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Database: UniProt
Entry: A0A410Q7I5_9FIRM
LinkDB: A0A410Q7I5_9FIRM
Original site: A0A410Q7I5_9FIRM 
ID   A0A410Q7I5_9FIRM        Unreviewed;       341 AA.
AC   A0A410Q7I5;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 20.
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=EQM14_07610 {ECO:0000313|EMBL:QAT51271.1};
OS   Caproiciproducens sp. NJN-50.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Caproiciproducens.
OX   NCBI_TaxID=2507162 {ECO:0000313|EMBL:QAT51271.1, ECO:0000313|Proteomes:UP000287564};
RN   [1] {ECO:0000313|EMBL:QAT51271.1, ECO:0000313|Proteomes:UP000287564}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NJN-50 {ECO:0000313|EMBL:QAT51271.1,
RC   ECO:0000313|Proteomes:UP000287564};
RA   Ma S.;
RT   "Draft genomes of a novel of Caproiciproducens strains.";
RL   Submitted (JAN-2019) 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}.
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DR   EMBL; CP035283; QAT51271.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A410Q7I5; -.
DR   KEGG; capr:EQM14_07610; -.
DR   OrthoDB; 9768127at2; -.
DR   Proteomes; UP000287564; Chromosome.
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:UP000287564}.
FT   BINDING         155..157
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
SQ   SEQUENCE   341 AA;  36381 MW;  9EB3BAE2163133A6 CRC64;
     MLGTDLAIDL GTSTTKIYLD GKGIVLNEPS VAAVNVETGE VVATGKEAYT MIGKTSDKIK
     VCLPLEGGVI SDFDMAQYLI GTYLKKVSQS HVVMPRVVVS VPCKITEVEK RAVVDAISSA
     GVRKICLIEE PVAAALGAGV DISQPHGTLV VDIGGGTTDM AVLSLSGIAI SRSVKVAGNT
     FNEAIVKYIR RKYNLIIGRR MAENAKLAIG CVYPRKDVSS FRVKGRNAMT GLPQWADITS
     DEILEALIEN VMQMIRVIQE MLEKTPPELI GDVYSDGMIL TGGSAQLFGF DSLISKKAKM
     PVHVADDPQN CVAVGAGKAI RFIDDMENKA YGVLNPLSAA Y
//
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