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Database: UniProt
Entry: A0A1X6ZW77_9RHOB
LinkDB: A0A1X6ZW77_9RHOB
Original site: A0A1X6ZW77_9RHOB 
ID   A0A1X6ZW77_9RHOB        Unreviewed;       348 AA.
AC   A0A1X6ZW77;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=Cell shape-determining protein MreB {ECO:0000256|HAMAP-Rule:MF_02207};
GN   Name=mreB {ECO:0000256|HAMAP-Rule:MF_02207,
GN   ECO:0000313|EMBL:SLN63183.1};
GN   ORFNames=PSM7751_03235 {ECO:0000313|EMBL:SLN63183.1};
OS   Pseudooceanicola marinus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Pseudooceanicola.
OX   NCBI_TaxID=396013 {ECO:0000313|EMBL:SLN63183.1, ECO:0000313|Proteomes:UP000193963};
RN   [1] {ECO:0000313|EMBL:SLN63183.1, ECO:0000313|Proteomes:UP000193963}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 7751 {ECO:0000313|EMBL:SLN63183.1,
RC   ECO:0000313|Proteomes:UP000193963};
RA   Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA   Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL   Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
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; FWFN01000006; SLN63183.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X6ZW77; -.
DR   OrthoDB; 9768127at2; -.
DR   Proteomes; UP000193963; Unassembled WGS sequence.
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:UP000193963}.
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;  36867 MW;  103CC7A9EA2E8C15 CRC64;
     MGIFDKMPGL FSSDMAIDLG TANTLVYVKG RGVILSEPSV VAYHVKDGVK KVLAVGEDAK
     LMLGRTPGSI EAIRPMREGV IADFDVAEEM IKHFIRKVHK RSTFSKPKII VCVPHGATPV
     EKRAIRQSVL SAGARRAGLI AEPIAAAIGA GMPITDPTGN MVVDIGGGTT EVAVLSLGDI
     VYARSVRVGG DRMDEAIISY LRRQQNLLIG ESTAERIKTS IGTARMPDDG RGASMQVRGR
     DLLNGVPKET EITQAQVAEA LAEPVQQICE AVMTALEATP PDLAADIVDR GVMLTGGGAL
     LGDLDLALRE QTGLGVSIAD ESLNCVALGT GKALEYEKQL RHAIDYDS
//
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