ID A0A0J7IV56_9FLAO Unreviewed; 341 AA.
AC A0A0J7IV56;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 32.
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=ACM39_02350 {ECO:0000313|EMBL:KMQ69902.1};
OS Chryseobacterium sp. FH2.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Chryseobacterium.
OX NCBI_TaxID=1674291 {ECO:0000313|EMBL:KMQ69902.1, ECO:0000313|Proteomes:UP000036315};
RN [1] {ECO:0000313|EMBL:KMQ69902.1, ECO:0000313|Proteomes:UP000036315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FH2 {ECO:0000313|EMBL:KMQ69902.1,
RC ECO:0000313|Proteomes:UP000036315};
RA Stropko S.J., Miller J.R., Newman J.D.;
RL Submitted (JUN-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:KMQ69902.1}.
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DR EMBL; LFNE01000001; KMQ69902.1; -; Genomic_DNA.
DR RefSeq; WP_034700899.1; NZ_LFNE01000001.1.
DR AlphaFoldDB; A0A0J7IV56; -.
DR STRING; 1674291.ACM39_02350; -.
DR PATRIC; fig|1674291.3.peg.478; -.
DR OrthoDB; 9768127at2; -.
DR Proteomes; UP000036315; 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 17..19
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT BINDING 163..165
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT BINDING 211..214
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT BINDING 293..296
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
SQ SEQUENCE 341 AA; 37245 MW; 07B24C27EFFF792C CRC64;
MSLFDMFTQE IAIDLGTANT LIIHNNKIVI DQPSIVAIER STGRPIAVGE QAKHMQGKTH
EDIKTIRPLK DGVIADFHAS EHMIKEFIKK IPGIKGRFIQ PALRIVICIP SGITEVEKRA
VRDSAQKVNA KEVRLIYEPM AAAIGVGIDV QKPEGNMIID IGGGTTEIAV VALGGIVCDK
SVKIAGDVFT NDIAYYLRTH HNLYIGERTA ERIKIEVGSA VEDLDVDIED IPVQGRDLIT
GKPKEIMVGY KEIARALDKS IIRIEDAVME TLSLTPPELA ADIYKTGIYL AGGGALLRGL
ADRLHKKTGL PVFVAEDPLR AVVRGTGIAL KNMDKFNFLI K
//
