNames=spr2023;
OS   Streptococcus pneumoniae (strain ATCC BAA-255 / R6).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=171101;
RN   [1] {ECO:0000312|EMBL:AAL00825.1}
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   FUNCTION, SUBUNIT, DOMAIN, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP   183-GLN--SER-272.
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).
RN   [3] {ECO:0000312|PDB:2QF4}
RP   X-RAY CRYSTALLOGRAPHY (1.20 ANGSTROMS) OF 106-272, AND SUBUNIT.
RC   STRAIN=ATCC BAA-255 / R6 {ECO:0000269|PubMed:17707860};
RX   PubMed=17707860; DOI=10.1016/j.jmb.2007.07.022;
RA   Lovering A.L., Strynadka N.C.;
RT   "High-resolution structure of the major periplasmic domain from the cell
RT   shape-determining filament MreC.";
RL   J. Mol. Biol. 372:1034-1044(2007).
CC   -!- FUNCTION: Involved in formation and maintenance of cell shape, probably
CC       part of the elongasome which synthesizes peripheral peptidogylcan (PG).
CC       {ECO:0000269|PubMed:28710862}.
CC   -!- SUBUNIT: Homodimer (Probable). Interacts with a number of proteins in
CC       the elongasome, including PBP1a (pbpA), PBP1b, PBP2a, PBP2b (penA),
CC       StkP, MltG, MreD and RodZ (PubMed:28710862).
CC       {ECO:0000269|PubMed:28710862, ECO:0000305|PubMed:17707860}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}.
CC   -!- DOMAIN: Deletion of the C-terminus (residues 183-272, CTD) suppresses
CC       activating mutations in khpB (also called eloR/jag); the deletion no
CC       longer interacts with MreD and interacts less efficiently with PBP1b
CC       and StkP, CTD deletion leads to increased phosphorylation of KhpB.
CC       {ECO:0000269|PubMed:28710862}.
CC   -!- DISRUPTION PHENOTYPE: Cell shape does not change, cells start
CC       autolysing earlier. Neither PBP2b (penA) nor rodA can be deleted when
CC       this gene is absent. {ECO:0000269|PubMed:28710862}.
CC   -!- SIMILARITY: Belongs to the MreC family. {ECO:0000305}.
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DR   EMBL; AE007317; AAL00825.1; -; Genomic_DNA.
DR   PIR; A95259; A95259.
DR   PIR; D98124; D98124.
DR   RefSeq; NP_359614.1; NC_003098.1.
DR   RefSeq; WP_001078983.1; NC_003098.1.
DR   PDB; 2QF4; X-ray; 1.20 A; A/B=106-272.
DR   PDB; 2QF5; X-ray; 2.23 A; A=106-272.
DR   PDBsum; 2QF4; -.
DR   PDBsum; 2QF5; -.
DR   AlphaFoldDB; Q8DMY2; -.
DR   SMR; Q8DMY2; -.
DR   BioGRID; 4182238; 3.
DR   STRING; 171101.spr2023; -.
DR   EnsemblBacteria; AAL00825; AAL00825; spr2023.
DR   GeneID; 60234073; -.
DR   GeneID; 66807289; -.
DR   KEGG; spr:spr2023; -.
DR   PATRIC; fig|171101.6.peg.2189; -.
DR   eggNOG; COG1792; Bacteria.
DR   HOGENOM; CLU_042663_1_1_9; -.
DR   OMA; NPFTHRI; -.
DR   EvolutionaryTrace; Q8DMY2; -.
DR   Proteomes; UP000000586; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0008360; P:regulation of cell shape; IBA:GO_Central.
DR   Gene3D; 2.40.10.340; -; 1.
DR   Gene3D; 2.40.10.350; -; 1.
DR   InterPro; IPR042177; Cell/Rod_1.
DR   InterPro; IPR042175; Cell/Rod_MreC_2.
DR   InterPro; IPR007221; MreC.
DR   PANTHER; PTHR34138; PTHR34138; 1.
DR   Pfam; PF04085; MreC; 1.
DR   PIRSF; PIRSF038471; MreC; 1.
DR   TIGRFAMs; TIGR00219; mreC; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell membrane; Cell shape; Coiled coil; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..272
FT                   /note="Cell shape-determining protein MreC"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000418060"
FT   TOPO_DOM        1..8
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:17707860"
FT   TRANSMEM        9..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        30..272
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305|PubMed:17707860"
FT   COILED          64..112
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         183..272
FT                   /note="Missing: Cells are round instead of ovoid, protein
FT                   no longer interacts with MreD."
FT                   /evidence="ECO:0000269|PubMed:28710862"
FT   STRAND          111..121
FT                   /evidence="ECO:0007829|PDB:2QF5"
FT   STRAND          129..133
FT                   /evidence="ECO:0007829|PDB:2QF5"
FT   HELIX           136..138
FT                   /evidence="ECO:0007829|PDB:2QF5"
FT   STRAND          145..148
FT                   /evidence="ECO:0007829|PDB:2QF5"
FT   STRAND          151..159
FT                   /evidence="ECO:0007829|PDB:2QF5"
FT   STRAND          164..168
FT                   /evidence="ECO:0007829|PDB:2QF5"
FT   STRAND          171..184
FT                   /evidence="ECO:0007829|PDB:2QF5"
FT   STRAND          187..197
FT                   /evidence="ECO:0007829|PDB:2QF5"
FT   TURN            198..201
FT                   /evidence="ECO:0007829|PDB:2QF5"
FT   STRAND          202..206
FT                   /evidence="ECO:0007829|PDB:2QF5"
FT   STRAND          219..223
FT                   /evidence="ECO:0007829|PDB:2QF5"
FT   STRAND          226..228
FT                   /evidence="ECO:0007829|PDB:2QF5"
FT   STRAND          231..242
FT                   /evidence="ECO:0007829|PDB:2QF5"
FT   STRAND          251..258
FT                   /evidence="ECO:0007829|PDB:2QF5"
FT   STRAND          265..271
FT                   /evidence="ECO:0007829|PDB:2QF5"
SQ   SEQUENCE   272 AA;  29739 MW;  E778882FEA7341B8 CRC64;
     MNRFKKSKYV IIVFVTVLLV SALLATTYSS TIVTKLGDGI SLVDRVVQKP FQWFDSVKSD
     LAHLTRTYNE NESLKKQLYQ LEVKSNEVES LKTENEQLRQ LLDMKSKLQA TKTLAADVIM
     RSPVSWKQEL TLDAGRSKGA SENMLAIANG GLIGSVSKVE ENSTIVNLLT NTENADKISV
     KIQHGSTTIY GIIIGYDKEN DVLKISQLNS NSDISAGDKV TTGGLGNFNV ADIPVGEVVA
     TTHSTDYLTR EVTVKLSADT HNVDVIELVG NS