ID   A0A0F3GN93_9BACT        Unreviewed;       342 AA.
AC   A0A0F3GN93;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
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=MBAV_004453 {ECO:0000313|EMBL:KJU83356.1};
OS   Candidatus Magnetobacterium bavaricum.
OC   Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC   Magnetobacterium.
OX   NCBI_TaxID=29290 {ECO:0000313|EMBL:KJU83356.1, ECO:0000313|Proteomes:UP000033423};
RN   [1] {ECO:0000313|EMBL:KJU83356.1, ECO:0000313|Proteomes:UP000033423}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TM-1 {ECO:0000313|EMBL:KJU83356.1};
RA   Kolinko S., Richter M., Glockner F.O., Brachmann A., Schuler D.;
RT   "Single-cell genomics of uncultivated deep-branching MTB reveals a
RT   conserved set of magnetosome genes.";
RL   Submitted (FEB-2015) 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:KJU83356.1}.
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DR   EMBL; LACI01001940; KJU83356.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F3GN93; -.
DR   PATRIC; fig|29290.4.peg.5909; -.
DR   Proteomes; UP000033423; 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:UP000033423}.
FT   BINDING         20..22
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT   BINDING         164..166
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT   BINDING         212..215
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT   BINDING         293..296
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
SQ   SEQUENCE   342 AA;  36507 MW;  41B300EF8A3B299F CRC64;
     MLFSKFLGLF SNDLAIDLGT ANTLVYAKGK GIVCDEPSVV VMRQDNKKVV AVGAEAKKML
     GKTPANIMTI RPMKDGVIAD FNAAGEMLKY FIKKAHNRKS FVSPRVIIGV PSTITLVEQR
     AVKEAAEASG AREVYLIAET MAAAVGVGLP IDEPYGNMIV DIGGGTTDVA VISMDGIVYS
     KTVKVGGDKM DEKIIVYVKE RYNFMIGDRT AEQIKIEIGS AYKINGEEST IDVNGRDLIS
     GIPKAVTIRE NEIRETLSDT VNIIVSTIKV ALENTPPELA SDIVDNGIVL AGGGALLRGL
     DSLIIKETGL PVIVPESPLT AVVMGVGKML EDLALLRRVA VT
//