ID A0A0F7M3H5_9GAMM Unreviewed; 345 AA.
AC A0A0F7M3H5;
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=IMCC21906_01168 {ECO:0000313|EMBL:AKH68847.1};
OS Spongiibacter sp. IMCC21906.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Spongiibacteraceae; Spongiibacter.
OX NCBI_TaxID=1620392 {ECO:0000313|EMBL:AKH68847.1, ECO:0000313|Proteomes:UP000035013};
RN [1] {ECO:0000313|EMBL:AKH68847.1, ECO:0000313|Proteomes:UP000035013}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMCC21906 {ECO:0000313|EMBL:AKH68847.1,
RC ECO:0000313|Proteomes:UP000035013};
RA Cho J.-C., Yang S.-J., Kang I.;
RT "Complete genome sequence of IMCC21906 belonging to the
RT Gammaproteobacteria.";
RL Submitted (MAY-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}.
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DR EMBL; CP011477; AKH68847.1; -; Genomic_DNA.
DR RefSeq; WP_047011363.1; NZ_CP011477.1.
DR AlphaFoldDB; A0A0F7M3H5; -.
DR STRING; 1620392.IMCC21906_01168; -.
DR KEGG; spoi:IMCC21906_01168; -.
DR PATRIC; fig|1620392.3.peg.1226; -.
DR OrthoDB; 9768127at2; -.
DR Proteomes; UP000035013; 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; -; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000035013}.
FT BINDING 19..21
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="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 294..297
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
SQ SEQUENCE 345 AA; 37098 MW; 9FFFC93FB58D51EB CRC64;
MLKRIRGMFS NDLSIDLGTA NTLIYVRGQG IVLDEPSVVA IRVHNGQKTI EAVGIEAKRM
LGRTPGNITA IRPLKDGVIA DFQVTEKMLQ HFIKLVHQNS FIRPSPRVLV SVPCKSTQVE
RRAIRESVLS AGAREVRLIE EPMAAAIGAG LRVEEASGSM VVDIGGGTTE IAIISLNGVV
YSDSVRVGGD RFDEAIVTHV RRTYGSLIGD ATAERIKQEI GCAYPGSELL EIDVRGRNLA
EGIPRRFTLN SDEILEALQE PLQVIIQGVK RALEQSPPEL AADIAETGIV LTGGGALLRG
IDQLLADESA LPVIIAEDPL SCVARGGGKA LEMIDRHHLD ILSAE
//
