ID A0A417YQE8_9BACI Unreviewed; 335 AA.
AC A0A417YQE8;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 19.
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=D1B31_16670 {ECO:0000313|EMBL:RHW36351.1};
OS Neobacillus notoginsengisoli.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Neobacillus.
OX NCBI_TaxID=1578198 {ECO:0000313|EMBL:RHW36351.1, ECO:0000313|Proteomes:UP000284416};
RN [1] {ECO:0000313|EMBL:RHW36351.1, ECO:0000313|Proteomes:UP000284416}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 30743 {ECO:0000313|EMBL:RHW36351.1,
RC ECO:0000313|Proteomes:UP000284416};
RX PubMed=28786779; DOI=10.1099/ijsem.0.001975;
RA Zhang M.Y., Cheng J., Cai Y., Zhang T.Y., Wu Y.Y., Manikprabhu D., Li W.J.,
RA Zhang Y.X.;
RT "Bacillus notoginsengisoli sp. nov., a novel bacterium isolated from the
RT rhizosphere of Panax notoginseng.";
RL Int. J. Syst. Evol. Microbiol. 67:2581-2585(2017).
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:RHW36351.1}.
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DR EMBL; QWEG01000011; RHW36351.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A417YQE8; -.
DR OrthoDB; 9768127at2; -.
DR Proteomes; UP000284416; 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 13..15
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 335 AA; 35857 MW; 4B8C29F5C2D7E2C6 CRC64;
MLSNAEIGID LGTANILVYS KNKGIALNEP SVVAIDTETK TVLAVGKEAK EMIGKTPGKI
VAIRPLKDGV IADYDVTTEL LTHIMRKASK KIGLSIRKPD VVVCTPSGST SVERRAIHDA
VRNAGAKKIH LIEEPVAAAI GAGMPVDEPV ANVIVDIGGG TTEVAIISFG GVVACHSIRV
AGDRLDEDII KHVRNEYNVL IGERTAELIK MEIGYALVDH QELKLEIRGR DLVTGLPKTI
TLSSYEIREA LREPLLQILE AIRATLEDCP AEMSGDIVDR GVIITGGGAL MKGMEEWLSK
EIFVPVHVAE EPLESVAIGT GKALQFIGKL QTVAK
//