ID A0A3G9J1M4_9FIRM Unreviewed; 329 AA.
AC A0A3G9J1M4;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Cell shape-determining protein MreB {ECO:0000256|HAMAP-Rule:MF_02207};
GN Name=mbl_1 {ECO:0000313|EMBL:BBH25087.1};
GN Synonyms=mreB {ECO:0000256|HAMAP-Rule:MF_02207};
GN ORFNames=SG0102_00210 {ECO:0000313|EMBL:BBH25087.1};
OS Intestinibaculum porci.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Erysipelotrichaceae; Intestinibaculum.
OX NCBI_TaxID=2487118 {ECO:0000313|EMBL:BBH25087.1, ECO:0000313|Proteomes:UP000268059};
RN [1] {ECO:0000313|EMBL:BBH25087.1, ECO:0000313|Proteomes:UP000268059}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG0102 {ECO:0000313|EMBL:BBH25087.1,
RC ECO:0000313|Proteomes:UP000268059};
RA Kim J.S., Choe H., Lee Y.R., Kim K.M., Park D.S.;
RT "Novel Erysipelotrichaceae bacterium isolated from small intestine of a
RT swine.";
RL Submitted (NOV-2018) 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}.
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DR EMBL; AP019309; BBH25087.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3G9J1M4; -.
DR KEGG; ebm:SG0102_00210; -.
DR InParanoid; A0A3G9J1M4; -.
DR OrthoDB; 9768127at2; -.
DR Proteomes; UP000268059; 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:SF4; CELL SHAPE-DETERMINING PROTEIN MBL; 1.
DR PANTHER; PTHR42749; 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:UP000268059}.
FT BINDING 13..15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT BINDING 157..159
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT BINDING 205..208
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT BINDING 285..288
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
SQ SEQUENCE 329 AA; 35162 MW; 58577C5516B354EF CRC64;
MSLSKEIGID LGTANILIYL KGTGIVVNEP SVVTINTETN KPVAVGEEAR EMLGKTPGRL
KAIRPLKDGV IADFQITEIL ITHFINKLNL KGLFSRPVIL ICCPSNITSI EKSAIQDVAL
RCGAKRVYIE EEPKVAAIGA GLDISKPSGN MVVDIGGGTT DVAVLSLGDI VTSQSLKIAG
NRMDSEIVKY VKDKYKLLIG DSTAEHVKMQ IGCAFDGDPD NKVDCRGRDI VTGLPKTIQI
SEAEVEEALH EVCAAILASA KQVLEQTPPE LSADIVNKGV FLTGGGALLH NLDKFMEQGL
KVPVFVADHP LNCVAEGCGV MLENTEYLQ
//
