ID   A0A2V3WEK9_9BACI        Unreviewed;       333 AA.
AC   A0A2V3WEK9;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   24-JAN-2024, entry version 22.
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=DES38_10353 {ECO:0000313|EMBL:PXW92038.1};
OS   Streptohalobacillus salinus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Streptohalobacillus.
OX   NCBI_TaxID=621096 {ECO:0000313|EMBL:PXW92038.1, ECO:0000313|Proteomes:UP000247922};
RN   [1] {ECO:0000313|EMBL:PXW92038.1, ECO:0000313|Proteomes:UP000247922}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22440 {ECO:0000313|EMBL:PXW92038.1,
RC   ECO:0000313|Proteomes:UP000247922};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (MAY-2018) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PXW92038.1}.
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DR   EMBL; QJJR01000003; PXW92038.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2V3WEK9; -.
DR   OrthoDB; 9768127at2; -.
DR   Proteomes; UP000247922; Unassembled WGS sequence.
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:UP000247922}.
FT   BINDING         12..14
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT   BINDING         156..158
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT   BINDING         204..207
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   333 AA;  36081 MW;  8AA5C7DDF053395F CRC64;
     MFSRDIGIDL GTANVLIHVK GKGIVLDEPS VVAMDRSTSK VLEVGEAARR MVGRTPGNIE
     AIRPLKDGVI ADFDVTEAML RHFISKINVR GMFSKPRMLI CCPTNITKVE QKAIKEAAEK
     SGGKKVYLEE EPKVAAIGAG MDIFQPSGNM VVDIGGGTTD VAVLSMGDIV TSQSIKLAGD
     KFDQEILNYV KKEYKLLIGE RTAEDIKIQV ATVFPGSRDE SIAIRGRDMV SGLPRTITIY
     SDEIEKALKE SVSMIVQAAK NVLEKTPPEL SADIIDRGVI LTGGGALLHG IDQLLAEELK
     VPVFLADEPM SCVARGTGIM LENIDKIERR SFL
//