ID A0A1T5B353_9SPHI Unreviewed; 340 AA.
AC A0A1T5B353;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
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=SAMN05660226_01314 {ECO:0000313|EMBL:SKB41711.1};
OS Parapedobacter luteus.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Parapedobacter.
OX NCBI_TaxID=623280 {ECO:0000313|EMBL:SKB41711.1, ECO:0000313|Proteomes:UP000190541};
RN [1] {ECO:0000313|EMBL:SKB41711.1, ECO:0000313|Proteomes:UP000190541}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22899 {ECO:0000313|EMBL:SKB41711.1,
RC ECO:0000313|Proteomes:UP000190541};
RA Peterson S.W.;
RL Submitted (FEB-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}.
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DR EMBL; FUYS01000002; SKB41711.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T5B353; -.
DR STRING; 623280.SAMN05660226_01314; -.
DR OrthoDB; 9768127at2; -.
DR Proteomes; UP000190541; 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:UP000190541}.
FT BINDING 17..19
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT BINDING 162..164
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT BINDING 210..213
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT BINDING 292..295
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
SQ SEQUENCE 340 AA; 37057 MW; 562B79497F6616BA CRC64;
MGLFNWFTQE VAIDLGTANT LIIHNDKVVV DEPSIVAFDR TTNKVIAIGR QAMQMEGKTH
DNIRTVRPLK DGVIADFNAA EHMIRGMIKM VNNGKGWFFP SLRMVICIPS GITEVEKRAV
RDSAEIAGAK EVYLVHEPMA AAVGIGIDVE EPMGNMVIDI GGGTTEIAVI ALSGIVCDQS
IRVAGDNFDS DIVQYIRRQH NIMIGDRTAE KIKIEVGSAL PELQDPPDDF AVQGRDLMTG
VPKQITVSYT EIAHCLDKSI SKIEEAILKA LEITPPELSA DIYQTGIYLT GGGALLRGLD
KRIQAKTKLP VHVAEDPLRA VVRGTGIALK NIGTFKFLMQ
//
