ID E3C640_9LACO Unreviewed; 331 AA.
AC E3C640;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=Cell shape-determining protein MreB {ECO:0000256|HAMAP-Rule:MF_02207};
GN Name=mbl {ECO:0000313|EMBL:EFQ53808.1};
GN Synonyms=mreB {ECO:0000256|HAMAP-Rule:MF_02207};
GN ORFNames=HMPREF9265_1343 {ECO:0000313|EMBL:EFQ53808.1};
OS Limosilactobacillus oris PB013-T2-3.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Limosilactobacillus.
OX NCBI_TaxID=908339 {ECO:0000313|EMBL:EFQ53808.1, ECO:0000313|Proteomes:UP000003070};
RN [1] {ECO:0000313|EMBL:EFQ53808.1, ECO:0000313|Proteomes:UP000003070}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB013-T2-3 {ECO:0000313|EMBL:EFQ53808.1,
RC ECO:0000313|Proteomes:UP000003070};
RA Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G.,
RA Nelson K.E.;
RL Submitted (OCT-2010) 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:EFQ53808.1}.
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DR EMBL; AEKL01000018; EFQ53808.1; -; Genomic_DNA.
DR RefSeq; WP_003711629.1; NZ_AEKL01000018.1.
DR AlphaFoldDB; E3C640; -.
DR eggNOG; COG1077; Bacteria.
DR OrthoDB; 9768127at2; -.
DR Proteomes; UP000003070; 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; -; 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}.
FT BINDING 11..13
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT BINDING 155..157
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT BINDING 203..206
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
SQ SEQUENCE 331 AA; 35459 MW; A5A6B2E36A8E97BE CRC64;
MAKDIGIDLG TANVLIYVQG KGIVLNEPSV VAIDTQTNKV LAVGSEAYRM VGRTPSNIRA
IRPLKNGVIS DFDVTQEMLS YFIGKLSVKG FMSKPNIMIC APTNITEIER KAIIQAAEQS
GGGKVYLEYE PKVAAIGAGL DIFKPRGSMV IDMGGGTSDI AILSLGDIVA SQSIRLAGDK
MNSNIAAYIK DKHGLVIGEH TAENIKMEIG TALQVDDPKE MDVRGRDVAS GMPKQITVNQ
NEIEEALHDT LDQIVTATIN VLETIPPELA SDIIDRGIVL TGGTSLLNGL DQLFSSRLKV
PVVVSQDPLD NVAKGAGEML ERMQKTDSKK K
//
