ID A0A1B3SJ97_9MOLU Unreviewed; 342 AA.
AC A0A1B3SJ97;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
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:AOG60006.1};
GN ORFNames=SHELI_v1c00510 {ECO:0000313|EMBL:AOG60006.1};
OS Spiroplasma helicoides.
OC Bacteria; Mycoplasmatota; Mollicutes; Entomoplasmatales; Spiroplasmataceae;
OC Spiroplasma.
OX NCBI_TaxID=216938 {ECO:0000313|EMBL:AOG60006.1, ECO:0000313|Proteomes:UP000094378};
RN [1] {ECO:0000313|EMBL:AOG60006.1, ECO:0000313|Proteomes:UP000094378}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TABS-2 {ECO:0000313|EMBL:AOG60006.1,
RC ECO:0000313|Proteomes:UP000094378};
RA Shen W.-Y., Lo W.-S., Lai Y.-C., Kuo C.-H.;
RT "Complete genome sequence of Spiroplasma helicoides TABS-2 (DSM 22551).";
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}.
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DR EMBL; CP017015; AOG60006.1; -; Genomic_DNA.
DR RefSeq; WP_069115787.1; NZ_CP017015.1.
DR AlphaFoldDB; A0A1B3SJ97; -.
DR STRING; 216938.SHELI_v1c00510; -.
DR KEGG; shj:SHELI_v1c00510; -.
DR PATRIC; fig|216938.3.peg.51; -.
DR OrthoDB; 391604at2; -.
DR Proteomes; UP000094378; 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 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:UP000094378}.
FT BINDING 158..160
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT BINDING 206..209
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT BINDING 286..289
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
SQ SEQUENCE 342 AA; 37503 MW; ED548636A0E7AE2F CRC64;
MKGDKKFVSI DLGTAYTLVY VNGKGIVYNE ASIVAYRRKD NSIIAVGEEA YKMIGKGNKT
IKIVKPMVDG VITDIETTTS QLRYIFKKLR IESYLKGAVV LLACPSVITG LEKLALQKIA
MNFGASRVFI EEEVKMAALG GGMNIFAPTG KLVIDSGGGT TDVAVLASGD IVVSKSIKVA
GNYLNEEIRR FIRSQYGMEV GQKTSEMVKI NIGSLAKYSD ERRMKVYGRD VVSGLPREIE
LSPEEVREVL KVPVSKIIDL TVQVLEETPP ELAGDIFKNG IIICGGGALI RGIDKYFADT
LQLPTRVGEQ PLLAVINGTR KFENQIFDYI REEKLSSSLV NF
//
