ID X2HFY0_9NEIS Unreviewed; 345 AA.
AC X2HFY0;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 35.
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=SALWKB2_1104 {ECO:0000313|EMBL:AHN28486.1};
OS Snodgrassella alvi wkB2.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Snodgrassella.
OX NCBI_TaxID=1196094 {ECO:0000313|EMBL:AHN28486.1, ECO:0000313|Proteomes:UP000019668};
RN [1] {ECO:0000313|EMBL:AHN28486.1, ECO:0000313|Proteomes:UP000019668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WkB2 {ECO:0000313|EMBL:AHN28486.1};
RX PubMed=25053814;
RA Kwong W.K., Engel P., Koch H., Moran N.A.;
RT "Genomics and host specialization of honey bee and bumble bee gut
RT symbionts.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:11509-11514(2014).
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; CP007446; AHN28486.1; -; Genomic_DNA.
DR RefSeq; WP_025330699.1; NZ_CP091515.1.
DR AlphaFoldDB; X2HFY0; -.
DR STRING; 1196094.SALWKB2_1104; -.
DR GeneID; 32538235; -.
DR KEGG; salv:SALWKB2_1104; -.
DR PATRIC; fig|1196094.4.peg.1105; -.
DR HOGENOM; CLU_052037_0_0_4; -.
DR OrthoDB; 9768127at2; -.
DR Proteomes; UP000019668; 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}.
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; 36480 MW; 31D8175BA9AFDAEA CRC64;
MFRFFSKYLS NDLAIDLGTA NTLIFIKNKG IVLNEPSVVA VQNDTINAKN GMLAVGTAAK
KMLGRTPGSI QAIRPMKDGV IADFNVTEKM LKQFIKKVNN SRFTAPRIVI CVPCGSTQVE
RKAIRDSALA AGASIVNLIE EPMAAAIGAG LPIEEPTGSM VVDIGGGTTE VGVISLSGVV
YSHSIRVGGD AFDDAIINYV RRNYGMLIGE STAEEIKKNI GSAFPGMEVK EIEVKGRNLA
EGIPRAFTIS SNEVLEALTE PLNQIVQAVK NALEQTPPEL GADIADRGLV LTGGGALLKG
LDRLLSEETG LPVMIAEDPL TCVARGSGHA LDMIGKMNSV FVSNP
//
