ID A0A3Q9HQ98_9FIRM Unreviewed; 346 AA.
AC A0A3Q9HQ98;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, 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=BBF96_07750 {ECO:0000313|EMBL:AZR73288.1};
OS Anoxybacter fermentans.
OC Bacteria; Bacillota; Clostridia; Halanaerobiales; Anoxybacter.
OX NCBI_TaxID=1323375 {ECO:0000313|EMBL:AZR73288.1, ECO:0000313|Proteomes:UP000267250};
RN [1] {ECO:0000313|EMBL:AZR73288.1, ECO:0000313|Proteomes:UP000267250}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DY22613 {ECO:0000313|EMBL:AZR73288.1,
RC ECO:0000313|Proteomes:UP000267250};
RA Zeng X., Shao Z.;
RT "Genome and transcriptome analysis of iron-reducing fermentative bacteria
RT Anoxybacter fermentans.";
RL Submitted (JUL-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}.
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DR EMBL; CP016379; AZR73288.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3Q9HQ98; -.
DR KEGG; aft:BBF96_07750; -.
DR OrthoDB; 9768127at2; -.
DR Proteomes; UP000267250; 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:UP000267250}.
FT BINDING 19..21
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"
FT BINDING 292..295
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
SQ SEQUENCE 346 AA; 37195 MW; 47D2F208FFA55BDF CRC64;
MFKFISAPFS RDMGIDLGTA NTLVYIKGKG ITIREPSVVA KQQDTGEILA VGEEAKRMIG
RTPGNIVAIR PMKDGVIADF DVTEAMLRHF IKKAHKRIRL VHPRIVICVP SGVTEVEKRA
VHDAAIHAGA REAYLIEEPM AAAIGAGLPV HEPAGNMVVD IGGGTTEVAI ISLGGIVTSE
SIRVGGDEMD SAIVQYVKQN YNLMIGERTA EQVKVEIGAA IVEPGENEIR EVRGRDLVSG
LPKTIEISAE EIKEALKEPI SRIISAVKRT LEQTPPELAS DVMDKGIIMT GGGSLLKGLD
RLISQETGMP VHIADDPLDC VAIGTGRVLD ELNVLRRVLI TPKKIS
//
