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MREB_SHIFL
ID   MREB_SHIFL              Reviewed;         347 AA.
AC   P0A9X8; P13519; P76678;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Cell shape-determining protein MreB {ECO:0000255|HAMAP-Rule:MF_02207};
GN   Name=mreB {ECO:0000255|HAMAP-Rule:MF_02207};
GN   OrderedLocusNames=SF3289, S3506;
OS   Shigella flexneri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA   Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA   Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA   Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA   Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA   Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella flexneri
RT   serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(2003).
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=AAN44753.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAP18564.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AE005674; AAN44753.2; ALT_INIT; Genomic_DNA.
DR   EMBL; AE014073; AAP18564.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_709046.4; NC_004337.2.
DR   RefSeq; WP_000913396.1; NZ_WPGW01000026.1.
DR   AlphaFoldDB; P0A9X8; -.
DR   SMR; P0A9X8; -.
DR   STRING; 198214.SF3289; -.
DR   EnsemblBacteria; AAN44753; AAN44753; SF3289.
DR   EnsemblBacteria; AAP18564; AAP18564; S3506.
DR   GeneID; 1026494; -.
DR   GeneID; 64728064; -.
DR   GeneID; 67517865; -.
DR   KEGG; sfl:SF3289; -.
DR   KEGG; sfx:S3506; -.
DR   PATRIC; fig|198214.7.peg.3896; -.
DR   HOGENOM; CLU_052037_0_0_6; -.
DR   OrthoDB; 410781at2; -.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; 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..347
FT                   /note="Cell shape-determining protein MreB"
FT                   /id="PRO_0000062765"
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
 
 
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