ID U5MLS8_CLOSA Unreviewed; 344 AA.
AC U5MLS8;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=Cell shape-determining protein MreB {ECO:0000256|HAMAP-Rule:MF_02207};
GN Name=mbl {ECO:0000313|EMBL:AGX41545.1};
GN Synonyms=mreB {ECO:0000256|HAMAP-Rule:MF_02207};
GN ORFNames=CLSA_c05220 {ECO:0000313|EMBL:AGX41545.1};
OS Clostridium saccharobutylicum DSM 13864.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1345695 {ECO:0000313|EMBL:AGX41545.1, ECO:0000313|Proteomes:UP000017118};
RN [1] {ECO:0000313|EMBL:AGX41545.1, ECO:0000313|Proteomes:UP000017118}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13864 {ECO:0000313|EMBL:AGX41545.1};
RX PubMed=24285650;
RA Poehlein A., Hartwich K., Krabben P., Ehrenreich A., Liebl W., Durre P.,
RA Gottschalk G., Daniel R.;
RT "Complete Genome Sequence of the Solvent Producer Clostridium
RT saccharobutylicum NCP262 (DSM 13864).";
RL Genome Announc. 1:e00997-13(2013).
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; CP006721; AGX41545.1; -; Genomic_DNA.
DR RefSeq; WP_022743832.1; NZ_AYXL01000174.1.
DR AlphaFoldDB; U5MLS8; -.
DR GeneID; 55473078; -.
DR KEGG; csb:CLSA_c05220; -.
DR PATRIC; fig|1345695.10.peg.1216; -.
DR eggNOG; COG1077; Bacteria.
DR HOGENOM; CLU_052037_0_0_9; -.
DR OrthoDB; 9768127at2; -.
DR Proteomes; UP000017118; 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 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:UP000017118}.
FT BINDING 160..162
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT BINDING 208..211
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT BINDING 288..291
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
SQ SEQUENCE 344 AA; 36935 MW; 2C017D0BD7B87102 CRC64;
MGFWRTGTDL AIDLGTATVL VYVKGKGVIL KEPSVVAINK NNNNLLAIGE EARKMIGRTP
GNIVAVRPLR DGVISDYDIT QKMLKEFIKK ACGKRNITAP KVIVCVPSQA TEVEKRAVID
AAMNSGAKTV HLIEEPLAAA IGAGLDITKP NGCMVVDIGG GTCDIAVISL GGVVERESIK
VAGDKFDDAI IKYVRNQYKL MIGEKTAEDL KINIGSAFKN SRNLAAIMKG RNLITGLPDE
VEITTEEIRN AIKEPVENIV ETVKRVLEKT PPELAADIVE KGILMTGGGA LLHGLDKLIQ
FRTGVETYVA EDSVECVAKG TGAVLNYIDK LDSDINSQQI VLIE
//
