ID A0A1S1XD09_9NEIS Unreviewed; 347 AA.
AC A0A1S1XD09;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
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=BUE93_19770 {ECO:0000313|EMBL:PRP68981.1};
OS Chromobacterium amazonense.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC Chromobacteriaceae; Chromobacterium.
OX NCBI_TaxID=1382803 {ECO:0000313|EMBL:PRP68981.1, ECO:0000313|Proteomes:UP000239469};
RN [1] {ECO:0000313|EMBL:PRP68981.1, ECO:0000313|Proteomes:UP000239469}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=56AF {ECO:0000313|EMBL:PRP68981.1,
RC ECO:0000313|Proteomes:UP000239469};
RA Santos A.B., Nascimento A.M., Da Silva P.C.;
RT "New insights into the genetic diversity of Chromobacterium isolated from
RT tropical freshwater lake.";
RL Submitted (JAN-2017) 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:PRP68981.1}.
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DR EMBL; MTBD01000036; PRP68981.1; -; Genomic_DNA.
DR RefSeq; WP_043623769.1; NZ_MTBD01000036.1.
DR AlphaFoldDB; A0A1S1XD09; -.
DR OrthoDB; 9768127at2; -.
DR Proteomes; UP000239469; 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; 36916 MW; 815ADD4F978E5825 CRC64;
MFRSLTGYFS NDLAIDLGTA NTLIYMRSKG IVLDEPSVVA IHSDAPTNKK SILAVGLEAK
RMLGRTPGSI QAIRPMKDGV IADFTVTEQM LKQFIKKVNP NRFFAASPRI VICVPCGSTQ
VERKAIRDSA LAAGARRVEL IEEPMAAAIG AGLPVEEPTG SMVVDIGGGT TEVGVISLGG
VVYSNSVRVG GDKFDEAIIN YIRRNYGMLI GETTAEEIKK TIGSAFPGAE VREMEVKGRN
LAEGIPRAFT VSSNEILEAL TEPLNQIVSA VKIALEQTPP ELGADIAEKG MVLTGGGALL
KDIDRLLAEE TGLPVFVAEE PLTCVVRGSG KALEKMDKIG TIFTNVP
//
