MREB_ECOL6
ID MREB_ECOL6 Reviewed; 347 AA.
AC P0A9X5; P13519; P76678;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Cell shape-determining protein MreB {ECO:0000255|HAMAP-Rule:MF_02207};
GN Name=mreB {ECO:0000255|HAMAP-Rule:MF_02207}; OrderedLocusNames=c4006;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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:0000255|HAMAP-Rule:MF_02207}.
CC -!- SUBUNIT: Forms polymers. {ECO:0000255|HAMAP-Rule:MF_02207}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02207}.
CC Note=Membrane-associated. {ECO:0000255|HAMAP-Rule:MF_02207}.
CC -!- SIMILARITY: Belongs to the FtsA/MreB family. {ECO:0000255|HAMAP-
CC Rule:MF_02207, ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAN82446.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE014075; AAN82446.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_000913396.1; NC_004431.1.
DR AlphaFoldDB; P0A9X5; -.
DR SMR; P0A9X5; -.
DR STRING; 199310.c4006; -.
DR EnsemblBacteria; AAN82446; AAN82446; c4006.
DR GeneID; 64728064; -.
DR GeneID; 67517865; -.
DR KEGG; ecc:c4006; -.
DR eggNOG; COG1077; Bacteria.
DR HOGENOM; CLU_052037_0_0_6; -.
DR OMA; MVICIPS; -.
DR Proteomes; UP000001410; 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 HAMAP; MF_02207; MreB; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR004753; MreB.
DR PRINTS; PR01652; SHAPEPROTEIN.
DR SUPFAM; SSF53067; SSF53067; 2.
DR TIGRFAMs; TIGR00904; mreB; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell shape; Cytoplasm; Nucleotide-binding.
FT CHAIN 1..347
FT /note="Cell shape-determining protein MreB"
FT /id="PRO_0000062760"
FT BINDING 19..21
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02207"
FT BINDING 168..170
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02207"
FT BINDING 216..219
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02207"
FT BINDING 296..299
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02207"
SQ SEQUENCE 347 AA; 36952 MW; 1393696D8CDAEF93 CRC64;
MLKKFRGMFS NDLSIDLGTA NTLIYVKGQG IVLNEPSVVA IRQDRAGSPK SVAAVGHDAK
QMLGRTPGNI AAIRPMKDGV IADFFVTEKM LQHFIKQVHS NSFMRPSPRV LVCVPVGATQ
VERRAIRESA QGAGAREVFL IEEPMAAAIG AGLPVSEATG SMVVDIGGGT TEVAVISLNG
VVYSSSVRIG GDRFDEAIIN YVRRNYGSLI GEATAERIKH EIGSAYPGDE VREIEVRGRN
LAEGVPRGFT LNSNEILEAL QEPLTGIVSA VMVALEQCPP ELASDISERG MVLTGGGALL
RNLDRLLMEE TGIPVVVAED PLTCVARGGG KALEMIDMHG GDLFSEE