MREB_PASMU
ID MREB_PASMU Reviewed; 351 AA.
AC Q9L6A3;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Cell shape-determining protein MreB {ECO:0000255|HAMAP-Rule:MF_02207};
GN Name=mreB {ECO:0000255|HAMAP-Rule:MF_02207}; OrderedLocusNames=PM1955;
OS Pasteurella multocida (strain Pm70).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Pasteurella.
OX NCBI_TaxID=272843;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10873488; DOI=10.1006/mpat.2000.0365;
RA Fuller T.E., Kennedy M.J., Lowery D.E.;
RT "Identification of Pasteurella multocida virulence genes in a septicemic
RT mouse model using signature-tagged mutagenesis.";
RL Microb. Pathog. 29:25-38(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pm70;
RX PubMed=11248100; DOI=10.1073/pnas.051634598;
RA May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT "Complete genomic sequence of Pasteurella multocida Pm70.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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}.
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DR EMBL; AF237936; AAF68422.1; -; Genomic_DNA.
DR EMBL; AE004439; AAK04039.1; -; Genomic_DNA.
DR RefSeq; WP_005719450.1; NC_002663.1.
DR AlphaFoldDB; Q9L6A3; -.
DR SMR; Q9L6A3; -.
DR STRING; 747.DR93_2143; -.
DR PRIDE; Q9L6A3; -.
DR EnsemblBacteria; AAK04039; AAK04039; PM1955.
DR GeneID; 62225904; -.
DR KEGG; pmu:PM1955; -.
DR HOGENOM; CLU_052037_0_0_6; -.
DR OMA; MVICIPS; -.
DR Proteomes; UP000000809; 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; Reference proteome.
FT CHAIN 1..351
FT /note="Cell shape-determining protein MreB"
FT /id="PRO_0000062762"
FT BINDING 20..22
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02207"
FT BINDING 169..171
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02207"
FT BINDING 217..220
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02207"
FT BINDING 299..302
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02207"
SQ SEQUENCE 351 AA; 37415 MW; CD1EDCCBEABD5D1E CRC64;
MLFKKIRGLF SNDLSIDLGT ANTLIYVKGQ GIVLDEPSVV AIRQERSGAL KSIAAVGRDA
KLMLGRTPKS IAAIRPMKDG VIADFFVTEK MLQYFIKQVH SSNFMRPSPR VLVCVPAGAT
QVERRAIKES AIGAGAREVY LIEEPMAAAI GAKLPVSTAT GSMVIDIGGG TTEVAVISLN
GIVYSSSVRI GGDRFDEAII SYVRKTFGSI IGEPTAERIK QEIGSAFIQE GDEVREIEVH
GHNLAEGAPR SFKLTSRDVL EAIQAPLNGI VAAVRTALEE CQPEHAADIF ERGMVLTGGG
ALIRNIDVLL SKETGVPVII ADDPLTCVAR GGGEALEMID MHGGDIFSDD I