ID A0A227PHY0_9FLAO Unreviewed; 342 AA.
AC A0A227PHY0;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Cell shape-determining protein MreB {ECO:0000256|HAMAP-Rule:MF_02207};
GN Name=mreB {ECO:0000256|HAMAP-Rule:MF_02207};
GN ORFNames=B0A64_01835 {ECO:0000313|EMBL:OXG09520.1};
OS Flavobacterium araucananum.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=946678 {ECO:0000313|EMBL:OXG09520.1, ECO:0000313|Proteomes:UP000214684};
RN [1] {ECO:0000313|EMBL:OXG09520.1, ECO:0000313|Proteomes:UP000214684}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24704 {ECO:0000313|EMBL:OXG09520.1,
RC ECO:0000313|Proteomes:UP000214684};
RA Stine C., Li C., Tadesse D.;
RT "Whole genomes of Flavobacteriaceae.";
RL Submitted (NOV-2016) 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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_02207}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OXG09520.1}.
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DR EMBL; MUGS01000002; OXG09520.1; -; Genomic_DNA.
DR RefSeq; WP_007804822.1; NZ_QGGJ01000001.1.
DR AlphaFoldDB; A0A227PHY0; -.
DR OrthoDB; 9768127at2; -.
DR Proteomes; UP000214684; 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}.
FT BINDING 17..19
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT BINDING 163..165
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT BINDING 211..214
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
SQ SEQUENCE 342 AA; 37254 MW; 57A884EA401FCC3B CRC64;
MGFFDFMTED IAIDLGTANT LIIHNDKVVI DSPSIVARDR ISGKIIAVGK EANMMQGKTH
ENIKTIRPLK DGVIADFDAS EKMINMFIKS IPALKKRMFT PALRMVVCIP SGITEVEMRA
VKESCERVNG KEVYLIHEPM AAAIGIGIDI MQPKGNMIVD IGGGTTEIAV IALGGIVCDK
SVKIAGDVFT NDIVYYMRTQ HNLFVGESTA EKIKIQIGAA IEDLDGPPED MSVQGRDLLT
GKPKQVDVSY REIAKALDKS IQRIEDAVME TLSQTPPELA ADIYNTGIYL AGGGSMLRGL
DKRISQKTDL PVYIAEDPLR AVVRGTGMAL KNIAKFKSIL IK
//