ID U3AFJ8_9VIBR Unreviewed; 347 AA.
AC U3AFJ8;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 32.
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:GAD78696.1};
GN ORFNames=VEZ01S_05_00850 {ECO:0000313|EMBL:GAD78696.1};
OS Vibrio ezurae NBRC 102218.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=1219080 {ECO:0000313|EMBL:GAD78696.1, ECO:0000313|Proteomes:UP000016562};
RN [1] {ECO:0000313|EMBL:GAD78696.1, ECO:0000313|Proteomes:UP000016562}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 102218 {ECO:0000313|EMBL:GAD78696.1,
RC ECO:0000313|Proteomes:UP000016562};
RA Yoshida I., Hosoyama A., Numata M., Hashimoto M., Hosoyama Y.,
RA Tsuchikane K., Noguchi M., Hirakata S., Ichikawa N., Ohji S., Yamazoe A.,
RA Fujita N.;
RT "Whole genome shotgun sequence of Vibrio ezurae NBRC 102218.";
RL Submitted (SEP-2013) 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:GAD78696.1}.
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DR EMBL; BATM01000005; GAD78696.1; -; Genomic_DNA.
DR RefSeq; WP_021712419.1; NZ_BATM01000005.1.
DR AlphaFoldDB; U3AFJ8; -.
DR STRING; 1219080.VEZ01S_05_00850; -.
DR eggNOG; COG1077; Bacteria.
DR OrthoDB; 9768127at2; -.
DR Proteomes; UP000016562; 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:UP000016562}.
FT BINDING 19..21
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 347 AA; 36879 MW; 3D20891DA1CFD662 CRC64;
MFKKIRGMFS NDLSIDLGTA NTLIYVKGQG IVLDEPSVVA IRQDRAGSTK SVAAVGHDAK
QMLGRTPGNI SAIRPMKDGV IADFFVTEKM LQHFIKQVHD NSFLKPSPRV LVCVPCGSTQ
VERRAIRESA LGAGAREVYL IDEPMAAAIG AGLRVSEPTG SMVVDIGGGT TEVAVISLNG
VVYSSSVRIG GDRFDEAIIN YVRRNYGSLI GEATAEKIKH VIGSAYPGDE VEELEVRGRN
LAEGVPRSFS LNSNEILEAL QEPLSGIVSA VMVALEQCPP ELASDISENG MVLTGGGALL
KDLDRLLTEE TGIPVVVAEE PLTCVARGGG KALEMIDMHG GDLFSEE
//
