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Database: UniProt
Entry: Q1GJG0_RUEST
LinkDB: Q1GJG0_RUEST
Original site: Q1GJG0_RUEST 
ID   Q1GJG0_RUEST            Unreviewed;       348 AA.
AC   Q1GJG0;
DT   27-JUN-2006, integrated into UniProtKB/TrEMBL.
DT   27-JUN-2006, sequence version 1.
DT   27-MAR-2024, entry version 96.
DE   RecName: Full=Cell shape-determining protein MreB {ECO:0000256|HAMAP-Rule:MF_02207};
GN   Name=mreB {ECO:0000256|HAMAP-Rule:MF_02207};
GN   OrderedLocusNames=TM1040_0473 {ECO:0000313|EMBL:ABF63206.1};
OS   Ruegeria sp. (strain TM1040) (Silicibacter sp.).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Ruegeria.
OX   NCBI_TaxID=292414 {ECO:0000313|EMBL:ABF63206.1, ECO:0000313|Proteomes:UP000000636};
RN   [1] {ECO:0000313|Proteomes:UP000000636}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TM1040 {ECO:0000313|Proteomes:UP000000636};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Brettin T., Bruce D., Han C., Tapia R., Goodwin L., Thompson L.S.,
RA   Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Belas R., Moran M.A., Buchan A., Gonzalez J.M., Schell M.A., Sun F.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Silicibacter sp. TM1040.";
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ABF63206.1, ECO:0000313|Proteomes:UP000000636}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TM1040 {ECO:0000313|EMBL:ABF63206.1,
RC   ECO:0000313|Proteomes:UP000000636};
RX   PubMed=17526795; DOI=10.1128/AEM.02580-06;
RA   Moran M.A., Belas R., Schell M.A., Gonzalez J.M., Sun F., Sun S.,
RA   Binder B.J., Edmonds J., Ye W., Orcutt B., Howard E.C., Meile C.,
RA   Palefsky W., Goesmann A., Ren Q., Paulsen I., Ulrich L.E., Thompson L.S.,
RA   Saunders E., Buchan A.;
RT   "Ecological genomics of marine Roseobacters.";
RL   Appl. Environ. Microbiol. 73:4559-4569(2007).
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; CP000377; ABF63206.1; -; Genomic_DNA.
DR   RefSeq; WP_011537821.1; NC_008044.1.
DR   AlphaFoldDB; Q1GJG0; -.
DR   STRING; 292414.TM1040_0473; -.
DR   KEGG; sit:TM1040_0473; -.
DR   eggNOG; COG1077; Bacteria.
DR   HOGENOM; CLU_052037_0_0_5; -.
DR   OrthoDB; 9768127at2; -.
DR   Proteomes; UP000000636; 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   Gene3D; 3.30.420.40; -; 2.
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:UP000000636}.
FT   BINDING         21..23
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT   BINDING         167..169
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT   BINDING         215..218
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT   BINDING         297..300
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
SQ   SEQUENCE   348 AA;  36792 MW;  1B384156B76DEF1E CRC64;
     MALFGNLGGL FTSDMAIDLG TANTLVYVKG RGVILSEPSV VAYHVKDGVK KVLAVGEDAK
     LMLGRTPGSI EAIRPMREGV IADFDTAEEM IKHFIRKVHK RSTFSKPKVI VCVPHGATPV
     EKRAIRSSVL AAGARRAGLI AEPIAAAIGA GMPITDPTGN MVVDIGGGTT EVAVLSLGDI
     VYARSVRVGG DRMDEAIISY LRRQQNLLIG EATAERIKTS IGTARMPDDG RGQSMQIRGR
     DLLNGVPKEI EISQAQVAEA LAEPVQQICE AVMTALETTP PDLAADIVDR GVMLTGGGAL
     LGDLDLALRE QTGLAVSIAD ESLNCVALGT GKALEYEKQL RHAIDYDS
//
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