ID A0A090KTX7_9BACI Unreviewed; 338 AA.
AC A0A090KTX7;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=Cell shape-determining protein MreB {ECO:0000256|HAMAP-Rule:MF_02207};
GN Name=mreB {ECO:0000256|HAMAP-Rule:MF_02207,
GN ECO:0000313|EMBL:CEE02179.1};
GN ORFNames=B4064_1574 {ECO:0000313|EMBL:KIO68927.1}, B4065_3420
GN {ECO:0000313|EMBL:KIO62200.1}, B4166_0831
GN {ECO:0000313|EMBL:KIO61081.1}, B4167_0866
GN {ECO:0000313|EMBL:KIO70174.1}, BT1A1_2359
GN {ECO:0000313|EMBL:CEE02179.1}, CQJ30_13005
GN {ECO:0000313|EMBL:AWI12994.1};
OS Caldibacillus thermoamylovorans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Caldibacillus.
OX NCBI_TaxID=35841 {ECO:0000313|EMBL:CEE02179.1, ECO:0000313|Proteomes:UP000040576};
RN [1] {ECO:0000313|EMBL:CEE02179.1, ECO:0000313|Proteomes:UP000040576}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wibberg Daniel;
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000032071, ECO:0000313|Proteomes:UP000032076}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B4064 {ECO:0000313|EMBL:KIO68927.1,
RC ECO:0000313|Proteomes:UP000032078}, B4065
RC {ECO:0000313|EMBL:KIO62200.1, ECO:0000313|Proteomes:UP000032071},
RC B4166 {ECO:0000313|EMBL:KIO61081.1,
RC ECO:0000313|Proteomes:UP000032097}, and B4167
RC {ECO:0000313|EMBL:KIO70174.1, ECO:0000313|Proteomes:UP000032076};
RA Krawcyk A.O., Berendsen E.M., Eijlander R.T., de Jong A., Wells-Bennik M.,
RA Kuipers O.P.;
RT "Draft Genome Sequences of Four Bacillus thermoamylovorans Strains,
RT Isolated From Food Products.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:AWI12994.1, ECO:0000313|Proteomes:UP000244914}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SSBM {ECO:0000313|EMBL:AWI12994.1,
RC ECO:0000313|Proteomes:UP000244914};
RX PubMed=29625286; DOI=10.1016/j.biortech.2018.03.121;
RA Cai L., Zheng S.W., Shen Y.J., Zheng G.D., Liu H.T., Wu Z.Y.;
RT "Complete genome sequence provides insights into the biodrying-related
RT microbial function of Bacillus thermoamylovorans isolated from sewage
RT sludge biodrying material.";
RL Bioresour. Technol. 260:141-149(2018).
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; CP023704; AWI12994.1; -; Genomic_DNA.
DR EMBL; CCRF01000066; CEE02179.1; -; Genomic_DNA.
DR EMBL; JXLT01000142; KIO61081.1; -; Genomic_DNA.
DR EMBL; JXLS01000097; KIO62200.1; -; Genomic_DNA.
DR EMBL; JXLR01000016; KIO68927.1; -; Genomic_DNA.
DR EMBL; JXLU01000147; KIO70174.1; -; Genomic_DNA.
DR RefSeq; WP_034771430.1; NZ_JXLU01000147.1.
DR AlphaFoldDB; A0A090KTX7; -.
DR STRING; 35841.B4167_0866; -.
DR KEGG; bthv:CQJ30_13005; -.
DR PATRIC; fig|35841.6.peg.776; -.
DR eggNOG; COG1077; Bacteria.
DR OrthoDB; 9768127at2; -.
DR Proteomes; UP000032071; Unassembled WGS sequence.
DR Proteomes; UP000032076; Unassembled WGS sequence.
DR Proteomes; UP000032078; Unassembled WGS sequence.
DR Proteomes; UP000032097; Unassembled WGS sequence.
DR Proteomes; UP000040576; Unassembled WGS sequence.
DR Proteomes; UP000244914; 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:UP000040576}.
FT BINDING 15..17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT BINDING 161..163
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT BINDING 209..212
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT BINDING 289..292
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
SQ SEQUENCE 338 AA; 36039 MW; 135EB7DE3EC01ABF CRC64;
MFGIGSKDLG IDLGTANTLV YIRGKGVVLR EPSVVAYQTD TKQIVAVGND AKNMIGRTPG
NVVALRPMKD GVIADYETTA KMMKYFINQA LKNKGGFGRK PYVMVCVPSG ITAVEERAVI
DATRQAGARD AYTIEEPFAA AIGADLPVWE PTGSMVVDIG GGTTEVAIIS LGGIVTSQSI
RIAGDEMDDS IITYIRKNYN LMIGDRTAET IKMEVGSAGM PEGIGNMEIR GRDLLTGLPK
TIEVTPEEIA EALKDTVFAI VEAVKNTLEK TPPELAADIM DRGIVLTGGG ALLRNLDRVI
ANETNMPVLI AENPLDCVAI GTGKALEHID LFKNKVRG
//