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Database: UniProt
Entry: A0A0M2U4F6_9FIRM
LinkDB: A0A0M2U4F6_9FIRM
Original site: A0A0M2U4F6_9FIRM 
ID   A0A0M2U4F6_9FIRM        Unreviewed;       344 AA.
AC   A0A0M2U4F6;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-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=SY88_11790 {ECO:0000313|EMBL:KKM10764.1};
OS   Clostridiales bacterium PH28_bin88.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales.
OX   NCBI_TaxID=1605376 {ECO:0000313|EMBL:KKM10764.1, ECO:0000313|Proteomes:UP000034222};
RN   [1] {ECO:0000313|EMBL:KKM10764.1, ECO:0000313|Proteomes:UP000034222}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Robbins S., Tyson G.;
RT   "High quality genome sequence of Candidatus Suratobacter aromatica.";
RL   Submitted (MAR-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: 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:KKM10764.1}.
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DR   EMBL; LAKY01000049; KKM10764.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M2U4F6; -.
DR   STRING; 1605376.SY88_11790; -.
DR   PATRIC; fig|1605376.3.peg.2164; -.
DR   Proteomes; UP000034222; 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:UP000034222}.
FT   BINDING         158..160
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT   BINDING         206..209
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT   BINDING         288..291
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
SQ   SEQUENCE   344 AA;  36418 MW;  9C703590ADEEF3F0 CRC64;
     MFGWNMDIGV DLGTASVLVY VKGKGIVLNE PSVVAIDKTT GQIIAVGEDA RRMLGRTPGN
     IVAIRPLREG VIADYDTTER MLRYFIEKAC GRRMFFRPRV MVCIPAGVTS VEERAVRQAT
     MQAGAKQAYL IEEPLAAALG AGLDISEASG SIVVDIGGGT ADIAVLSLGG IVVSKSLRVG
     GDKFDEAVVR YIRREYNLMV GERTAEELKI TVGTAFPEGK VGETSMEIRG RDLVSGLPKT
     VTVTSQQAWE AMQEPVEAVI AGVKEVLERT PPELASDIIN KGIVLTGGGS LLNGLDTLLS
     KRTGLPVHVA DDAISCVALG TGKALSMLHV LQSSGVVAAT RKIV
//
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