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Database: UniProt
Entry: A0A0M8VQ07_9ACTN
LinkDB: A0A0M8VQ07_9ACTN
Original site: A0A0M8VQ07_9ACTN 
ID   A0A0M8VQ07_9ACTN        Unreviewed;       341 AA.
AC   A0A0M8VQ07;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 29.
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=ADK64_08170 {ECO:0000313|EMBL:KOV67957.1};
OS   Streptomyces sp. MMG1121.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1415544 {ECO:0000313|EMBL:KOV67957.1, ECO:0000313|Proteomes:UP000037687};
RN   [1] {ECO:0000313|Proteomes:UP000037687}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MMG1121 {ECO:0000313|Proteomes:UP000037687};
RA   Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL   Submitted (JUL-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:KOV67957.1}.
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DR   EMBL; LGDV01000074; KOV67957.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M8VQ07; -.
DR   STRING; 1415544.ADK64_08170; -.
DR   PATRIC; fig|1415544.3.peg.1742; -.
DR   Proteomes; UP000037687; 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; -; 3.
DR   HAMAP; MF_02207; MreB; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR004753; MreB.
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:UP000037687}.
FT   BINDING         290..293
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
SQ   SEQUENCE   341 AA;  36016 MW;  2809D9475F1F7A4C CRC64;
     MEQLRRCHFA VDLGAARTRV YVKGAGLVVD QPSAAAVNTR TGALIAVGEF AERMTGRTPS
     YIRVVRPISG GTVVDIEMAQ RMLRQLLGDK MRRALRRNLR LRAAACTPHD TDPLAQRATI
     ETLVGLGARR VELVDTLIAA AVGCGLPVER PEATMIMVCG AAATQVAVLS LGSIVTAERI
     PVGGEAVDHA IVQHLRHEHE LILPSQSVRP LQLALSGNGL TSQGPASTEI HGRDVATGLA
     RSVQVDTAAV RDAIQTPLTA VLDGIGKVLR GCPPDLVADL ADRGIMMVGG SALLPGFDQM
     LRQATRMPVH IAERPDICAA QGIGAMLEGR IEPLVLNPLA A
//
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