ID   G6EXY2_9PROT            Unreviewed;       339 AA.
AC   G6EXY2;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 33.
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=CIN_03020 {ECO:0000313|EMBL:EHD14370.1};
OS   Commensalibacter intestini A911.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae.
OX   NCBI_TaxID=1088868 {ECO:0000313|EMBL:EHD14370.1, ECO:0000313|Proteomes:UP000005939};
RN   [1] {ECO:0000313|EMBL:EHD14370.1, ECO:0000313|Proteomes:UP000005939}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A911 {ECO:0000313|EMBL:EHD14370.1,
RC   ECO:0000313|Proteomes:UP000005939};
RA   Lee W.-J., Kim E.-K.;
RT   "Genome Sequence of Commensalibacter intestini A911, isolated from
RT   Drosophila gut.";
RL   Submitted (OCT-2011) 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:EHD14370.1}.
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DR   EMBL; AGFR01000003; EHD14370.1; -; Genomic_DNA.
DR   AlphaFoldDB; G6EXY2; -.
DR   STRING; 1088868.CIN_03020; -.
DR   PATRIC; fig|1088868.3.peg.302; -.
DR   eggNOG; COG1077; Bacteria.
DR   Proteomes; UP000005939; 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; CELL SHAPE-DETERMINING PROTEIN MREB; 1.
DR   PANTHER; PTHR42749:SF1; 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}.
FT   BINDING         11..13
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         288..291
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
SQ   SEQUENCE   339 AA;  35876 MW;  52780C1136622474 CRC64;
     MSADMAIDLG TANTLVYVKG RGIVLNEPSV VAIAEVRGKK QVLAVGEEAK NMVGRTPGNI
     TAIRPMRDGV IADFEVAEEM IKHFIHKVHN RRMFASPQIV ICVPSGATAV ERRAIQESAE
     GAGARRVQLI EEPMAAAIGA GLPVTEPSGS MIVDIGGGTT EVAVISLGGI VYSRSVRVGG
     DRMDEAIIAY IRRHHNLLIG ESSAEKIKME LGAAIASPSA DGGPWREVKG RDLMNGVPRE
     VLVSQEQIAD SLAEPIAQIV EGVSIALENT PPELAADIVD KGIMLTGGGS LLARLDDVLR
     QATGLPVIVA ENPLDCVALG TGRALEEMKR LRNILTSMY
//