ID A0A069CT16_WEIOS Unreviewed; 333 AA.
AC A0A069CT16;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 33.
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:GAK30614.1};
GN ORFNames=WOSG25_040540 {ECO:0000313|EMBL:GAK30614.1};
OS Weissella oryzae (strain DSM 25784 / JCM 18191 / LMG 30913 / SG25).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae; Weissella.
OX NCBI_TaxID=1329250 {ECO:0000313|EMBL:GAK30614.1, ECO:0000313|Proteomes:UP000030643};
RN [1] {ECO:0000313|Proteomes:UP000030643}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25784 / JCM 18191 / LMG 30913 / SG25
RC {ECO:0000313|Proteomes:UP000030643};
RX PubMed=25013139; DOI=10.1128/genomea.00667-14;
RA Tanizawa Y., Fujisawa T., Mochizuki T., Kaminuma E., Suzuki Y.,
RA Nakamura Y., Tohno M.;
RT "Draft genome sequence of Weissella oryzae SG25T, isolated from fermented
RT rice grains.";
RL Genome Announc. 2:0-0(2014).
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; DF820487; GAK30614.1; -; Genomic_DNA.
DR RefSeq; WP_027698706.1; NZ_DF820487.1.
DR AlphaFoldDB; A0A069CT16; -.
DR STRING; 1329250.WOSG25_040540; -.
DR eggNOG; COG1077; Bacteria.
DR OrthoDB; 9768127at2; -.
DR Proteomes; UP000030643; 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:UP000030643}.
FT BINDING 15..17
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 288..291
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
SQ SEQUENCE 333 AA; 34957 MW; 1A01184B60DE21C1 CRC64;
MFSFGSRNVG IDLGTANTLV YIEGKGIVLR EPSVVARNTR TDEVVAVGEA AKEMLGRTPG
SIKAIRPMRD GVIADYETTV AMLKYYLNKA LGNGRTNPKV VIGVPSGVTA VERRAVTDAA
RVAGAKDAFV IEEPFAAAVG AGLPVMEPTG SMVVDMGGGT TDVATISLGG IVSSRSIRMA
GDRLDDAIMT YIRQNYSVLI GEQSAERLKM EIGSANLELA KDMDGATIRG RDLVTGLPKT
IEVTAFDVAD AIKDVIAEII VAIKETLEET SPEIAADVID HGIILTGGGA LLHHIDEVIA
DATKVPVFIA TEPLDAVVLG TGEILKSIDV LNN
//
