ID   A0A1B6YSL2_9RHOB        Unreviewed;       348 AA.
AC   A0A1B6YSL2;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
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=A8B83_09060 {ECO:0000313|EMBL:OAN72521.1};
OS   Rhodobacteraceae bacterium EhC02.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae.
OX   NCBI_TaxID=1849170 {ECO:0000313|EMBL:OAN72521.1, ECO:0000313|Proteomes:UP000078223};
RN   [1] {ECO:0000313|EMBL:OAN72521.1, ECO:0000313|Proteomes:UP000078223}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EhC02 {ECO:0000313|EMBL:OAN72521.1,
RC   ECO:0000313|Proteomes:UP000078223};
RA   Lavstsen T., Jespersen J.S.;
RL   Submitted (MAY-2016) 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:OAN72521.1}.
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DR   EMBL; LXYH01000005; OAN72521.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1B6YSL2; -.
DR   STRING; 1849170.A8B83_09060; -.
DR   OrthoDB; 9768127at2; -.
DR   Proteomes; UP000078223; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078223}.
FT   BINDING         21..23
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT   BINDING         167..169
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT   BINDING         215..218
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT   BINDING         297..300
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
SQ   SEQUENCE   348 AA;  36916 MW;  9BE8D27C328F8706 CRC64;
     MSIFDKMPSI FASDMAIDLG TANTLVYVKG KGIVLSEPSV VAYHVKDGVK KVLAVGEDAK
     LMLGRTPGSI EAIRPMRDGV IADFDTAEEM IKHFIRKVLK RSTFSKPKII VCVPHGATPV
     EKRAIRQSVL SAGARRAGLI AEPIAAAIGA GMPITDPTGN MVVDIGGGTT EVAVLSLGDI
     VYARSVRVGG DRMDEAIINY LRRQHNLLVG EATAERIKTS IGTARMPDDG RGTSMMIRGR
     DLLNGVPKET EISQAQVAEA LSEPVQQICE AVMTALEATP PDLAADIVDR GVMLTGGGAL
     LGDLDLALRE QTGLAVSIAD ESLNCVALGT GKALEYEKQL RHAIDYDS
//