ID A0A432ZX95_9MOLU Unreviewed; 352 AA.
AC A0A432ZX95;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, 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 ORFNames=D9R21_01295 {ECO:0000313|EMBL:RUO86747.1};
OS Spiroplasma endosymbiont of Megaselia nigra.
OC Bacteria; Mycoplasmatota; Mollicutes; Entomoplasmatales; Spiroplasmataceae;
OC Spiroplasma.
OX NCBI_TaxID=2478537 {ECO:0000313|EMBL:RUO86747.1, ECO:0000313|Proteomes:UP000270797};
RN [1] {ECO:0000313|EMBL:RUO86747.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SNigra {ECO:0000313|EMBL:RUO86747.1};
RX PubMed=30576446; DOI=.1093/gbe/evy272;
RA Ballinger M.J., Gawryluk R.M., Perlman S.J.;
RT "Toxin and genome evolution in a Drosophila defensive symbiosis.";
RL Genome Biol. Evol. 11:253-262(2019).
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:RUO86747.1}.
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DR EMBL; RCOO01000011; RUO86747.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A432ZX95; -.
DR Proteomes; UP000270797; 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 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:UP000270797}.
FT BINDING 15..17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT BINDING 159..161
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT BINDING 207..210
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT BINDING 287..290
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
SQ SEQUENCE 352 AA; 38618 MW; 45FA232D4BB119C9 CRC64;
MRPETRPFIS LDLGTANVLA YVSGQGVIYN EPSLMAYNNK TNSLIALGKA AYDMVGKTHG
DIRMVTPLVD GVIADMEAAQ DLLKHIFSRM KMMNIWKNAI VLLACPSGVT ELEREALKNV
AKEMGAELVI IEEEAKMAAL GAGINIELPK GHLIIDIGGG TADLAIISSG DIVVSKSIKV
AGNHFDDDIR KYIRSEYNIA IGQKTAEDVK KFIGSLVKYH NERSMQIYGR DIVSGLPKEA
KISSEEIRNV LLNAFSKITD LVIELLENTP PELAGDIFRN GITVCGGGAL IRNIDKYFFD
IFQLPTKIAS DPLNCVIEGT KIFEKTIKKN IENGLYNFQE KGLLSSLGKK RK
//
