ID A0A1M5TQR4_9BACT Unreviewed; 335 AA.
AC A0A1M5TQR4;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-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=SAMN02745199_1462 {ECO:0000313|EMBL:SHH53102.1};
OS Thermosipho atlanticus DSM 15807.
OC Bacteria; Thermotogota; Thermotogae; Thermotogales; Fervidobacteriaceae;
OC Thermosipho.
OX NCBI_TaxID=1123380 {ECO:0000313|EMBL:SHH53102.1, ECO:0000313|Proteomes:UP000242592};
RN [1] {ECO:0000313|Proteomes:UP000242592}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15807 {ECO:0000313|Proteomes:UP000242592};
RA Varghese N., Submissions S.;
RL Submitted (NOV-2016) 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; FQXN01000005; SHH53102.1; -; Genomic_DNA.
DR RefSeq; WP_073073653.1; NZ_FQXN01000005.1.
DR AlphaFoldDB; A0A1M5TQR4; -.
DR STRING; 1123380.SAMN02745199_1462; -.
DR OrthoDB; 9768127at2; -.
DR Proteomes; UP000242592; 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:UP000242592}.
FT BINDING 12..14
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT BINDING 156..158
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT BINDING 204..207
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT BINDING 284..287
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
SQ SEQUENCE 335 AA; 35704 MW; BADBBF2E0D0BDBCF CRC64;
MGKNDLGIDL GTANFIVYQK GKGIVLYQPS VVAISKKTGK IVAIGDEAKE MLGKTPEDII
TAVRPMKDGV IADYTIISEV LQIFIKKVTK GFLFKPNMVI GIPAKTTTVE KRAVFDAALN
AGAKKVYVVS EPLAAAIGSG IDVTKPRGNM IIDIGGGTTD IAVISLGGIV VGDSIKLAGD
AMNDIIVKSI RKLFGLIIGE STAEEIKMKV GKAHSDIEDI EMEIKGRDAV TGLPRIDVIN
SQHIYEMLKP LIENLVSKIK IVLEKTPPEL SADIMEQGIT LTGGGSLLRG IDKAIYDEIG
VPCKIADDPM TCVARGTGIL LDDEELLEQV AATYE
//
