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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
 
 
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