ID A0A402BUK4_9FIRM Unreviewed; 341 AA.
AC A0A402BUK4;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Cell shape-determining protein MreB {ECO:0000256|HAMAP-Rule:MF_02207};
GN Name=mreB2 {ECO:0000313|EMBL:GCE34954.1};
GN Synonyms=mreB {ECO:0000256|HAMAP-Rule:MF_02207};
GN ORFNames=SPFL3102_02782 {ECO:0000313|EMBL:GCE34954.1};
OS Sporomusaceae bacterium.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae.
OX NCBI_TaxID=1917525 {ECO:0000313|EMBL:GCE34954.1, ECO:0000313|Proteomes:UP000287175};
RN [1] {ECO:0000313|EMBL:GCE34954.1, ECO:0000313|Proteomes:UP000287175}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FL31 {ECO:0000313|EMBL:GCE34954.1,
RC ECO:0000313|Proteomes:UP000287175};
RA Aoyagi T., Kurasawa H., Amachi S., Nakajima N., Hori T., Yamamura S.;
RT "Draft genome sequence of Sporomusaceae bacterium strain FL31, a lactate-
RT fermenting bacterium of the class Negativicutes.";
RL Submitted (DEC-2018) 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: 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:GCE34954.1}.
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DR EMBL; BIFV01000012; GCE34954.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A402BUK4; -.
DR OrthoDB; 9768127at2; -.
DR Proteomes; UP000287175; 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:UP000287175}.
FT BINDING 18..20
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT BINDING 162..164
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT BINDING 210..213
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT BINDING 291..294
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
SQ SEQUENCE 341 AA; 36101 MW; 5332A9BD34F80BFA CRC64;
MLGLFRESGC ELGIDLGTAN MLVYSKGQGI VLQEPSVVAV LQHTGEVLAL GEEARAMLGR
TPGDIMALRP LKNGVIADLD VTQQMLEFFI RKAVSSRFYR KPRVVISVPS INTEVEKRAV
VSAATQAGAQ EVYLIEDVMA AAIGAGLAVE EPSGNMVVDI GGGTTDVAVI SLGGIVRSQA
IRIGGVEMDE AISQYVKKTH SLIIGEQTAE AVKIALGSTV AVSGDKAQLE IRGRNILTGL
PRALVLSERE VRLALTEPIT AIVEVIKSTL ERTPPELVAD IIDNGMVLTG GGALLRGLDE
LLVQETGITV RIADEPLTCV ARGAGKVLGN LKNLRPMPHF R
//
