ID A0A0B0ICX6_9BACI Unreviewed; 340 AA.
AC A0A0B0ICX6;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
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=LQ50_19520 {ECO:0000313|EMBL:KHF38747.1};
OS Halalkalibacter okhensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halalkalibacter.
OX NCBI_TaxID=333138 {ECO:0000313|EMBL:KHF38747.1, ECO:0000313|Proteomes:UP000030832};
RN [1] {ECO:0000313|EMBL:KHF38747.1, ECO:0000313|Proteomes:UP000030832}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Kh10-101T {ECO:0000313|Proteomes:UP000030832};
RA Prakash J.S.;
RT "Genome sequencing and annotation of Bacillus Okhensis strain Kh10-101T.";
RL Submitted (SEP-2014) 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:KHF38747.1}.
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DR EMBL; JRJU01000031; KHF38747.1; -; Genomic_DNA.
DR RefSeq; WP_034631997.1; NZ_JRJU01000031.1.
DR AlphaFoldDB; A0A0B0ICX6; -.
DR STRING; 333138.LQ50_19520; -.
DR eggNOG; COG1077; Bacteria.
DR OrthoDB; 9768127at2; -.
DR Proteomes; UP000030832; 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:SF4; CELL SHAPE-DETERMINING PROTEIN MBL; 1.
DR PANTHER; PTHR42749; 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:UP000030832}.
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 340 AA; 36765 MW; C691E324969DA1F8 CRC64;
MFGRDIGIDL GTANVLIYVK GSGIVLNEPS VVAVETTTNR VLAVGEEAFR MVGRTPGNIV
ALRPMKDGVI ANFEMTESML KHFLSKINVK SLFSKPRILI CCPTNITSVE QKAIREAAEK
SGGKNVYLEE EPKVAAIGAG MDIFQPSGNM VVDIGGGTTD VAVLSMGDIV TASSIKVAGD
RFDSDILAYI KKKYKLLIGE RTAENIKVQV ATVFPGARQE EIDIRGRDMV SGLPRTITVH
SKEIEEALME SVSYIVHASK QVLEQTPPEL SADIIDRGVI LTGGGALLHG IDQLLAEELK
VPVLVADEPM HCVAKGTGII LENLDRMSSK KYVFKRTSLR
//
