ID A0A075RBS0_BRELA Unreviewed; 335 AA.
AC A0A075RBS0;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=Cell shape-determining protein MreB {ECO:0000256|HAMAP-Rule:MF_02207};
GN Name=mreB_2 {ECO:0000313|EMBL:AIG28673.1};
GN Synonyms=mreB {ECO:0000256|HAMAP-Rule:MF_02207};
GN ORFNames=BRLA_c044090 {ECO:0000313|EMBL:AIG28673.1};
OS Brevibacillus laterosporus LMG 15441.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX NCBI_TaxID=1042163 {ECO:0000313|EMBL:AIG28673.1, ECO:0000313|Proteomes:UP000005850};
RN [1] {ECO:0000313|EMBL:AIG28673.1, ECO:0000313|Proteomes:UP000005850}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 15441 {ECO:0000313|EMBL:AIG28673.1,
RC ECO:0000313|Proteomes:UP000005850};
RX PubMed=21914864; DOI=10.1128/JB.05696-11;
RA Djukic M., Poehlein A., Thurmer A., Daniel R.;
RT "Genome sequence of Brevibacillus laterosporus LMG 15441, a pathogen of
RT invertebrates.";
RL J. Bacteriol. 193:5535-5536(2011).
CC -!- FUNCTION: Forms membrane-associated dynamic filaments that are
CC essential for cell shape determination. Acts by regulating cell wall
CC synthesis and cell elongation, and thus cell shape. A feedback loop
CC between cell geometry and MreB localization may maintain elongated cell
CC shape by targeting cell wall growth to regions of negative cell wall
CC curvature. {ECO:0000256|HAMAP-Rule:MF_02207}.
CC -!- SUBUNIT: Forms polymers. {ECO:0000256|HAMAP-Rule:MF_02207}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02207}.
CC Note=Membrane-associated. {ECO:0000256|HAMAP-Rule:MF_02207}.
CC -!- SIMILARITY: Belongs to the FtsA/MreB family.
CC {ECO:0000256|ARBA:ARBA00023458, ECO:0000256|HAMAP-Rule:MF_02207}.
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DR EMBL; CP007806; AIG28673.1; -; Genomic_DNA.
DR RefSeq; WP_003334277.1; NZ_CP007806.1.
DR AlphaFoldDB; A0A075RBS0; -.
DR STRING; 1042163.BRLA_c044090; -.
DR KEGG; blr:BRLA_c044090; -.
DR eggNOG; COG1077; Bacteria.
DR HOGENOM; CLU_052037_0_0_9; -.
DR Proteomes; UP000005850; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000902; P:cell morphogenesis; IEA:InterPro.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-UniRule.
DR CDD; cd10225; MreB_like; 1.
DR Gene3D; 3.30.420.40; -; 3.
DR HAMAP; MF_02207; MreB; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR004753; MreB.
DR NCBIfam; TIGR00904; mreB; 1.
DR PANTHER; PTHR42749:SF4; CELL SHAPE-DETERMINING PROTEIN MBL; 1.
DR PANTHER; PTHR42749; CELL SHAPE-DETERMINING PROTEIN MREB; 1.
DR Pfam; PF06723; MreB_Mbl; 1.
DR PRINTS; PR01652; SHAPEPROTEIN.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_02207};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|HAMAP-
KW Rule:MF_02207}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02207};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02207};
KW Reference proteome {ECO:0000313|Proteomes:UP000005850}.
FT BINDING 12..14
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT BINDING 157..159
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT BINDING 205..208
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT BINDING 284..287
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
SQ SEQUENCE 335 AA; 36218 MW; A8F061776D809936 CRC64;
MLSKDIGIDL GTANVLIYVK GRGIVLDEPS VVAIDDHTKK VLAVGNEAHR MVGRTPGNII
AIRPLRDGVI ADFEITEAML KHFMAKIGAK SFFARPRILI CCPTNITSVE QKAIREAAER
SGGAREVFIE EEPKVAAIGA GMDIYQPSGN MVVDIGGGTT DVAVLSMGDI VTASSIKVAG
DKFDLAIMRY IKSKYKMLIG ERTAEDIKVQ IGTVYGSRQD EMDIRGRDMV SGLPQTITIR
SQEVQISLAE SVSQIVQASK NVLERTPPEL SADIIDKGVF LTGGGALLHG LDQMLMDELK
VPVLVAEEPM NCVAKGTGLM LDYLDKLPSR KKFFG
//
