ID A0A0X1RY37_9BACL Unreviewed; 330 AA.
AC A0A0X1RY37;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, 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=ASO14_457 {ECO:0000313|EMBL:AMA63446.1};
OS Kurthia sp. 11kri321.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Kurthia.
OX NCBI_TaxID=1750719 {ECO:0000313|EMBL:AMA63446.1, ECO:0000313|Proteomes:UP000058129};
RN [1] {ECO:0000313|EMBL:AMA63446.1, ECO:0000313|Proteomes:UP000058129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=11kri321 {ECO:0000313|EMBL:AMA63446.1,
RC ECO:0000313|Proteomes:UP000058129};
RA Zhang Y., Guo Z.;
RL Submitted (NOV-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}.
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DR EMBL; CP013217; AMA63446.1; -; Genomic_DNA.
DR RefSeq; WP_068450887.1; NZ_CP013217.1.
DR AlphaFoldDB; A0A0X1RY37; -.
DR STRING; 1750719.ASO14_457; -.
DR KEGG; kur:ASO14_457; -.
DR PATRIC; fig|1750719.3.peg.435; -.
DR OrthoDB; 9768127at2; -.
DR Proteomes; UP000058129; 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:UP000058129}.
FT BINDING 13..15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT BINDING 158..160
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT BINDING 206..209
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
SQ SEQUENCE 330 AA; 34926 MW; 451D1248EF5FE26D CRC64;
MFTSSALGID LGTANTLVYV KNKGIILNEP SVVAVNTTTK QVIAIGHEAK AMIGKTPPNI
TVCHPLKDGV IADFDMATAL LKTILDRVFK DKGRFKKPNI VICAPSGATS IERLAIQDAA
RQCGAKEAFL IDEPVAAAIG AELPVNEPTA SAIVDLGGGT TEVGIISLGG IVTTATAKIG
GDSINDDIIH YLRKEFNLLI GAKTAEEIKI EIGHAPIEHA VAQMTVTGRD LVTGLPRSIT
IDSMQLQDCL SETFQAILEL IRRTLESCPP ELAGDIVERG IVLAGGTSLL QGLDEWLANE
LFIPVYRAQS PLEAVAIGTG LSTETLHYLK
//
