DIV4A_STRR6
ID DIV4A_STRR6 Reviewed; 262 AA.
AC Q8CWP9;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2012, sequence version 2.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Cell division protein DivIVA;
GN Name=divIVA; OrderedLocusNames=spr1505;
OS Streptococcus pneumoniae (strain ATCC BAA-255 / R6).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=171101;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-255 / R6;
RX PubMed=11544234; DOI=10.1128/jb.183.19.5709-5717.2001;
RA Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S.,
RA DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C.,
RA Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., LeBlanc D.J.,
RA Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., McAhren S.M., McHenney M.,
RA McLeaster K., Mundy C.W., Nicas T.I., Norris F.H., O'Gara M., Peery R.B.,
RA Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y.,
RA Young-Bellido M., Zhao G., Zook C.A., Baltz R.H., Jaskunas S.R.,
RA Rosteck P.R. Jr., Skatrud P.L., Glass J.I.;
RT "Genome of the bacterium Streptococcus pneumoniae strain R6.";
RL J. Bacteriol. 183:5709-5717(2001).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=Rx1;
RX PubMed=14526035; DOI=10.1128/jb.185.20.6209-6214.2003;
RA Fadda D., Pischedda C., Caldara F., Whalen M.B., Anderluzzi D.,
RA Domenici E., Massidda O.;
RT "Characterization of divIVA and other genes located in the chromosomal
RT region downstream of the dcw cluster in Streptococcus pneumoniae.";
RL J. Bacteriol. 185:6209-6214(2003).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, PROTEIN INTERACTION, DISRUPTION PHENOTYPE,
RP AND MUTAGENESIS OF ALA-78.
RC STRAIN=Rx1;
RX PubMed=17098892; DOI=10.1128/jb.01168-06;
RA Fadda D., Santona A., D'Ulisse V., Ghelardini P., Ennas M.G., Whalen M.B.,
RA Massidda O.;
RT "Streptococcus pneumoniae DivIVA: localization and interactions in a MinCD-
RT free context.";
RL J. Bacteriol. 189:1288-1298(2007).
RN [4]
RP PHOSPHORYLATION BY STKP, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=20453092; DOI=10.1128/jb.01564-09;
RA Novakova L., Bezouskova S., Pompach P., Spidlova P., Saskova L., Weiser J.,
RA Branny P.;
RT "Identification of multiple substrates of the StkP Ser/Thr protein kinase
RT in Streptococcus pneumoniae.";
RL J. Bacteriol. 192:3629-3638(2010).
RN [5]
RP PHOSPHORYLATION AT THR-201 BY STKP, PTM, AND MUTAGENESIS OF THR-201.
RC STRAIN=R6 / R800;
RX PubMed=22211696; DOI=10.1111/j.1365-2958.2011.07962.x;
RA Fleurie A., Cluzel C., Guiral S., Freton C., Galisson F., Zanella-Cleon I.,
RA Di Guilmi A.M., Grangeasse C.;
RT "Mutational dissection of the S/T-kinase StkP reveals crucial roles in cell
RT division of Streptococcus pneumoniae.";
RL Mol. Microbiol. 83:746-758(2012).
CC -!- FUNCTION: Appears to have a multifaceted role in controlling cell
CC morphology, completion of cell division and separation, as well as
CC chromosome segregation, through a complex interaction web. Seems to be
CC primarily involved in the formation and maturation of the cell poles.
CC {ECO:0000269|PubMed:14526035, ECO:0000269|PubMed:17098892}.
CC -!- SUBUNIT: Interacts with itself and with a number of cell division
CC proteins, including FtsZ and Spo0J.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17098892}.
CC Note=Localizes primarily near the membrane at the midcell division
CC sites (as a ring) and at the cell poles (as dots) simultaneously.
CC DivIVA is recruited to the septum at a later stage than FtsZ and is
CC retained at the poles after cell separation.
CC -!- PTM: Phosphorylated on Thr-201 by StkP in vivo. Phosphorylation would
CC regulate the scaffold DivIVA function directing cell wall synthesis and
CC the formation of mature poles. {ECO:0000269|PubMed:20453092,
CC ECO:0000269|PubMed:22211696}.
CC -!- DISRUPTION PHENOTYPE: Inactivation of divIVA results in severe growth
CC inhibition and defects in cell shape, nucleoid segregation, and cell
CC division, since it leads to the formation of chains of unseparated,
CC morphologically altered cells with incomplete septa, often devoid of
CC nucleoids (PubMed:14526035). However, a further study (PubMed:17098892)
CC showed that the anucleate cells observed in the divIVA null mutant
CC (corresponding to 15% to 20% of the population) were indeed dead cells
CC in the process of lysing. All the cell division proteins tested are
CC localized in the divIVA null mutant, although the percentage of cells
CC having constricted Z rings is significantly reduced (PubMed:17098892).
CC {ECO:0000269|PubMed:14526035, ECO:0000269|PubMed:17098892}.
CC -!- SIMILARITY: Belongs to the DivIVA family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL00309.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE007317; AAL00309.1; ALT_INIT; Genomic_DNA.
DR PIR; H98059; H98059.
DR RefSeq; NP_359098.1; NC_003098.1.
DR RefSeq; WP_001810114.1; NC_003098.1.
DR AlphaFoldDB; Q8CWP9; -.
DR SMR; Q8CWP9; -.
DR IntAct; Q8CWP9; 1.
DR STRING; 171101.spr1505; -.
DR iPTMnet; Q8CWP9; -.
DR PRIDE; Q8CWP9; -.
DR EnsemblBacteria; AAL00309; AAL00309; spr1505.
DR GeneID; 60234452; -.
DR GeneID; 66806736; -.
DR KEGG; spr:spr1505; -.
DR PATRIC; fig|171101.6.peg.1625; -.
DR eggNOG; COG3599; Bacteria.
DR HOGENOM; CLU_076854_0_0_9; -.
DR Proteomes; UP000000586; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000917; P:division septum assembly; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR InterPro; IPR019933; DivIVA_domain.
DR InterPro; IPR007793; DivIVA_fam.
DR PANTHER; PTHR35794; PTHR35794; 1.
DR Pfam; PF05103; DivIVA; 1.
DR TIGRFAMs; TIGR03544; DivI1A_domain; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cell shape; Coiled coil; Cytoplasm;
KW Phosphoprotein; Reference proteome; Septation.
FT CHAIN 1..262
FT /note="Cell division protein DivIVA"
FT /id="PRO_0000418151"
FT COILED 34..135
FT /evidence="ECO:0000255"
FT COILED 199..236
FT /evidence="ECO:0000255"
FT MOD_RES 201
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:22211696"
FT MUTAGEN 78
FT /note="A->T: Mutant cells are impaired in cell division
FT (they form chains) but not in chromosome segregation. They
FT display an altered localization profile, and although the
FT protein is still visible at the septum and the poles, the
FT majority is located diffusely around the cell. Still able
FT to self-interact. Some protein interactions are
FT significantly reduced or absent."
FT /evidence="ECO:0000269|PubMed:17098892"
FT MUTAGEN 201
FT /note="T->A: Loss of phosphorylation. Cells display
FT severely altered morphology compared with wild-type strain
FT cells. A significant number of cells has an elongated size
FT and forms a giant polar bulge, with a hampered septum
FT closure at the base of the bulge. These cells show a
FT diffuse spatial localization of nascent peptidoglycan
FT around the bulge, but more intense at the top of the bulge
FT (old cell pole)."
FT /evidence="ECO:0000269|PubMed:22211696"
SQ SEQUENCE 262 AA; 30185 MW; 446FBA7A863201A5 CRC64;
MPITSLEIKD KTFGTRFRGF DPEEVDEFLD IVVRDYEDLV RANHDKNLRI KSLEERLSYF
DEIKDSLSQS VLIAQDTAER VKQAAHERSN NIIHQAEQDA QRLLEEAKYK ANEILRQATD
NAKKVAVETE ELKNKSRVFH QRLKSTIESQ LAIVESSDWE DILRPTATYL QTSDEAFKEV
VSEVLGEPIP APIEEEPIDM TRQFSQAEME ELQARIEVAD KELSEFEAQI KQEVETPTPV
VSPQVEEEPL LIQLAQCMKN QK
