ID   A0A365ZWV9_9ACTN        Unreviewed;       339 AA.
AC   A0A365ZWV9;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-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=DEH69_02275 {ECO:0000313|EMBL:RBM23633.1};
OS   Streptomyces sp. PT12.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1510197 {ECO:0000313|EMBL:RBM23633.1, ECO:0000313|Proteomes:UP000252839};
RN   [1] {ECO:0000313|EMBL:RBM23633.1, ECO:0000313|Proteomes:UP000252839}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PT12 {ECO:0000313|EMBL:RBM23633.1,
RC   ECO:0000313|Proteomes:UP000252839};
RA   Devaraj K., Tan G.Y.A.;
RT   "Diversity of actinobacteria isolated from Cape Rachado, Malaysia.";
RL   Submitted (MAY-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:RBM23633.1}.
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DR   EMBL; QEST01000019; RBM23633.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A365ZWV9; -.
DR   OrthoDB; 9768127at2; -.
DR   Proteomes; UP000252839; 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:UP000252839}.
FT   BINDING         14..16
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT   BINDING         158..160
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT   BINDING         206..209
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT   BINDING         286..289
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
SQ   SEQUENCE   339 AA;  36285 MW;  B4C91F57FA428AFB CRC64;
     MSFIGRDMAV DLGTANTLVY VRGRGIVLNE PSVVAINTNT GNILAVGAEA KKMIGRTPGN
     IVAVRPLKDG VIADFEITER MLRYFILKIH KRRYLARPRV VVCVPSGITG VERRAVIEAS
     TQAGARQVHI IEEPMAAAIG SGLPVHEATG NMVVDIGGGT TEVAVISLGG IVTAQSIRVA
     GDELDNAIIQ HIKKEYSLLL GERTAESIKI TIGSAHEMDQ DEHTEIRGRD LVSGLPKTVV
     ISSAEVRKAM EEPVNAIVDA VKTTLDKCPP ELSGDIMDRG IVLTGGGALL RGLDERLRKE
     TGMPIHIAED PLDSVALGSG KCVEEFEALQ QVLDAQPRR
//