ID A0A2P7R0A5_9SPHN Unreviewed; 346 AA.
AC A0A2P7R0A5;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, 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=C7I55_02380 {ECO:0000313|EMBL:PSJ43626.1};
OS Sphingomonas deserti.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=2116704 {ECO:0000313|EMBL:PSJ43626.1, ECO:0000313|Proteomes:UP000241167};
RN [1] {ECO:0000313|EMBL:PSJ43626.1, ECO:0000313|Proteomes:UP000241167}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GL-C-18 {ECO:0000313|EMBL:PSJ43626.1,
RC ECO:0000313|Proteomes:UP000241167};
RA Liu L., Li L., Liang L., Zhang X., Wang T.;
RT "The draft genome of Sphingosinicella sp. GL-C-18.";
RL Submitted (MAR-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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {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:PSJ43626.1}.
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DR EMBL; PXYI01000001; PSJ43626.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P7R0A5; -.
DR OrthoDB; 9768127at2; -.
DR Proteomes; UP000241167; 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:UP000241167}.
FT BINDING 168..170
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT BINDING 216..219
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT BINDING 297..300
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
SQ SEQUENCE 346 AA; 36268 MW; AEA1E31719B48F8B CRC64;
MQLPKFLRLA SQDMAIDLGT VNTVVCLRDS GIVLNEPSVV AIETIDGVRR VKAVGRDAKL
MMGKTPASIQ AIRPLRDGVI ADIDVAEQMI KHFIDKAHGG RSRLPRRPEI VVCVPSGSTS
VERRAIRDAA SNAGASKVWL IEEPMAAAIG AGLPVLDPVG AMIVDIGGGT TEVAILSMRG
LAYSTSVRVG GDKMDEAIIN AVRRKHNLII GEATAERIKM ALGAALPPTG DAPTLTVRGR
HLAAGMPKEI TISQIEVAQS LFDAVAQIIG AVRTALENSA PELAADIVDS GIVMTGGGAL
LQRLDQALSK ATGLPVIVAP DPLTCVALGA WRALEDPEYR AVLIEG
//
