ID A0A399EQP7_9DEIN Unreviewed; 348 AA.
AC A0A399EQP7;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Cell shape-determining protein MreB {ECO:0000256|HAMAP-Rule:MF_02207};
GN Name=mreB {ECO:0000256|HAMAP-Rule:MF_02207,
GN ECO:0000313|EMBL:RIH84481.1};
GN ORFNames=Mlute_01868 {ECO:0000313|EMBL:RIH84481.1};
OS Meiothermus luteus.
OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Meiothermus.
OX NCBI_TaxID=2026184 {ECO:0000313|EMBL:RIH84481.1, ECO:0000313|Proteomes:UP000265800};
RN [1] {ECO:0000313|EMBL:RIH84481.1, ECO:0000313|Proteomes:UP000265800}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 52599 {ECO:0000313|EMBL:RIH84481.1,
RC ECO:0000313|Proteomes:UP000265800};
RA Da Costa M.S., Albuquerque L., Raposo P., Froufe H.J.C., Barroso C.S.,
RA Egas C.;
RT "Meiothermus luteus KCTC 52599 genome sequencing project.";
RL Submitted (AUG-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: 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:RIH84481.1}.
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DR EMBL; QWKZ01000060; RIH84481.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A399EQP7; -.
DR OrthoDB; 9768127at2; -.
DR Proteomes; UP000265800; 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 162..164
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT BINDING 210..213
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT BINDING 292..295
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
SQ SEQUENCE 348 AA; 36966 MW; D772DFBAAA162881 CRC64;
MAGWFSFRGE DVGIDLGTAS VLIYMRGKGI VLREPSVIAM VSDTKEVKAV GAEAYRMLGR
TPGNIVAARP LKDGVIADYT LTERMLTLFI KKVLPPLRFF RPQVMVGVPS GVTEVERRAV
VQAIVEAGAK RAYLIDEPLA AAIGAGIKIA EPTGSMVVDI GGGSSDIAVI SLGGIVRSTS
LRIAGNEFDE SIIRYVRSKY NLLIGERTAE DLKIKIGAAK LAPGEQEMVA EVRGRDLISG
LPKSIEVTTG DVVEALKEPL EKIVQGVRGV LETTPPELVA DIIDRGILLT GGGALLRNLD
LLLQEATGVP VVVAENAVEA VALGTGKALD MLHVLRDALV TSDNVLRR
//