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Database: UniProt
Entry: A0A1D2KDI7_BROTH
LinkDB: A0A1D2KDI7_BROTH
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ID   A0A1D2KDI7_BROTH        Unreviewed;       338 AA.
AC   A0A1D2KDI7;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=Cell shape-determining protein MreB {ECO:0000256|HAMAP-Rule:MF_02207};
GN   Name=mreB {ECO:0000256|HAMAP-Rule:MF_02207,
GN   ECO:0000313|EMBL:SPP28377.1};
GN   ORFNames=BTBSAS_20247 {ECO:0000313|EMBL:SPP28377.1}, CNY62_01275
GN   {ECO:0000313|EMBL:ATF25121.1};
OS   Brochothrix thermosphacta (Microbacterium thermosphactum).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Brochothrix.
OX   NCBI_TaxID=2756 {ECO:0000313|EMBL:ATF25121.1, ECO:0000313|Proteomes:UP000243591};
RN   [1] {ECO:0000313|EMBL:ATF25121.1, ECO:0000313|Proteomes:UP000243591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BI {ECO:0000313|EMBL:ATF25121.1,
RC   ECO:0000313|Proteomes:UP000243591};
RA   Paoli G.C., Wijey C., Chen C.-Y., Nguyen L., Yan X., Irwin P.L.;
RT   "Complete Genome Sequences of Two Strains of the Meat Spoilage Bacterium
RT   Brochothrix thermosphacta Isolated from Ground Chicken.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:SPP28377.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BSAS1 3 {ECO:0000313|EMBL:SPP28377.1};
RA   Go L.Y., Mitchell J.A.;
RL   Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Proteomes:UP000270190}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Illikoud N.;
RL   Submitted (APR-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}.
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DR   EMBL; CP023483; ATF25121.1; -; Genomic_DNA.
DR   EMBL; OUNC01000012; SPP28377.1; -; Genomic_DNA.
DR   RefSeq; WP_029092192.1; NZ_RSDU01000001.1.
DR   AlphaFoldDB; A0A1D2KDI7; -.
DR   STRING; 2756.BFR44_02245; -.
DR   KEGG; bths:CNY62_01275; -.
DR   OrthoDB; 9768127at2; -.
DR   Proteomes; UP000243591; Chromosome.
DR   Proteomes; UP000270190; 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:UP000243591}.
FT   BINDING         15..17
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT   BINDING         159..161
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT   BINDING         207..210
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT   BINDING         288..291
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
SQ   SEQUENCE   338 AA;  35763 MW;  17799210483E2AC2 CRC64;
     MFNFGSKDIG IDLGTANTLV YVKGKGIALR EPSVVAINKD SGQIVAVGSD ARNMIGRTPG
     NIVAIRPMKD GVIADYDITA AMMKYYINKL NKGMGIGKPH VMICIPVGVT GVEERAVIDA
     TRQAGARDAY TIEEPFAAAI GAGLPVWEPT GSMVVDIGGG TTEVAIISLG GIVTAVSERT
     AGDKLDEAIV NYIRKTYNLL IGERTAEQIK MEIGSANVEG LEKQTTDIRG RDLVTGLPKT
     IEITAAEICT ALHDSVMQVI DAVKTTLEST PPELAADIMD RGIVLTGGGA LLHNIDRLIS
     EETNMPVVIA EDPLDCVAIG TGKSLDNIDL FKNAKKSR
//
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