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Database: UniProt
Entry: A0A0G1JKF4_9BACT
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ID   A0A0G1JKF4_9BACT        Unreviewed;       353 AA.
AC   A0A0G1JKF4;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 27.
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=UW63_C0002G0019 {ECO:0000313|EMBL:KKT72051.1};
OS   Candidatus Uhrbacteria bacterium GW2011_GWF2_44_350.
OC   Bacteria; Candidatus Uhrbacteria.
OX   NCBI_TaxID=1619000 {ECO:0000313|EMBL:KKT72051.1, ECO:0000313|Proteomes:UP000034154};
RN   [1] {ECO:0000313|EMBL:KKT72051.1, ECO:0000313|Proteomes:UP000034154}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
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:KKT72051.1}.
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DR   EMBL; LCJB01000002; KKT72051.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1JKF4; -.
DR   PATRIC; fig|1619000.3.peg.40; -.
DR   Proteomes; UP000034154; 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         22..24
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT   BINDING         168..170
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT   BINDING         216..219
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT   BINDING         296..299
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
SQ   SEQUENCE   353 AA;  38265 MW;  9031C76952E687AB CRC64;
     MNNFVNNFLG KFSKDVGIDL GTANTLVYVK DQGIVINEPS VVAINTRTDQ ILAVGRDARD
     MIGKTPPHLS VVRPLTKGVI SDFEVTEKML KYFIDQVHKE SKSFIPRPRV VIGVPPEITE
     VERKAVEDAV FSAGAREVFL VEEPMLAAIG ARLPVAESVG TLVVDIGGGT TDIAVISLAG
     VVTWKSLPIA GDELNKNIIT YSRDVFNLLL GERQAELVKM RVGSAIPQDE PLSMEMRGRD
     LLSGLPKEII VSDSQIREAI HRSVRTIVEN VKATLEVTPP ELVADIYERG IVMIGGGALL
     RGFDKLLSTE TAIPVRVADD PLTCVVRGAG LLLENEELLR DVTLPSSRDG GIV
//
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