ID A0A073J0J8_9RHOB Unreviewed; 348 AA.
AC A0A073J0J8;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=SUH3_21090 {ECO:0000313|EMBL:KEJ95484.1};
OS Pseudosulfitobacter pseudonitzschiae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Pseudosulfitobacter.
OX NCBI_TaxID=1402135 {ECO:0000313|EMBL:KEJ95484.1, ECO:0000313|Proteomes:UP000027746};
RN [1] {ECO:0000313|EMBL:KEJ95484.1, ECO:0000313|Proteomes:UP000027746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H3 {ECO:0000313|EMBL:KEJ95484.1,
RC ECO:0000313|Proteomes:UP000027746};
RA Lai Q., Hong Z.;
RT "Sulfitobacter sp. H3 (MCCC 1A00686) Genome Sequencing.";
RL Submitted (JAN-2014) 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:KEJ95484.1}.
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DR EMBL; JAMD01000006; KEJ95484.1; -; Genomic_DNA.
DR RefSeq; WP_028955141.1; NZ_WKFG01000017.1.
DR AlphaFoldDB; A0A073J0J8; -.
DR GeneID; 68871438; -.
DR OrthoDB; 9768127at2; -.
DR Proteomes; UP000027746; 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:UP000027746}.
FT BINDING 21..23
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT BINDING 167..169
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT BINDING 215..218
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 348 AA; 36925 MW; 8FABC9BC16D16DCC CRC64;
MSWFGNLGGL FSSDMAIDLG TANTLIYVKG KGVVLSEPSV VAYHIKDGVK KVLAVGEDAK
LMLGRTPGSI EAIRPMREGV IADFDTAEEM IKHFIRKVHK RSTFSKPKII VCVPHGATPV
EKRAIRQSVL SAGARRAGLI AEPIAAAIGA GMPITDPTGN MVVDIGGGTT EVAVLSLGDI
VYARSVRVGG DRMDEAIISY LRRQQNLLVG ETTAERIKTT IGTARMPDDG RGTSMQIRGR
DLLNGVPKEI EVTQAQIAEA LAEPVQQICE AVMTALETTP PDLAADIVDR GVMLTGGGAL
LGDLDLALRE QTGLAVSIAN ESLNCVALGT GKALEFEKQL RHAIDYDS
//
