ID A0A151JID6_9VIBR Unreviewed; 347 AA.
AC A0A151JID6; A0A151KS35;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
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=ATY37_01240 {ECO:0000313|EMBL:KYN80215.1}, AUQ44_06805
GN {ECO:0000313|EMBL:KYN25337.1};
OS Vibrio cidicii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=1763883 {ECO:0000313|EMBL:KYN25337.1, ECO:0000313|Proteomes:UP000075349};
RN [1] {ECO:0000313|EMBL:KYN25337.1, ECO:0000313|Proteomes:UP000075346}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2538-88 {ECO:0000313|Proteomes:UP000075346}, and 2756-81
RC {ECO:0000313|EMBL:KYN25337.1};
RA Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KYN80215.1, ECO:0000313|Proteomes:UP000075349}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2538-88 {ECO:0000313|EMBL:KYN80215.1}, and 2756-81
RC {ECO:0000313|Proteomes:UP000075349};
RA Tarr C.L., Gladney L.M.;
RL Submitted (DEC-2015) 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:KYN25337.1}.
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DR EMBL; LOMK01000001; KYN25337.1; -; Genomic_DNA.
DR EMBL; LOBR01000127; KYN80215.1; -; Genomic_DNA.
DR RefSeq; WP_039461330.1; NZ_MPKQ01000008.1.
DR GeneID; 59230172; -.
DR Proteomes; UP000075346; Unassembled WGS sequence.
DR Proteomes; UP000075349; 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 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; 36811 MW; EA35217B6F724831 CRC64;
MFKKLRGMFS NDLSIDLGTA NTLIYVKGQG IVLDEPSVVA IRQDRAGSAK SVAAVGHAAK
QMLGRTPGNI SAIRPMKDGV IADFYVTEKM LQHFIKQVHD NSILKPSPRV LVCVPCGSTQ
VERRAIRESA LGAGAREVYL IDEPMAAAIG AGLRVSEPTG SMVVDIGGGT TEVAVISLNG
VVYSSSVRIG GDRFDEAIIN YVRRNYGSLI GEATAEKIKH EIGSAYPGDE VHEIEVRGRN
LAEGVPRSFS LNSNEILEAL QEPLSGIVSA VMVALEQCPP ELASDISENG MVLTGGGALL
KDLDRLLTEE TGIPVVIADD PLTCVARGGG KALEMIDMHG GDLFSEE
//
