ID A0A0L0QKQ1_VIRPA Unreviewed; 335 AA.
AC A0A0L0QKQ1;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=AFK71_11040 {ECO:0000313|EMBL:KNE19084.1};
OS Virgibacillus pantothenticus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Virgibacillus.
OX NCBI_TaxID=1473 {ECO:0000313|EMBL:KNE19084.1, ECO:0000313|Proteomes:UP000036780};
RN [1] {ECO:0000313|Proteomes:UP000036780}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26 {ECO:0000313|Proteomes:UP000036780};
RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA Shi H., Pan Z., Liu X.;
RT "Fjat-10053 dsm26.";
RL Submitted (JUL-2015) 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:KNE19084.1}.
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DR EMBL; LGTO01000007; KNE19084.1; -; Genomic_DNA.
DR RefSeq; WP_050351587.1; NZ_LGTO01000007.1.
DR AlphaFoldDB; A0A0L0QKQ1; -.
DR GeneID; 66872109; -.
DR PATRIC; fig|1473.5.peg.737; -.
DR OrthoDB; 9768127at2; -.
DR Proteomes; UP000036780; 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; -; 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:UP000036780}.
FT BINDING 13..15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT BINDING 159..161
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT BINDING 207..210
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT BINDING 287..290
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
SQ SEQUENCE 335 AA; 35937 MW; C0E626CAB9B56292 CRC64;
MFSTAEVGID LGTANILIYT KSKGIVLNEP SVVAIDVNTK QVVAVGAEAK EMVGKTPQNI
IPIRPLKDGV IADYDVTSQM LKAFLKKVSK QIGMSMRKPV VVVCTPSGST TVERRAIHNA
VSSYGAKQVH LIEEPIAAAI GADLPVDEPV ANVIVDIGGG TSEVGIISFG GVVSCNSVRV
GGDKMDEEII HHIRKNYNVL IGERTAENIK MEIGYAHPNH KEESMEIRGR DMVTGLPKTI
TITSKEIHLA LKESLEQVLE AIRLTLENCP PELSGDIVDH GIVLTGGGAL LHGMKEWLSH
ELIVPVHLAP NPLESVAIGT GRSLKMIHKL QKAAK
//
