ID A0A0G0Y6Q0_9BACT Unreviewed; 334 AA.
AC A0A0G0Y6Q0;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=UU93_C0007G0014 {ECO:0000313|EMBL:KKS32409.1};
OS Candidatus Amesbacteria bacterium GW2011_GWA2_42_12.
OC Bacteria; Candidatus Amesbacteria.
OX NCBI_TaxID=1618356 {ECO:0000313|EMBL:KKS32409.1, ECO:0000313|Proteomes:UP000034160};
RN [1] {ECO:0000313|EMBL:KKS32409.1, ECO:0000313|Proteomes:UP000034160}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {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:KKS32409.1}.
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DR EMBL; LCCN01000007; KKS32409.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0Y6Q0; -.
DR STRING; 1618356.UU93_C0007G0014; -.
DR PATRIC; fig|1618356.3.peg.429; -.
DR Proteomes; UP000034160; 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 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"
SQ SEQUENCE 334 AA; 35279 MW; 70FB31C24A0916BE CRC64;
MLNKRIGIDL GTANSLVWVA GQGLVMNEPT VVAVGTEDGR IVAVGNEAKE MLGRTPGNIT
ASRPMRDGVI ADYRVTEAML KYFIQKVCGR IFLFKPEVMI CVPAGVTQVE RRAVLDATLS
AGAKAAYLID EPLAAAIGAR LPIAAASGNM IIDIGGGSAE AAVICLGGVV VHKSVRVAGN
KLDEAIIGYM KKKHNLLIGE TTAEEAKIRI GSALVLDKPE SMEIKGRDSI TGLPRAIETS
STEITEAIRP VLLAIIGAAK GVLEETPPEL ASDIIDKGII MSGGTSALRN FDRLMTELTG
VPCHVAEDPL MCVVRGTGIA IENLDLYKKS IIKR
//
