ID A0A2G5K193_9FLAO Unreviewed; 342 AA.
AC A0A2G5K193;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, 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 ORFNames=BFP77_16335 {ECO:0000313|EMBL:PIB23316.1};
OS Maribacter sp. 4U21.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Maribacter.
OX NCBI_TaxID=1889779 {ECO:0000313|EMBL:PIB23316.1, ECO:0000313|Proteomes:UP000243243};
RN [1] {ECO:0000313|EMBL:PIB23316.1, ECO:0000313|Proteomes:UP000243243}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4U21 {ECO:0000313|EMBL:PIB23316.1,
RC ECO:0000313|Proteomes:UP000243243};
RA Wong S.-K., Hamasaki K., Yoshizawa S.;
RT "Draft genome of Maribacter sp. strain 4U21.";
RL Submitted (AUG-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:PIB23316.1}.
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DR EMBL; MDGN01000078; PIB23316.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5K193; -.
DR OrthoDB; 9768127at2; -.
DR Proteomes; UP000243243; 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; -; 3.
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:UP000243243}.
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; 37424 MW; E3689D1B9C117BB3 CRC64;
MGFFDFLTEE IAIDLGTANT LIIHNDKVVV DSPSIVARDR ITGKIIAVGK EANMMQGKTH
ENIKTIRPLK DGVIADFDAS EKMINMFIKN IPALKKKWFP PALRMVICIP SGITEVEMRA
VKESAERVNG KEVYLIHEPM AAAIGIGLDI MQPKGNMIVD IGGGTTEIAV IALGGIVCDK
SVKIAGDVFT NDIIYYMRTQ HNLYVGESTA EAIKIEIGSA TEDLQTPPDE KSVQGRDLLT
GKPKQVQISY REIAKALDKS ILRVEDAVME TLSQTPPELA ADIYNTGIYL AGGGSMLRGL
DRRLSQKTDL PVYIAEDPLR AVVRGTGIAL KNLERYKSIL IK
//