MREBH_BACSU
ID MREBH_BACSU Reviewed; 335 AA.
AC P39763;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Cell shape-determining protein MreBH {ECO:0000305};
DE AltName: Full=Actin-like MreBH protein {ECO:0000305};
DE AltName: Full=Rod shape-determining protein MreBH {ECO:0000305};
GN Name=mreBH; OrderedLocusNames=BSU14470;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / JH642;
RA Kobayashi K., Sato T., Kobayashi Y.;
RT "The nucleotide sequence analysis of kinC region.";
RL Submitted (JUL-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=8969500; DOI=10.1099/13500872-142-11-3033;
RA Winters P., Caldwell R.M., Enfield L., Ferrari E.;
RT "The ampS-nprE (124 degrees-127 degrees) region of the Bacillus subtilis
RT 168 chromosome: sequencing of a 27 kb segment and identification of several
RT genes in the area.";
RL Microbiology 142:3033-3037(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RA Caldwell R.M., Ferrari E.;
RT "Sequence analysis of the mobA-ampS region of the Bacillus subtilis
RT chromosome.";
RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [5]
RP FUNCTION, SUBUNIT, INTERACTION WITH LYTE, SUBCELLULAR LOCATION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=16950129; DOI=10.1016/j.devcel.2006.07.017;
RA Carballido-Lopez R., Formstone A., Li Y., Ehrlich S.D., Noirot P.,
RA Errington J.;
RT "Actin homolog MreBH governs cell morphogenesis by localization of the cell
RT wall hydrolase LytE.";
RL Dev. Cell 11:399-409(2006).
RN [6]
RP INDUCTION.
RC STRAIN=168;
RX PubMed=18156261; DOI=10.1128/jb.01497-07;
RA Tseng C.-L., Shaw G.-C.;
RT "Genetic evidence for the actin homolog gene mreBH and the bacitracin
RT resistance gene bcrC as targets of the alternative sigma factor sigI of
RT Bacillus subtilis.";
RL J. Bacteriol. 190:1561-1567(2008).
RN [7]
RP FUNCTION, AND SUBUNIT.
RX PubMed=19659933; DOI=10.1111/j.1365-2958.2009.06805.x;
RA Kawai Y., Asai K., Errington J.;
RT "Partial functional redundancy of MreB isoforms, MreB, Mbl and MreBH, in
RT cell morphogenesis of Bacillus subtilis.";
RL Mol. Microbiol. 73:719-731(2009).
RN [8]
RP FUNCTION.
RX PubMed=21636745; DOI=10.1126/science.1203285;
RA Garner E.C., Bernard R., Wang W., Zhuang X., Rudner D.Z., Mitchison T.;
RT "Coupled, circumferential motions of the cell wall synthesis machinery and
RT MreB filaments in B. subtilis.";
RL Science 333:222-225(2011).
RN [9]
RP FUNCTION.
RX PubMed=21636744; DOI=10.1126/science.1203466;
RA Dominguez-Escobar J., Chastanet A., Crevenna A.H., Fromion V.,
RA Wedlich-Soeldner R., Carballido-Lopez R.;
RT "Processive movement of MreB-associated cell wall biosynthetic complexes in
RT bacteria.";
RL Science 333:225-228(2011).
RN [10]
RP SUBCELLULAR LOCATION.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=22882210; DOI=10.1111/j.1365-2958.2012.08205.x;
RA Yepes A., Schneider J., Mielich B., Koch G., Garcia-Betancur J.C.,
RA Ramamurthi K.S., Vlamakis H., Lopez D.;
RT "The biofilm formation defect of a Bacillus subtilis flotillin-defective
RT mutant involves the protease FtsH.";
RL Mol. Microbiol. 86:457-471(2012).
CC -!- FUNCTION: Forms membrane-associated dynamic filaments that are
CC essential for cell shape determination (PubMed:16950129,
CC PubMed:19659933). Acts by regulating cell wall synthesis and cell
CC elongation, and thus cell shape (PubMed:16950129, PubMed:19659933). A
CC feedback loop between cell geometry and MreBH localization may maintain
CC elongated cell shape by targeting cell wall growth to regions of
CC negative cell wall curvature (By similarity). Filaments rotate around
CC the cell circumference in concert with the cell wall synthesis enzymes.
CC The process is driven by the cell wall synthesis machinery and does not
CC depend on MreBH polymerization (PubMed:21636745, PubMed:21636744).
CC Organizes peptidoglycan synthesis in the lateral cell wall
CC (PubMed:19659933). Required for the localization of the cell wall
CC hydrolase LytE into the cylindrical part of the cell wall
CC (PubMed:16950129). {ECO:0000250|UniProtKB:P0A9X4,
CC ECO:0000269|PubMed:16950129, ECO:0000269|PubMed:19659933,
CC ECO:0000269|PubMed:21636744, ECO:0000269|PubMed:21636745}.
CC -!- SUBUNIT: Forms polymers (PubMed:16950129). Forms a complex with Mbl and
CC MreB (PubMed:19659933). Interacts with the C-terminal catalytic domain
CC of LytE (PubMed:16950129). {ECO:0000269|PubMed:16950129,
CC ECO:0000269|PubMed:19659933}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16950129}. Membrane
CC raft {ECO:0000269|PubMed:22882210}. Note=Membrane-associated.
CC Colocalizes with MreB and Mbl (PubMed:16950129). Present in detergent-
CC resistant membrane (DRM) fractions that may be equivalent to eukaryotic
CC membrane rafts; these rafts include proteins involved in signaling,
CC molecule trafficking and protein secretion (PubMed:22882210).
CC {ECO:0000269|PubMed:16950129, ECO:0000269|PubMed:22882210}.
CC -!- INDUCTION: Expression is sigma I-dependent.
CC {ECO:0000269|PubMed:18156261}.
CC -!- DISRUPTION PHENOTYPE: Disruption of the gene leads to cells that are
CC curved, bent at irregular angles and affected in length and width.
CC {ECO:0000269|PubMed:16950129}.
CC -!- MISCELLANEOUS: B.subtilis has three MreB paralogs: MreB, Mbl and MreBH.
CC All paralogs have the ability to support rod-shaped cell growth normal
CC conditions. The multiplicity of paralogs becomes important under stress
CC conditions. They are probably used to allow cells to maintain proper
CC growth and morphogenesis under changing conditions.
CC {ECO:0000269|PubMed:19659933}.
CC -!- SIMILARITY: Belongs to the FtsA/MreB family. {ECO:0000255|HAMAP-
CC Rule:MF_02207, ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D37799; BAA07047.1; -; Genomic_DNA.
DR EMBL; AF012285; AAC24922.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13320.1; -; Genomic_DNA.
DR PIR; C69660; C69660.
DR RefSeq; NP_389330.1; NC_000964.3.
DR RefSeq; WP_003245743.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; P39763; -.
DR SMR; P39763; -.
DR STRING; 224308.BSU14470; -.
DR PaxDb; P39763; -.
DR PRIDE; P39763; -.
DR EnsemblBacteria; CAB13320; CAB13320; BSU_14470.
DR GeneID; 938746; -.
DR KEGG; bsu:BSU14470; -.
DR PATRIC; fig|224308.179.peg.1577; -.
DR eggNOG; COG1077; Bacteria.
DR InParanoid; P39763; -.
DR OMA; NTLEMCP; -.
DR PhylomeDB; P39763; -.
DR BioCyc; BSUB:BSU14470-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0045121; C:membrane raft; 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 HAMAP; MF_02207; MreB; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR004753; MreB.
DR PRINTS; PR01652; SHAPEPROTEIN.
DR SUPFAM; SSF53067; SSF53067; 2.
DR TIGRFAMs; TIGR00904; mreB; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell shape; Cytoplasm; Membrane; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..335
FT /note="Cell shape-determining protein MreBH"
FT /id="PRO_0000062757"
FT BINDING 13..15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02207"
FT BINDING 159..161
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02207"
FT BINDING 207..210
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02207"
FT BINDING 287..290
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02207"
SQ SEQUENCE 335 AA; 35687 MW; 699784E5531323DD CRC64;
MFQSTEIGID LGTANILVYS KNKGIILNEP SVVAVDTTTK AVLAIGADAK NMIGKTPGKI
VAVRPMKDGV IADYDMTTDL LKHIMKKAAK SIGMSFRKPN VVVCTPSGST AVERRAISDA
VKNCGAKNVH LIEEPVAAAI GADLPVDEPV ANVVVDIGGG TTEVAIISFG GVVSCHSIRI
GGDQLDEDIV SFVRKKYNLL IGERTAEQVK MEIGHALIEH IPEAMEIRGR DLVTGLPKTI
MLQSNEIQDA MRESLLHILE AIRATLEDCP PELSGDIVDR GVILTGGGAL LNGIKEWLTE
EIVVPVHVAQ NPLESVAIGT GRSLEVIDKL QKAIK
