DIVIB_BACSU
ID DIVIB_BACSU Reviewed; 263 AA.
AC P16655;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Cell division protein DivIB {ECO:0000255|HAMAP-Rule:MF_00912};
DE AltName: Full=Cell division and sporulation protein;
DE AltName: Full=Division initiation protein DivIB;
GN Name=divIB {ECO:0000255|HAMAP-Rule:MF_00912}; Synonyms=dds;
GN OrderedLocusNames=BSU15240;
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=2556376; DOI=10.1128/jb.171.12.6835-6839.1989;
RA Harry E.J., Wake R.G.;
RT "Cloning and expression of a Bacillus subtilis division initiation gene for
RT which a homolog has not been identified in another organism.";
RL J. Bacteriol. 171:6835-6839(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2556375; DOI=10.1128/jb.171.12.6821-6834.1989;
RA Beall B., Lutkenhaus J.;
RT "Nucleotide sequence and insertional inactivation of a Bacillus subtilis
RT gene that affects cell division, sporulation, and temperature
RT sensitivity.";
RL J. Bacteriol. 171:6821-6834(1989).
RN [3]
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 [4]
RP SUBCELLULAR LOCATION.
RC STRAIN=168;
RX PubMed=10852898; DOI=10.1128/jb.182.12.3607-3611.2000;
RA Katis V.L., Wake R.G., Harry E.J.;
RT "Septal localization of the membrane-bound division proteins of Bacillus
RT subtilis DivIB and DivIC is codependent only at high temperatures and
RT requires FtsZ.";
RL J. Bacteriol. 182:3607-3611(2000).
RN [5]
RP FUNCTION.
RC STRAIN=168;
RX PubMed=10792716; DOI=10.1046/j.1365-2958.2000.01857.x;
RA Daniel R.A., Errington J.;
RT "Intrinsic instability of the essential cell division protein FtsL of
RT Bacillus subtilis and a role for DivIB protein in FtsL turnover.";
RL Mol. Microbiol. 36:278-289(2000).
RN [6]
RP FUNCTION IN SPORULATION.
RX PubMed=15659156; DOI=10.1111/j.1365-2958.2004.04399.x;
RA Real G., Autret S., Harry E.J., Errington J., Henriques A.O.;
RT "Cell division protein DivIB influences the Spo0J/Soj system of chromosome
RT segregation in Bacillus subtilis.";
RL Mol. Microbiol. 55:349-367(2005).
RN [7]
RP FUNCTION, INTERACTION WITH FTSL AND DIVIC, AND SUBUNIT.
RC STRAIN=168;
RX PubMed=16936019; DOI=10.1128/jb.01031-06;
RA Daniel R.A., Noirot-Gros M.F., Noirot P., Errington J.;
RT "Multiple interactions between the transmembrane division proteins of
RT Bacillus subtilis and the role of FtsL instability in divisome assembly.";
RL J. Bacteriol. 188:7396-7404(2006).
RN [8]
RP FUNCTION IN SPORULATION, AND DISRUPTION PHENOTYPE.
RX PubMed=16936026; DOI=10.1128/jb.01072-06;
RA Thompson L.S., Beech P.L., Real G., Henriques A.O., Harry E.J.;
RT "Requirement for the cell division protein DivIB in polar cell division and
RT engulfment during sporulation in Bacillus subtilis.";
RL J. Bacteriol. 188:7677-7685(2006).
RN [9]
RP SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF MET-37; ILE-41; LEU-44;
RP ILE-59; GLU-122; PRO-192; TYR-208 AND PRO-225.
RC STRAIN=168;
RX PubMed=18208530; DOI=10.1111/j.1365-2958.2008.06114.x;
RA Wadsworth K.D., Rowland S.L., Harry E.J., King G.F.;
RT "The divisomal protein DivIB contains multiple epitopes that mediate its
RT recruitment to incipient division sites.";
RL Mol. Microbiol. 67:1143-1155(2008).
RN [10]
RP FUNCTION, INTERACTION WITH PBP-2B, DOMAIN, AND MUTAGENESIS OF GLU-122;
RP LEU-139; GLU-140; ASN-141; SER-186; GLU-187; PRO-192; TYR-203; ASN-205;
RP ASP-206 AND TYR-246.
RC STRAIN=168;
RX PubMed=20870765; DOI=10.1128/jb.00783-10;
RA Rowland S.L., Wadsworth K.D., Robson S.A., Robichon C., Beckwith J.,
RA King G.F.;
RT "Evidence from artificial septal targeting and site-directed mutagenesis
RT that residues in the extracytoplasmic beta domain of DivIB mediate its
RT interaction with the divisomal transpeptidase PBP 2B.";
RL J. Bacteriol. 192:6116-6125(2010).
CC -!- FUNCTION: Cell division protein that may be involved in stabilizing or
CC promoting the assembly of the division complex. Plays an essential role
CC in division at high temperatures, maybe by protecting FtsL from
CC degradation or by promoting formation of the FtsL-DivIC complex. May
CC modulate the transpeptidase activity of PBP-2B. Also required for
CC efficient sporulation at all temperatures. Could be directly involved
CC in the engulfment process or be required to form a sporulation septum
CC competent for engulfment. Influences the Spo0J/Soj system of chromosome
CC segregation. {ECO:0000255|HAMAP-Rule:MF_00912,
CC ECO:0000269|PubMed:10792716, ECO:0000269|PubMed:15659156,
CC ECO:0000269|PubMed:16936019, ECO:0000269|PubMed:16936026,
CC ECO:0000269|PubMed:20870765}.
CC -!- SUBUNIT: Interacts with FtsL, DivIC and PBP-2B.
CC {ECO:0000269|PubMed:16936019, ECO:0000269|PubMed:20870765}.
CC -!- INTERACTION:
CC P16655; Q07868: pbpB; NbExp=3; IntAct=EBI-5243256, EBI-5243272;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00912,
CC ECO:0000269|PubMed:10852898, ECO:0000269|PubMed:18208530}; Single-pass
CC type II membrane protein {ECO:0000255|HAMAP-Rule:MF_00912,
CC ECO:0000269|PubMed:10852898, ECO:0000269|PubMed:18208530}.
CC Note=Localizes to the division septum. Localization requires FtsZ and
CC DivIC. Localization of DivIB and DivIC is codependent at high
CC temperatures.
CC -!- DOMAIN: The extracellular region contains three distinct subdomains: a
CC membrane proximal alpha domain, a central beta domain and an
CC unstructured C-terminal gamma domain. The C-terminal region of the beta
CC domain is critical for interaction with PBP-2B. Contains multiple
CC septal localization epitopes that are located within the transmembrane
CC region and within the extracellular region. These epitopes may
CC represent sites of interaction with other divisomal proteins.
CC {ECO:0000269|PubMed:18208530, ECO:0000269|PubMed:20870765}.
CC -!- DISRUPTION PHENOTYPE: Mutants show a drastic decrease in sporulation
CC efficiency. Polar septation is delayed and less efficient, and the
CC completed septa are thicker than those of the wild type. Mutants are
CC also unable to undergo engulfment. {ECO:0000269|PubMed:16936026}.
CC -!- SIMILARITY: Belongs to the FtsQ/DivIB family. DivIB subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00912}.
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DR EMBL; M31800; AAA22393.1; -; Genomic_DNA.
DR EMBL; M31827; AAA83970.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13397.1; -; Genomic_DNA.
DR PIR; B43727; B43727.
DR RefSeq; NP_389407.1; NC_000964.3.
DR RefSeq; WP_003232178.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; P16655; -.
DR IntAct; P16655; 12.
DR STRING; 224308.BSU15240; -.
DR jPOST; P16655; -.
DR PaxDb; P16655; -.
DR PRIDE; P16655; -.
DR EnsemblBacteria; CAB13397; CAB13397; BSU_15240.
DR GeneID; 939701; -.
DR KEGG; bsu:BSU15240; -.
DR PATRIC; fig|224308.179.peg.1662; -.
DR eggNOG; COG1589; Bacteria.
DR InParanoid; P16655; -.
DR OMA; YMNDGNE; -.
DR PhylomeDB; P16655; -.
DR BioCyc; BSUB:BSU15240-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0032153; C:cell division site; IEA:UniProtKB-UniRule.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0043093; P:FtsZ-dependent cytokinesis; IEA:UniProtKB-UniRule.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR HAMAP; MF_00912; DivIB; 1.
DR InterPro; IPR005548; Cell_div_FtsQ/DivIB_C.
DR InterPro; IPR026580; DivIB.
DR InterPro; IPR034746; POTRA.
DR InterPro; IPR013685; POTRA_FtsQ_type.
DR Pfam; PF03799; FtsQ; 1.
DR Pfam; PF08478; POTRA_1; 1.
DR PROSITE; PS51779; POTRA; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cell membrane; Membrane; Reference proteome;
KW Sporulation; Transmembrane; Transmembrane helix.
FT CHAIN 1..263
FT /note="Cell division protein DivIB"
FT /id="PRO_0000079921"
FT TOPO_DOM 1..32
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00912"
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00912"
FT TOPO_DOM 54..263
FT /note="Extracellular"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00912"
FT DOMAIN 54..123
FT /note="POTRA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01115"
FT REGION 51..123
FT /note="Alpha"
FT REGION 124..251
FT /note="Beta"
FT REGION 229..263
FT /note="Gamma"
FT MUTAGEN 37
FT /note="M->R: Does not affect septal localization; when
FT associated with R-41 and R-44."
FT /evidence="ECO:0000269|PubMed:18208530"
FT MUTAGEN 41
FT /note="I->R: Does not affect septal localization; when
FT associated with R-37 and R-44."
FT /evidence="ECO:0000269|PubMed:18208530"
FT MUTAGEN 44
FT /note="L->R: Does not affect septal localization; when
FT associated with R-37 and R-41."
FT /evidence="ECO:0000269|PubMed:18208530"
FT MUTAGEN 59
FT /note="I->P: Does not affect septal localization."
FT /evidence="ECO:0000269|PubMed:18208530"
FT MUTAGEN 122
FT /note="E->A: Does not affect septal localization and
FT growth."
FT /evidence="ECO:0000269|PubMed:18208530,
FT ECO:0000269|PubMed:20870765"
FT MUTAGEN 139
FT /note="L->A: Does not affect growth."
FT /evidence="ECO:0000269|PubMed:20870765"
FT MUTAGEN 140
FT /note="E->A: Does not affect growth."
FT /evidence="ECO:0000269|PubMed:20870765"
FT MUTAGEN 141
FT /note="N->A: Does not affect growth."
FT /evidence="ECO:0000269|PubMed:20870765"
FT MUTAGEN 186
FT /note="S->A: Does not affect growth."
FT /evidence="ECO:0000269|PubMed:20870765"
FT MUTAGEN 187
FT /note="E->A: Does not affect growth."
FT /evidence="ECO:0000269|PubMed:20870765"
FT MUTAGEN 192
FT /note="P->A: Does not affect septal localization and
FT growth."
FT /evidence="ECO:0000269|PubMed:18208530,
FT ECO:0000269|PubMed:20870765"
FT MUTAGEN 203
FT /note="Y->A: Does not affect growth."
FT /evidence="ECO:0000269|PubMed:20870765"
FT MUTAGEN 205
FT /note="N->A: Does not affect growth."
FT /evidence="ECO:0000269|PubMed:20870765"
FT MUTAGEN 206
FT /note="D->A: Does not affect growth."
FT /evidence="ECO:0000269|PubMed:20870765"
FT MUTAGEN 208
FT /note="Y->A: Does not affect septal localization."
FT /evidence="ECO:0000269|PubMed:18208530"
FT MUTAGEN 225
FT /note="P->A: Does not affect septal localization."
FT /evidence="ECO:0000269|PubMed:18208530"
FT MUTAGEN 246
FT /note="Y->A: Impairs cell growth."
FT /evidence="ECO:0000269|PubMed:20870765"
SQ SEQUENCE 263 AA; 30167 MW; 7CBEC797F4352864 CRC64;
MNPGQDREKI VNIEERIPKI KEQRKQKANR RLISFIMLFF IMVLIIVYLQ TPISKVSTIS
VTGNENVSKK EIIDLSDINS GDTEFWSLDK QKTEKKIQQN KLVKKAEISK SLPNKINIAI
EEYKAIAYLE KDDVYYEVLE NGSVLPNEVT PDDAGPILVN WTNAKKRSQM AKQLDALSNS
LKQSISEIYY TPVKMDENRI KLYMNDGYVV TASIKTFADR MKTYPSIISQ LSSNKKGIIH
LEVATYFEEF GKNDKAAKKE DEN
