MREC_BACSU
ID MREC_BACSU Reviewed; 290 AA.
AC Q01466;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 3.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Cell shape-determining protein MreC;
DE AltName: Full=Cell shape protein MreC;
DE AltName: Full=Rod shape-determining protein MreC;
DE Flags: Precursor;
GN Name=mreC; OrderedLocusNames=BSU28020;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / PY79;
RX PubMed=1400224; DOI=10.1128/jb.174.21.6717-6728.1992;
RA Levin P.A., Margolis P.S., Setlow P., Losick R., Sun D.;
RT "Identification of Bacillus subtilis genes for septum placement and shape
RT determination.";
RL J. Bacteriol. 174:6717-6728(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=1400225; DOI=10.1128/jb.174.21.6729-6742.1992;
RA Varley A.W., Stewart G.C.;
RT "The divIVB region of the Bacillus subtilis chromosome encodes homologs of
RT Escherichia coli septum placement (minCD) and cell shape (mreBCD)
RT determinants.";
RL J. Bacteriol. 174:6729-6742(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [4]
RP SEQUENCE REVISION TO 143 AND 176.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [5]
RP DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=12867458; DOI=10.1128/jb.185.15.4490-4498.2003;
RA Lee J.C., Stewart G.C.;
RT "Essential nature of the mreC determinant of Bacillus subtilis.";
RL J. Bacteriol. 185:4490-4498(2003).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=15745453; DOI=10.1186/1471-2121-6-10;
RA Defeu Soufo H.J., Graumann P.L.;
RT "Bacillus subtilis actin-like protein MreB influences the positioning of
RT the replication machinery and requires membrane proteins MreC/D and other
RT actin-like proteins for proper localization.";
RL BMC Cell Biol. 6:10-10(2005).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=16101995; DOI=10.1111/j.1365-2958.2005.04736.x;
RA Leaver M., Errington J.;
RT "Roles for MreC and MreD proteins in helical growth of the cylindrical cell
RT wall in Bacillus subtilis.";
RL Mol. Microbiol. 57:1196-1209(2005).
RN [8]
RP SELF-ASSOCIATION, INTERACTION WITH MRED AND PENICILLIN-BINDING PROTEINS,
RP AND MUTAGENESIS OF 229-THR-SER-230.
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).
RN [9]
RP SUBCELLULAR LOCATION.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=22882210; DOI=10.1111/j.1365-2958.2012.08205.x;
RA Yepes A., Schneider J., Mielich B., Koch G., Garcia-Betancur J.C.,
RA Ramamurthi K.S., Vlamakis H., Lopez D.;
RT "The biofilm formation defect of a Bacillus subtilis flotillin-defective
RT mutant involves the protease FtsH.";
RL Mol. Microbiol. 86:457-471(2012).
RN [10]
RP NMR SPECTROSCOPY OF 104-279.
RX PubMed=20623345; DOI=10.1007/s12104-010-9249-2;
RA Kyburz A., Raulinaitis V., Koskela O., Kontinen V., Permi P.,
RA Kilpelainen I., Seppala R.;
RT "1H, 13C and 15N resonance assignments of the major extracytoplasmic domain
RT of the cell shape-determining protein MreC from Bacillus subtilis.";
RL Biomol. NMR. Assign. 4:235-238(2010).
CC -!- FUNCTION: Involved in formation and maintenance of cell shape. Required
CC for the formation of proper helical filaments of MreB and for cell wall
CC synthesis in the cylindrical part of the cell leading to cell
CC elongation. {ECO:0000269|PubMed:15745453, ECO:0000269|PubMed:16101995}.
CC -!- SUBUNIT: Self-associates. Interacts with MreD and proteins that belong
CC to class A and class B high-molecular-weight penicillin-binding
CC proteins (PBP2b, PBP1, PBP2a, PBP3, PBP4, PBP2c, PBP2d, PBPH and
CC PBP4b). {ECO:0000269|PubMed:17427287}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22882210}. Cell
CC septum. Membrane raft {ECO:0000269|PubMed:22882210}. Note=Localizes in
CC helical patterns when associated with the cell membrane
CC (PubMed:15745453). Present in detergent-resistant membrane (DRM)
CC fractions that may be equivalent to eukaryotic membrane rafts; these
CC rafts include proteins involved in signaling, molecule trafficking and
CC protein secretion (PubMed:22882210). {ECO:0000269|PubMed:15745453,
CC ECO:0000269|PubMed:22882210}.
CC -!- DISRUPTION PHENOTYPE: Loss of viability. Cells lacking sufficient
CC quantities of this protein undergo morphological changes, namely,
CC swelling and twisting of the cells followed by cell lysis. A polymeric
CC material accumulates at one side of the division septum of the cells
CC and the presence of this material correlates with the bending of the
CC cell. After prolonged depletion in the presence of MgCl(2), the cells
CC become very short and fat and eventually spheroidal, but no significant
CC lysis is observed. Addition of sucrose results in rounded cells. Cells
CC are still capable of making division septa. Null mutants show little or
CC no sign of a defined long axis and have a severe shape defect.
CC {ECO:0000269|PubMed:12867458, ECO:0000269|PubMed:1400225,
CC ECO:0000269|PubMed:15745453, ECO:0000269|PubMed:16101995}.
CC -!- SIMILARITY: Belongs to the MreC family. {ECO:0000305}.
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DR EMBL; M96343; AAA22398.1; -; Genomic_DNA.
DR EMBL; M95582; AAA22606.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14762.2; -; Genomic_DNA.
DR PIR; C45240; C45240.
DR PIR; E69660; E69660.
DR RefSeq; NP_390680.2; NC_000964.3.
DR RefSeq; WP_009967915.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; Q01466; -.
DR BMRB; Q01466; -.
DR SMR; Q01466; -.
DR IntAct; Q01466; 10.
DR STRING; 224308.BSU28020; -.
DR TCDB; 9.B.157.1.1; the cell shape-determining mrebcd (mrebcd) family.
DR PaxDb; Q01466; -.
DR PRIDE; Q01466; -.
DR EnsemblBacteria; CAB14762; CAB14762; BSU_28020.
DR GeneID; 937498; -.
DR KEGG; bsu:BSU28020; -.
DR PATRIC; fig|224308.179.peg.3044; -.
DR eggNOG; COG1792; Bacteria.
DR InParanoid; Q01466; -.
DR OMA; NPFTHRI; -.
DR PhylomeDB; Q01466; -.
DR BioCyc; BSUB:BSU28020-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0030428; C:cell septum; IDA:UniProtKB.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0043621; F:protein self-association; IPI:UniProtKB.
DR GO; GO:0009273; P:peptidoglycan-based cell wall biogenesis; IMP:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; IMP: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 Cell membrane; Cell shape; Coiled coil; Membrane; Reference proteome;
KW Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..290
FT /note="Cell shape-determining protein MreC"
FT /id="PRO_0000062766"
FT COILED 58..111
FT /evidence="ECO:0000255"
FT MUTAGEN 229..230
FT /note="TS->AA: No effect on cell shape or cell viability."
FT /evidence="ECO:0000269|PubMed:17427287"
FT CONFLICT 143
FT /note="K -> F (in Ref. 2; AAA22398)"
FT /evidence="ECO:0000305"
FT CONFLICT 176
FT /note="T -> P (in Ref. 2; AAA22398)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 290 AA; 32141 MW; B9984D25BB414A5C CRC64;
MPNKRLMLLL LCIIILVAMI GFSLKGGRNT TWPEKVIGDT TGVFQNIFHT PAEFFAGIFE
NINDLKNTYK ENERLREKLD GQTQYEAKLQ ELEEENKSLR DELGHVKSIK DYKPILATVI
ARSPDNWAKQ VTINKGTQQN VAKDMAVTNE KGALIGKIKS SGLNNFTSAV QLLSDTDRNN
RVATKISGKK GSKGYGLIEG YDKEKKRLKM TIIERKDKQD VKKGDLIETS GTGGVFPEGL
TIGEVTDIES DSYGLTKVAY VKPAADLTDL NNVIVVNRDV PTVDTEEEGS
