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Database: UniProt
Entry: A0A0G1VCA0_9BACT
LinkDB: A0A0G1VCA0_9BACT
Original site: A0A0G1VCA0_9BACT 
ID   A0A0G1VCA0_9BACT        Unreviewed;       350 AA.
AC   A0A0G1VCA0;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 27.
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=UY01_C0004G0010 {ECO:0000313|EMBL:KKU75783.1};
OS   Candidatus Nomurabacteria bacterium GW2011_GWB1_47_6.
OC   Bacteria; Candidatus Nomurabacteria.
OX   NCBI_TaxID=1618749 {ECO:0000313|EMBL:KKU75783.1, ECO:0000313|Proteomes:UP000034879};
RN   [1] {ECO:0000313|EMBL:KKU75783.1, ECO:0000313|Proteomes:UP000034879}
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:KKU75783.1}.
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DR   EMBL; LCOJ01000004; KKU75783.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1VCA0; -.
DR   PATRIC; fig|1618749.3.peg.109; -.
DR   Proteomes; UP000034879; 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         166..168
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT   BINDING         214..217
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   350 AA;  37640 MW;  E4A661C18E38AEE1 CRC64;
     MQIFEKFYKL VSNDIGIDLG TSNTLVYLKG HGIVINEPSV VAVNMKTNQI LAVGGKAKEM
     LGRTPGHIKA VRPLVDGVIS DFEVTEEMLS YLINKADRIS KKLARPRVLI GVPTGTTNVE
     TRAVYDAAKS AGAREVYLVE EPMAAAIGIR LPIKDPVGTM IIDIGGGTTD VAVISLGGIV
     KSKNLKIAGD RLNNDIISYM RDEFKILIGE RTAEMVKIEI GSAMPGGYME TEVHGRDLLT
     GLPREVVVTD ADIREALSLS VRGLIDGVKD MLESTPPEIL SDIMHRGITL SGGGALLPGL
     SELLQNALKI PVYVVEDPLS AVARGTGVIL DNLPMYQEVL IGHQDELPPR
//
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