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Database: UniProt
Entry: A0A1T5KMG3_9CLOT
LinkDB: A0A1T5KMG3_9CLOT
Original site: A0A1T5KMG3_9CLOT 
ID   A0A1T5KMG3_9CLOT        Unreviewed;       344 AA.
AC   A0A1T5KMG3;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
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=SAMN02194393_01933 {ECO:0000313|EMBL:SKC64468.1};
OS   Maledivibacter halophilus.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Maledivibacter.
OX   NCBI_TaxID=36842 {ECO:0000313|EMBL:SKC64468.1, ECO:0000313|Proteomes:UP000190285};
RN   [1] {ECO:0000313|EMBL:SKC64468.1, ECO:0000313|Proteomes:UP000190285}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M1 {ECO:0000313|EMBL:SKC64468.1,
RC   ECO:0000313|Proteomes:UP000190285};
RA   Peterson S.W.;
RL   Submitted (FEB-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: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_02207}.
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DR   EMBL; FUZT01000004; SKC64468.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1T5KMG3; -.
DR   STRING; 36842.SAMN02194393_01933; -.
DR   OrthoDB; 9768127at2; -.
DR   Proteomes; UP000190285; 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:UP000190285}.
FT   BINDING         17..19
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT   BINDING         162..164
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT   BINDING         290..293
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
SQ   SEQUENCE   344 AA;  36899 MW;  2AFD27994F216569 CRC64;
     MGLFNLFTKD IGIDLGTANT LINVKGKGIV IREPSVVAIQ EDTKDVLAVG LEAKKMIGRT
     PGNIVAIRPL KDGVIADFDT TQGMLRYFIK RANPKNSVVF RPRVLVCVPS GVTEVEKRAV
     IDATEQAGAK EAFLIEEPMA AAIGAGLPVA DPTGSMVVDI GGGTTEIAVI SLGGIVTSKS
     IRIGGDEMDE AIVHYIKKEY NLMIGERTAE ETKITIGSAF PKTKEERMEI RGRDLVSGLP
     KTLTITSTEI LDALNEPVNS ILEGIKITLE KTPPELAADI MEYGIMLTGG GALLDGLDKL
     IKEETGMPVR IAEQPLDCVA SGTGVALENY DLLKRVFISP RRNR
//
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