MREC_LISMO
ID MREC_LISMO Reviewed; 295 AA.
AC Q8Y6Y4;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Cell shape-determining protein MreC {ECO:0000250|UniProtKB:Q01466};
DE AltName: Full=Cell shape protein MreC {ECO:0000250|UniProtKB:Q01466};
DE AltName: Full=Rod shape-determining protein MreC {ECO:0000250|UniProtKB:Q01466};
DE Flags: Precursor;
GN Name=mreC {ECO:0000312|EMBL:CAC99625.1}; OrderedLocusNames=lmo1547;
OS Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=169963;
RN [1] {ECO:0000312|EMBL:CAC99625.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).
RN [2] {ECO:0000312|PDB:2J5U}
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 50-295, AND SUBUNIT.
RC STRAIN=ATCC BAA-679 / EGD-e {ECO:0000269|PubMed:17427287};
RX PubMed=17427287; DOI=10.1111/j.1365-2958.2006.05485.x;
RA van den Ent F., Leaver M., Bendezu F., Errington J., de Boer P., Lowe J.;
RT "Dimeric structure of the cell shape protein MreC and its functional
RT implications.";
RL Mol. Microbiol. 62:1631-1642(2006).
CC -!- FUNCTION: Involved in formation and maintenance of cell shape.
CC {ECO:0000250|UniProtKB:Q01466}.
CC -!- SUBUNIT: Homooligomer of 24 subunits, arranged as 12 dimers.
CC {ECO:0000269|PubMed:17427287}.
CC -!- SIMILARITY: Belongs to the MreC family. {ECO:0000305}.
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DR EMBL; AL591979; CAC99625.1; -; Genomic_DNA.
DR PIR; AC1268; AC1268.
DR RefSeq; NP_465072.1; NC_003210.1.
DR RefSeq; WP_003725674.1; NZ_CP023861.1.
DR PDB; 2J5U; X-ray; 2.50 A; A/B=50-295.
DR PDBsum; 2J5U; -.
DR AlphaFoldDB; Q8Y6Y4; -.
DR SMR; Q8Y6Y4; -.
DR STRING; 169963.lmo1547; -.
DR PaxDb; Q8Y6Y4; -.
DR EnsemblBacteria; CAC99625; CAC99625; CAC99625.
DR GeneID; 986941; -.
DR KEGG; lmo:lmo1547; -.
DR PATRIC; fig|169963.11.peg.1588; -.
DR eggNOG; COG1792; Bacteria.
DR HOGENOM; CLU_042663_1_1_9; -.
DR OMA; NPFTHRI; -.
DR PhylomeDB; Q8Y6Y4; -.
DR BioCyc; LMON169963:LMO1547-MON; -.
DR EvolutionaryTrace; Q8Y6Y4; -.
DR Proteomes; UP000000817; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0008360; P:regulation of cell shape; ISS:UniProtKB.
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 shape; Coiled coil; Reference proteome; Signal.
FT SIGNAL 1..34
FT /evidence="ECO:0000255"
FT CHAIN 35..295
FT /note="Cell shape-determining protein MreC"
FT /evidence="ECO:0000255"
FT /id="PRO_0000418058"
FT REGION 276..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 66..112
FT /evidence="ECO:0000255"
FT TURN 75..77
FT /evidence="ECO:0007829|PDB:2J5U"
FT HELIX 79..106
FT /evidence="ECO:0007829|PDB:2J5U"
FT STRAND 116..125
FT /evidence="ECO:0007829|PDB:2J5U"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:2J5U"
FT TURN 131..133
FT /evidence="ECO:0007829|PDB:2J5U"
FT STRAND 134..138
FT /evidence="ECO:0007829|PDB:2J5U"
FT HELIX 141..143
FT /evidence="ECO:0007829|PDB:2J5U"
FT STRAND 150..153
FT /evidence="ECO:0007829|PDB:2J5U"
FT STRAND 156..164
FT /evidence="ECO:0007829|PDB:2J5U"
FT STRAND 169..173
FT /evidence="ECO:0007829|PDB:2J5U"
FT STRAND 183..187
FT /evidence="ECO:0007829|PDB:2J5U"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:2J5U"
FT STRAND 193..201
FT /evidence="ECO:0007829|PDB:2J5U"
FT TURN 202..205
FT /evidence="ECO:0007829|PDB:2J5U"
FT STRAND 206..213
FT /evidence="ECO:0007829|PDB:2J5U"
FT STRAND 223..226
FT /evidence="ECO:0007829|PDB:2J5U"
FT STRAND 231..233
FT /evidence="ECO:0007829|PDB:2J5U"
FT STRAND 238..247
FT /evidence="ECO:0007829|PDB:2J5U"
FT STRAND 251..262
FT /evidence="ECO:0007829|PDB:2J5U"
FT STRAND 269..275
FT /evidence="ECO:0007829|PDB:2J5U"
SQ SEQUENCE 295 AA; 32094 MW; 80DAA3218D329834 CRC64;
MPQFFLNKRL IILLISIIVL VALVGFSLRD RENASWPEQF VKDVVGFGEN IVAKPTSFIS
GAVDGVVDLK NTYTENQHLK ERLEELAQLE SEVADLKKEN KDLKESLDIT DSIRDYDPLN
ASVISRNPTN WNDQVEIDKG SSDGVKPDMA VTTPSGLIGK VTTTGAKSAT VELLTSSDVK
NRVSAKVQGK ENAFGIINGY DSDTKLLELK QLPYDMKFKK GQKVVTSGLG GKFPAGIFIG
TIEKVETDKM GLSQTAFIKP GADMYDLNHV TVLKRSAEAG TTDDDTTSSD TTGGQ
