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Database: UniProt
Entry: A0A418WCC0_9PROT
LinkDB: A0A418WCC0_9PROT
Original site: A0A418WCC0_9PROT 
ID   A0A418WCC0_9PROT        Unreviewed;       346 AA.
AC   A0A418WCC0;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, 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=D3874_11505 {ECO:0000313|EMBL:RJF87568.1};
OS   Oleomonas cavernae.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Oleomonas.
OX   NCBI_TaxID=2320859 {ECO:0000313|EMBL:RJF87568.1, ECO:0000313|Proteomes:UP000284605};
RN   [1] {ECO:0000313|EMBL:RJF87568.1, ECO:0000313|Proteomes:UP000284605}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K1W22B-8 {ECO:0000313|EMBL:RJF87568.1,
RC   ECO:0000313|Proteomes:UP000284605};
RA   Zhu H.;
RL   Submitted (SEP-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: 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:RJF87568.1}.
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DR   EMBL; QYUK01000011; RJF87568.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A418WCC0; -.
DR   OrthoDB; 9768127at2; -.
DR   Proteomes; UP000284605; 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:UP000284605}.
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         295..298
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
SQ   SEQUENCE   346 AA;  36570 MW;  AE1C057FE9A1B897 CRC64;
     MFSKLLGILS ADMAIDLGTA NTLVYVKGRG IVLNEPSVVA MVSNRGKKQV LAVGDEAKMM
     LGRTPGNIEA IRPLRDGVIA DFEVAEEMIK HFIRKVHNRR SFASPQIVVC VPSGSTAVER
     RAIQESAESA GARRVFLIEE PMAAAIGANL PVTEPTGSMV VDIGGGTTEV AVLSLGGIVY
     SRSVRVGGDK MDEAIIAYIR RNHNLLVGEA SAERIKKEIG SAAPPEDGYG ATMEIKGRDL
     MNGVPKELVI SQRQIAESLA EPVSAIVEAV KVALEHTAPE LAADIVDKGI VLTGGGALLG
     NLDLVLRHAT GLPVSIADDP LTCVAKGTGR ALEEMKTLRH VLTQAY
//
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