ID A0A023X3P4_9ACTN Unreviewed; 342 AA.
AC A0A023X3P4;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 24-JAN-2024, entry version 35.
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=RradSPS_1538 {ECO:0000313|EMBL:AHY46821.1};
OS Rubrobacter radiotolerans.
OC Bacteria; Actinomycetota; Rubrobacteria; Rubrobacterales; Rubrobacteraceae;
OC Rubrobacter.
OX NCBI_TaxID=42256 {ECO:0000313|EMBL:AHY46821.1, ECO:0000313|Proteomes:UP000025229};
RN [1] {ECO:0000313|EMBL:AHY46821.1, ECO:0000313|Proteomes:UP000025229}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RSPS-4 {ECO:0000313|EMBL:AHY46821.1,
RC ECO:0000313|Proteomes:UP000025229};
RA Egas C.C., Barroso C.C., Froufe H.J.C., Pacheco J.J., Albuquerque L.L.,
RA da Costa M.M.S.;
RT "Complete genome sequence of the Radio-Resistant Rubrobacter radiotolerans
RT RSPS-4.";
RL Submitted (MAR-2014) 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; CP007514; AHY46821.1; -; Genomic_DNA.
DR RefSeq; WP_038681775.1; NZ_CP007514.1.
DR AlphaFoldDB; A0A023X3P4; -.
DR STRING; 42256.RradSPS_1538; -.
DR KEGG; rrd:RradSPS_1538; -.
DR PATRIC; fig|42256.3.peg.1557; -.
DR eggNOG; COG1077; Bacteria.
DR HOGENOM; CLU_052037_0_0_11; -.
DR OrthoDB; 9768127at2; -.
DR Proteomes; UP000025229; 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; -; 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:UP000025229}.
FT BINDING 16..18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT BINDING 164..166
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT BINDING 212..215
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT BINDING 292..295
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
SQ SEQUENCE 342 AA; 36188 MW; 2FA8F92A210CACE5 CRC64;
MFGGLFGRDV AIDLGTANTL VFVKGHGIVL SEPSVVAIDN KTDKVVAVGS AAKSMIGRTP
GNIVAMRPLK DGVIADFEVT EKMLSYFIRK VQPRRGIFRS IIGPRVVVCV PSGVTGVELR
AVKEATESAG ARQAFTIEEP LAAAIGAGLP VNEAQGSMIV DIGGGTSEVA VISLGGIVTK
SSIRIAGDDV DDAITTYIQK EYKLAIGTQT AEQLKIELGS AFRLEEEESA EIRGRDLVTG
LPKTVVITSE EIREAISVPV EAIIAAVRDT LDRTPPELAS DIMDRGMILA GGGALLQHLD
ERLRRETMIP VHVAEDPLMC VALGSGRSLE EIDSFRNALS AS
//
