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Database: UniProt
Entry: A0A0G0B2H2_9BACT
LinkDB: A0A0G0B2H2_9BACT
Original site: A0A0G0B2H2_9BACT 
ID   A0A0G0B2H2_9BACT        Unreviewed;       412 AA.
AC   A0A0G0B2H2;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 28.
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=UR51_C0010G0012 {ECO:0000313|EMBL:KKP57856.1};
OS   Candidatus Moranbacteria bacterium GW2011_GWF1_34_10.
OC   Bacteria; Candidatus Moranbacteria.
OX   NCBI_TaxID=1618715 {ECO:0000313|EMBL:KKP57856.1, ECO:0000313|Proteomes:UP000034605};
RN   [1] {ECO:0000313|EMBL:KKP57856.1, ECO:0000313|Proteomes:UP000034605}
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: 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:KKP57856.1}.
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DR   EMBL; LBPM01000010; KKP57856.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0B2H2; -.
DR   STRING; 1618715.UR51_C0010G0012; -.
DR   PATRIC; fig|1618715.3.peg.867; -.
DR   Proteomes; UP000034605; 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         80..82
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT   BINDING         226..228
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT   BINDING         274..277
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT   BINDING         354..357
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
SQ   SEQUENCE   412 AA;  45252 MW;  5F080461A17E33EC CRC64;
     MICLGFQLVF RSEFQSFIKT RYFRQFLSKN KNNSLNKRPL SNYFSRGFVY MFKKIRNVYL
     KITGKIFGKF SKDIGIDLGT ANTLVYVGGK GIVINEPSVV AINKKTGQIL AIGKKAKQMV
     GKTPSHIVAT RPLVDGVISD FEVTEQMLRY FIDKVHQDSF SILPRPRVLI GIPSEVTEVE
     KRAVIDAAIS AGAREAYIID EPMAAAIGAH LPVTTAAGNM IVDIGGGTAE IAVISLGGVV
     SSRSLRIAGD EMNEDIVRYC RDEFNLLIGE RTAEDIKISI GSAYPLEKKL TMDIRGRDLV
     SGLPKKIKVN DEQIREALSR SIRIIVNNIK IIIEDTPPEL IADIMQRGII LAGGGSLIRG
     LDNLIANQTG ISVRTMEDPL TAVVRGTGIV LEDLESLKEV LAANQYDDSP LR
//
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