MBL_BACSU
ID MBL_BACSU Reviewed; 333 AA.
AC P39751; O32275;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Cell shape-determining protein Mbl {ECO:0000305};
DE AltName: Full=Actin-like Mbl protein {ECO:0000305};
DE AltName: Full=Rod shape-determining protein Mbl {ECO:0000305};
GN Name=mbl; OrderedLocusNames=BSU36410;
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;
RX PubMed=7836311; DOI=10.1128/jb.177.3.765-773.1995;
RA Abhayawardhane Y., Stewart G.C.;
RT "Bacillus subtilis possesses a second determinant with extensive sequence
RT similarity to the Escherichia coli mreB morphogene.";
RL J. Bacteriol. 177:765-773(1995).
RN [2]
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 [3]
RP SEQUENCE REVISION.
RX PubMed=10568751; DOI=10.1101/gr.9.11.1116;
RA Medigue C., Rose M., Viari A., Danchin A.;
RT "Detecting and analyzing DNA sequencing errors: toward a higher quality of
RT the Bacillus subtilis genome sequence.";
RL Genome Res. 9:1116-1127(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-301.
RC STRAIN=168;
RX PubMed=9353933; DOI=10.1099/00221287-143-10-3313;
RA Presecan E., Moszer I., Boursier L., Cruz Ramos H., De La Fuente V.,
RA Hullo M.-F., Lelong C., Schleich S., Sekowska A., Song B.H., Villani G.,
RA Kunst F., Danchin A., Glaser P.;
RT "The Bacillus subtilis genome from gerBC (311 degrees) to licR (334
RT degrees).";
RL Microbiology 143:3313-3328(1997).
RN [5]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=11290328; DOI=10.1016/s0092-8674(01)00287-2;
RA Jones L.J., Carballido-Lopez R., Errington J.;
RT "Control of cell shape in bacteria: helical, actin-like filaments in
RT Bacillus subtilis.";
RL Cell 104:913-922(2001).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=14588250; DOI=10.1016/j.cub.2003.10.024;
RA Soufo H.J., Graumann P.L.;
RT "Actin-like proteins MreB and Mbl from Bacillus subtilis are required for
RT bipolar positioning of replication origins.";
RL Curr. Biol. 13:1916-1920(2003).
RN [7]
RP SUBCELLULAR LOCATION.
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 [8]
RP INTERACTION WITH MREB; MREBH AND MREC, AND SUBCELLULAR LOCATION.
RX PubMed=17064365; DOI=10.1111/j.1365-2958.2006.05457.x;
RA Defeu Soufo H.J., Graumann P.L.;
RT "Dynamic localization and interaction with other Bacillus subtilis actin-
RT like proteins are important for the function of MreB.";
RL Mol. Microbiol. 62:1340-1356(2006).
RN [9]
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 [10]
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 [11]
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).
CC -!- FUNCTION: Forms membrane-associated dynamic filaments that are
CC essential for cell shape determination (PubMed:11290328,
CC PubMed:19659933). Acts by regulating cell wall synthesis and cell
CC elongation, and thus cell shape (PubMed:19659933). A feedback loop
CC between cell geometry and Mbl localization may maintain elongated cell
CC shape by targeting cell wall growth to regions of negative cell wall
CC curvature (By similarity). Filaments rotate around the cell
CC circumference in concert with the cell wall synthesis enzymes. The
CC process is driven by the cell wall synthesis machinery and does not
CC depend on Mbl polymerization (PubMed:21636745, PubMed:21636744).
CC Organizes peptidoglycan synthesis in the lateral cell wall
CC (PubMed:19659933). Also required for proper chromosome segregation
CC (PubMed:14588250). {ECO:0000250|UniProtKB:P0A9X4,
CC ECO:0000269|PubMed:11290328, ECO:0000269|PubMed:14588250,
CC ECO:0000269|PubMed:19659933, ECO:0000269|PubMed:21636744,
CC ECO:0000269|PubMed:21636745}.
CC -!- SUBUNIT: Forms polymers (PubMed:11290328, PubMed:19659933). Forms a
CC complex with MreB and MreBH (PubMed:17064365, PubMed:19659933).
CC Interacts with MreC (PubMed:17064365). {ECO:0000269|PubMed:11290328,
CC ECO:0000269|PubMed:17064365, ECO:0000269|PubMed:19659933}.
CC -!- INTERACTION:
CC P39751; P33166: tuf; NbExp=3; IntAct=EBI-2122805, EBI-2122675;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17064365,
CC ECO:0000305|PubMed:11290328}. Note=Membrane-associated
CC (PubMed:17064365). Localizes in the form of helical filaments that run
CC the length of the cell (PubMed:11290328). Colocalizes with MreB, MreBH
CC and MreC (PubMed:16950129, PubMed:17064365).
CC {ECO:0000269|PubMed:11290328, ECO:0000269|PubMed:16950129,
CC ECO:0000269|PubMed:17064365}.
CC -!- DISRUPTION PHENOTYPE: Mutants are bent and twisted at irregular angles
CC (PubMed:11290328). Depletion leads to a strong defect in chromosome
CC segregation (PubMed:14588250). {ECO:0000269|PubMed:11290328,
CC ECO:0000269|PubMed:14588250}.
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}.
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DR EMBL; U12962; AAA67878.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15658.2; -; Genomic_DNA.
DR EMBL; Z82987; CAB05381.1; -; Genomic_DNA.
DR PIR; I40531; I40531.
DR RefSeq; NP_391522.2; NC_000964.3.
DR RefSeq; WP_003227776.1; NZ_JNCM01000034.1.
DR AlphaFoldDB; P39751; -.
DR SMR; P39751; -.
DR DIP; DIP-52430N; -.
DR IntAct; P39751; 2.
DR STRING; 224308.BSU36410; -.
DR jPOST; P39751; -.
DR PaxDb; P39751; -.
DR PRIDE; P39751; -.
DR EnsemblBacteria; CAB15658; CAB15658; BSU_36410.
DR GeneID; 936916; -.
DR KEGG; bsu:BSU36410; -.
DR PATRIC; fig|224308.179.peg.3941; -.
DR eggNOG; COG1077; Bacteria.
DR InParanoid; P39751; -.
DR OMA; MDIFQPS; -.
DR PhylomeDB; P39751; -.
DR BioCyc; BSUB:BSU36410-MON; -.
DR Proteomes; UP000001570; 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 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; Nucleotide-binding; Reference proteome.
FT CHAIN 1..333
FT /note="Cell shape-determining protein Mbl"
FT /id="PRO_0000062755"
FT BINDING 12..14
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02207"
FT BINDING 156..158
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02207"
FT BINDING 204..207
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02207"
FT BINDING 284..287
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02207"
SQ SEQUENCE 333 AA; 35861 MW; D1599B7EEDEAF8A9 CRC64;
MFARDIGIDL GTANVLIHVK GKGIVLNEPS VVALDKNSGK VLAVGEEARR MVGRTPGNIV
AIRPLKDGVI ADFEVTEAML KHFINKLNVK GLFSKPRMLI CCPTNITSVE QKAIKEAAEK
SGGKHVYLEE EPKVAAIGAG MEIFQPSGNM VVDIGGGTTD IAVISMGDIV TSSSIKMAGD
KFDMEILNYI KREYKLLIGE RTAEDIKIKV ATVFPDARHE EISIRGRDMV SGLPRTITVN
SKEVEEALRE SVAVIVQAAK QVLERTPPEL SADIIDRGVI ITGGGALLNG LDQLLAEELK
VPVLVAENPM DCVAIGTGVM LDNMDKLPKR KLS
