ID   A0A0D6A3X5_9LACO        Unreviewed;       329 AA.
AC   A0A0D6A3X5;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=Cell shape-determining protein MreB {ECO:0000256|HAMAP-Rule:MF_02207};
GN   Name=mreB {ECO:0000256|HAMAP-Rule:MF_02207};
GN   ORFNames=LBAT_1052 {ECO:0000313|EMBL:BAQ57441.1};
OS   Lactobacillus acetotolerans.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=1600 {ECO:0000313|EMBL:BAQ57441.1, ECO:0000313|Proteomes:UP000035709};
RN   [1] {ECO:0000313|EMBL:BAQ57441.1, ECO:0000313|Proteomes:UP000035709}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 13120 {ECO:0000313|EMBL:BAQ57441.1,
RC   ECO:0000313|Proteomes:UP000035709};
RA   Toh H., Morita H., Fujita N.;
RT   "Complete genome sequence of Lactobacillus acetotolerans NBRC 13120.";
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
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; AP014808; BAQ57441.1; -; Genomic_DNA.
DR   RefSeq; WP_060459561.1; NZ_AP014808.1.
DR   AlphaFoldDB; A0A0D6A3X5; -.
DR   STRING; 1600.LBAT_1052; -.
DR   KEGG; lae:LBAT_1052; -.
DR   PATRIC; fig|1600.4.peg.1076; -.
DR   OrthoDB; 9768127at2; -.
DR   Proteomes; UP000035709; 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; -; 2.
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:UP000035709}.
FT   BINDING         11..13
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT   BINDING         155..157
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT   BINDING         203..206
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT   BINDING         283..286
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
SQ   SEQUENCE   329 AA;  34938 MW;  2A38D7A25391B5AC CRC64;
     MARDIGIDLG TANVLINVSG KGIVLNEPSV VAVNTSTNNV VAVGTEAYKM VGRTPGNIRV
     IRPLKNGVIA DFDITEAMLS YFIKKLNVKG FMSKPNILIC APTGVTSIEQ KAIIQAAEKS
     GGGKVYLDFE PKVAAVGAGL DIFKPQGNMV IDIGGGTTDI AVLSMGEIVT SQSMRYAGDR
     MNQAVISYIK NKHNLLIGSR TAEQIKIEIG SAFGPDKDAS ITVRGRDVVD GLPKQTTVTA
     PEIQEALHNG LMSIVAATKE VLEKTPPELS ADIIDRGIML TGGGALLKNI DKLISYYLKV
     PVLTADHPLE AVANGTGVLL KNIEKHQRH
//