ID A0A329MVK7_9BACL Unreviewed; 344 AA.
AC A0A329MVK7;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
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=DQG23_08030 {ECO:0000313|EMBL:RAV21977.1};
OS Paenibacillus contaminans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=450362 {ECO:0000313|EMBL:RAV21977.1, ECO:0000313|Proteomes:UP000250369};
RN [1] {ECO:0000313|EMBL:RAV21977.1, ECO:0000313|Proteomes:UP000250369}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CKOBP-6 {ECO:0000313|EMBL:RAV21977.1,
RC ECO:0000313|Proteomes:UP000250369};
RX PubMed=19126735; DOI=10.1099/ijs.0.001495-0;
RA Chou J.H., Lee J.H., Lin M.C., Chang P.S., Arun A.B., Young C.C.,
RA Chen W.M.;
RT "Paenibacillus contaminans sp. nov., isolated from a contaminated
RT laboratory plate.";
RL Int. J. Syst. Evol. Microbiol. 59:125-129(2009).
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:RAV21977.1}.
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DR EMBL; QMFB01000003; RAV21977.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A329MVK7; -.
DR OrthoDB; 9768127at2; -.
DR Proteomes; UP000250369; 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:UP000250369}.
FT BINDING 15..17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT BINDING 161..163
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT BINDING 209..212
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT BINDING 289..292
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
SQ SEQUENCE 344 AA; 36937 MW; E0C9BFCB9E2E6E48 CRC64;
MFGGFTKDLG IDLGTANTLV YVKGKGIVVR EPSVVALRTD TKTIEAVGEA AKKMIGRTPG
NIRAVRPMKD GVIADFETTA TMIKYFLRQA QKQRYLFQRH PSVMVCVPSG ITAVEKRAVE
DATRQAGARE AFTIEEPFAA AIGADLPVWE PTGSMVVDIG GGTTEVAVIS LGGIVTSRSI
RVAGDEMDEA IMQYIKRTYN LMIGERTSES LKMEIGSALP MEKIETMEIR GRDLVSGLPK
TIAVTSDEIT DALTDTVTSI VDAVKVTLEK CPPELAADIM DRGIVLTGGG GLLRNLDKLL
ARETGMPVLV AENPLDCVAI GTGRALENIH LFKLKSGPAS KSRR
//
