ID   A0A2M9E4H4_9GAMM        Unreviewed;       347 AA.
AC   A0A2M9E4H4;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   24-JAN-2024, entry version 20.
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=CO641_08330 {ECO:0000313|EMBL:PJJ98601.1};
OS   Xanthomonadaceae bacterium NML91-0213.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae.
OX   NCBI_TaxID=2032582 {ECO:0000313|EMBL:PJJ98601.1, ECO:0000313|Proteomes:UP000229012};
RN   [1] {ECO:0000313|EMBL:PJJ98601.1, ECO:0000313|Proteomes:UP000229012}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NML91-0213 {ECO:0000313|EMBL:PJJ98601.1,
RC   ECO:0000313|Proteomes:UP000229012};
RA   Bernier A.-M., Bernard K.;
RT   "Zoonotically transmitted species of Xanthomonadaceae : Genome sequencing
RT   and assembly.";
RL   Submitted (SEP-2017) 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:PJJ98601.1}.
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DR   EMBL; NWQL01000003; PJJ98601.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2M9E4H4; -.
DR   OrthoDB; 9768127at2; -.
DR   Proteomes; UP000229012; 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; -; 2.
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         19..21
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT   BINDING         168..170
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT   BINDING         216..219
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT   BINDING         296..299
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
SQ   SEQUENCE   347 AA;  37238 MW;  9BCC96B1EECCF9CC CRC64;
     MFKKFRGLFS NDLSIDLGTA NTLIFVRGQG IVLNEPSVVA VRQDRAGGQK VVAAVGSEAK
     QMLGRTPGNI TTHRPMKDGV IADFTYTEEM LKHFIRKVHK SRLLRPSPRV LICVPAGSTQ
     VEKRAIKDSA LEAGARDVSL IEEPMAAAIG AGMPVTEARG SMVVDVGGGT TEVAVIALNG
     IVYSQSARIG GDRFDESIIN YVRRNHGMLI GEATAERVKI ELGCAYPQEK VEETEISGRH
     LAEGVPKMVK INSNEVLEAL REPLMGIVAA VRQALEQTPP ELSADVAERG IVLTGGGALL
     RDLDRLISEE TGLHVQVADD PLTCVARGGG RALELLDLHG NEFFTAD
//