ID A0A220S405_9NEIS Unreviewed; 345 AA.
AC A0A220S405;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, 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 ORFNames=BG910_11350 {ECO:0000313|EMBL:ASK28249.1};
OS Neisseria chenwenguii.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=1853278 {ECO:0000313|EMBL:ASK28249.1, ECO:0000313|Proteomes:UP000198238};
RN [1] {ECO:0000313|EMBL:ASK28249.1, ECO:0000313|Proteomes:UP000198238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=10023 {ECO:0000313|EMBL:ASK28249.1,
RC ECO:0000313|Proteomes:UP000198238};
RA Zhang G.;
RT "Neisseria chenwenguii sp. nov., isolated from the intestinal contents of
RT Tibetan Plateau Pika in Yushu, Qinghai Province, China.";
RL Submitted (JUN-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; CP022278; ASK28249.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A220S405; -.
DR KEGG; nei:BG910_11350; -.
DR Proteomes; UP000198238; Chromosome.
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:UP000198238}.
FT BINDING 19..21
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT BINDING 166..168
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT BINDING 214..217
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT BINDING 294..297
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
SQ SEQUENCE 345 AA; 36285 MW; 0EBED51B4412FF61 CRC64;
MFRFLSNYFS NDIAIDLGTA NTLIFVRGRG IVLDEPSMVA LQAGVLGGKN RIVAVGMEAK
KMQGRAPKNI EIVRPMKDGV IADFELTERM LGILIKKAVG KVVVPPRIVI CVPGGATPVE
RKVIRDSAFA AGASSVHLIE EPMAAALGAR LPVEEAAGSM IVDIGGGTTE IGILSLGGMA
YSDSVRVGGD AFDESIVHYL RRNRGILIGE ATAEELKKEI GTVFGREATT ALRIKGRDLA
EGTPKSLAVT SDEVREALSE PLNQIIRAVR LALEQAPPEL AGDIADRGIM LTGGGALLRG
IDGVLADATG LPVGIADEPL NCVAYGCGQA LEYIGKWDAV FADQV
//
