ID A0A1B6AKV4_9ACTN Unreviewed; 343 AA.
AC A0A1B6AKV4;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Cell shape-determining protein MreB {ECO:0000256|HAMAP-Rule:MF_02207};
GN Name=mreB {ECO:0000256|HAMAP-Rule:MF_02207,
GN ECO:0000313|EMBL:GAU68190.1};
GN ORFNames=SSP35_06_02790 {ECO:0000313|EMBL:GAU68190.1};
OS Streptomyces sp. NBRC 110611.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1621259 {ECO:0000313|EMBL:GAU68190.1, ECO:0000313|Proteomes:UP000094479};
RN [1] {ECO:0000313|EMBL:GAU68190.1, ECO:0000313|Proteomes:UP000094479}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 110611 {ECO:0000313|EMBL:GAU68190.1,
RC ECO:0000313|Proteomes:UP000094479};
RA Igarashi Y., Komaki H., Ichikawa N., Hosoyama A., Fujita N., Panbangred W.;
RT "Whole genome shotgun sequence of Streptomyces sp. NBRC 110611.";
RL Submitted (MAR-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:GAU68190.1}.
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DR EMBL; BBUY01000006; GAU68190.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B6AKV4; -.
DR STRING; 1621259.GCA_001590865_03499; -.
DR Proteomes; UP000094479; 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:UP000094479}.
FT BINDING 18..20
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 290..293
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
SQ SEQUENCE 343 AA; 36664 MW; A39776F397FD4B48 CRC64;
MGNNMSFIGR DMAVDLGTAN TLVYVRGRGI VLNEPSVVAI NTNTGGILAV GAEAKKMIGR
TPGNIVAVRP LKDGVIADFE ITERMLRYFI LKIHKRRYLA RPRVVVCVPS GITGVERRAV
IEASTQAGAR QVHIIEEPMA AAIGSGLPVH EATGNMVVDI GGGTTEVAVI SLGGIVTAQS
IRVAGDELDN AIIQHIKKEY SLLLGERTAE SIKITIGSAY DLEQDEHTEI RGRDLVSGLP
KTVVISAAEV RKAIEEPVNS IVDAVKTTLD KCPPELSGDV MDRGIVLTGG GALLRGLDER
LRRETGMPIH IAEDPLDSVA LGSGKCVEEF EALQQVLDSQ PRR
//
