ID A0A143WR03_9ENTR Unreviewed; 347 AA.
AC A0A143WR03;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
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:CUX96148.1};
GN ORFNames=FVIR_GE00283 {ECO:0000313|EMBL:CUX96148.1};
OS Candidatus Gullanella endobia.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Gullanella.
OX NCBI_TaxID=1070130 {ECO:0000313|EMBL:CUX96148.1, ECO:0000313|Proteomes:UP000095665};
RN [1] {ECO:0000313|Proteomes:UP000095665}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Husnik F.;
RL Submitted (JAN-2016) 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; LN999832; CUX96148.1; -; Genomic_DNA.
DR RefSeq; WP_067498000.1; NZ_LN999832.1.
DR AlphaFoldDB; A0A143WR03; -.
DR STRING; 1070130.FVIR_GE00283; -.
DR KEGG; ged:FVIR_GE00283; -.
DR PATRIC; fig|1070130.3.peg.456; -.
DR OrthoDB; 9768127at2; -.
DR Proteomes; UP000095665; Chromosome i.
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:UP000095665}.
FT BINDING 19..21
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT BINDING 168..170
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT BINDING 216..219
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT BINDING 296..299
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
SQ SEQUENCE 347 AA; 36968 MW; 1A8BAE00DD637406 CRC64;
MFKKFRGIFS NDLSIDLGTA NTLIYVKGQG IVLNEPSVVA IRQDRAGSPK SVAAVGHEAK
QMLGRTPGNI AAIRPMKDGV IADFFVTEKM LQHFIKQVHS NSLMRPSPRV LVCVPVGATQ
VERRAIRESA QGAGAREVFL IEEPMAAAIG AGLPVSEATG SMVVDIGGGT TEVAVISLNG
VVYSSSVRIG GDRFDESIIN YVRRNYGSLI GEATAERIKH SIGSAYLDDE VHEIEVRGRN
LAEGVPRGFT LHSNEILEAL QEPLTGIVSA VMVALEQCPP ELASDISERG MVLTGGGALL
LNLDLLLMEE TGIPVIIAED PLTCVARGGG KALEMIDMYG GDFLSEE
//
