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Database: UniProt
Entry: A0A0D6MVB5_ACEAC
LinkDB: A0A0D6MVB5_ACEAC
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ID   A0A0D6MVB5_ACEAC        Unreviewed;       348 AA.
AC   A0A0D6MVB5;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 30.
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=Abac_017_086 {ECO:0000313|EMBL:GAN57385.1};
OS   Acetobacter aceti NBRC 14818.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Acetobacter; Acetobacter subgen. Acetobacter.
OX   NCBI_TaxID=887700 {ECO:0000313|EMBL:GAN57385.1, ECO:0000313|Proteomes:UP000032677};
RN   [1] {ECO:0000313|EMBL:GAN57385.1, ECO:0000313|Proteomes:UP000032677}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 14818 {ECO:0000313|EMBL:GAN57385.1,
RC   ECO:0000313|Proteomes:UP000032677};
RA   Azuma Y., Higashiura N., Hirakawa H., Matsushita K.;
RT   "Whole genome sequence of Acetobacter aceti NBRC 14818.";
RL   Submitted (NOV-2012) 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:GAN57385.1}.
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DR   EMBL; BAMU01000017; GAN57385.1; -; Genomic_DNA.
DR   RefSeq; WP_010668496.1; NZ_SLZP01000001.1.
DR   AlphaFoldDB; A0A0D6MVB5; -.
DR   OrthoDB; 9768127at2; -.
DR   Proteomes; UP000032677; 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}.
FT   BINDING         19..21
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT   BINDING         165..167
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT   BINDING         213..216
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;  36976 MW;  622EF5094E8A83C9 CRC64;
     MFARLLGLMS ADMAIDLGTA NTLVYVKGRG IVLNEPSVVA IADSRGKKQV LAVGEEAKQM
     VGRTPGNIMA IRPMRDGVIA DFEVAEEMIK HFIRRVHNRS IFASPQVIVC VPSGSTAVER
     RAIQESAESA GARRVFLIEE PMAAAIGAGL PVTEPSGSMI VDIGGGTTEV AVISLGGIVY
     ARSVRVGGDK MDEAIISYIR RMHNLLIGES SAERIKMSIG SAMMPDDPND PGPLQNVKGR
     DLITGAPREV IVSQAQIADS LAEPITQIIE AVKLTLENTP PELAADIVDK GIVLTGGGAL
     LYRLDEVLRL ATGLPVTVGE DPLSCVALGT GRALEEMKRL RNVLTTMY
//
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