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
//