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Database: UniProt
Entry: A0A2G1XGM7_STRCJ
LinkDB: A0A2G1XGM7_STRCJ
Original site: A0A2G1XGM7_STRCJ 
ID   A0A2G1XGM7_STRCJ        Unreviewed;       339 AA.
AC   A0A2G1XGM7;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   24-JAN-2024, entry version 24.
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=BLA24_20875 {ECO:0000313|EMBL:PHQ50390.1}, CYQ11_09905
GN   {ECO:0000313|EMBL:PPT13161.1};
OS   Streptomyces cinnamoneus (Streptoverticillium cinnamoneum).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces; Streptomyces cinnamoneus group.
OX   NCBI_TaxID=53446 {ECO:0000313|EMBL:PHQ50390.1, ECO:0000313|Proteomes:UP000222531};
RN   [1] {ECO:0000313|EMBL:PHQ50390.1, ECO:0000313|Proteomes:UP000222531}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 21532 {ECO:0000313|EMBL:PHQ50390.1,
RC   ECO:0000313|Proteomes:UP000222531};
RX   PubMed=29053243;
RA   Patteson J., Cai W., Johnson R.A., Santa Maria K., Li B.;
RT   "Identification of the Biosynthetic Pathway for the Antibiotic
RT   Bicyclomycin.";
RL   Biochemistry 0:0-0(2017).
RN   [2] {ECO:0000313|EMBL:PPT13161.1, ECO:0000313|Proteomes:UP000239771}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 41675 {ECO:0000313|EMBL:PPT13161.1,
RC   ECO:0000313|Proteomes:UP000239771};
RA   Vior N.M., Lacret R., Chandra G., Dorai-Raj S., Trick M., Truman A.W.;
RT   "Discovery and biosynthesis of the antibiotic bicyclomycin in distant
RT   bacterial classes.";
RL   Submitted (DEC-2017) 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:PHQ50390.1}.
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DR   EMBL; NHZO01000151; PHQ50390.1; -; Genomic_DNA.
DR   EMBL; PKFQ01000001; PPT13161.1; -; Genomic_DNA.
DR   RefSeq; WP_004950903.1; NZ_PKFQ01000001.1.
DR   AlphaFoldDB; A0A2G1XGM7; -.
DR   OrthoDB; 9768127at2; -.
DR   Proteomes; UP000222531; Unassembled WGS sequence.
DR   Proteomes; UP000239771; 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:UP000222531}.
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;  36314 MW;  8509FD98AF1D3108 CRC64;
     MSFIGRDMAV DLGTANTLVY VRGRGIVLNE PSVVAINTNT GGILAVGAEA KKMIGRTPGN
     IVAVRPLKDG VIADFEITER MLRYFILKIH KRRWMARPRV VVCVPSGITG VERRAVIEAS
     TQAGARQVHI IEEPMAAAIG SGLPVHEATG NMVVDIGGGT TEVAVISLGG IVTAQSIRVA
     GDELDNAIIQ HIKKEYSLLL GERTAEQIKI TIGSAYDLEQ DEHTEIRGRD LVSGLPKTVV
     ISAAEVRKAI EEPVNSIVDA VKTTLDKCPP ELSGDVMDRG IVLTGGGALL RGLDERLRRE
     TGMPIHIAED PLDSVALGSG KCVEEFEALQ QVLDAQPRR
//
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