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Mid-cell-anchored protein Z

 MAPZ_STRR6              Reviewed;         464 AA.
Q8DR55;
11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 1.
25-OCT-2017, entry version 70.
RecName: Full=Mid-cell-anchored protein Z {ECO:0000255|HAMAP-Rule:MF_01941, ECO:0000303|PubMed:25470041};
Name=mapZ {ECO:0000255|HAMAP-Rule:MF_01941,
ECO:0000303|PubMed:25470041};
Synonyms=locZ {ECO:0000303|PubMed:25550321};
OrderedLocusNames=spr0334 {ECO:0000312|EMBL:AAK99138.1};
Streptococcus pneumoniae (strain ATCC BAA-255 / R6).
Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
Streptococcus.
NCBI_TaxID=171101;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC BAA-255 / R6;
PubMed=11544234; DOI=10.1128/JB.183.19.5709-5717.2001;
Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S.,
DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C.,
Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E.,
LeBlanc D.J., Lee L.N., Lefkowitz E.J., Lu J., Matsushima P.,
McAhren S.M., McHenney M., McLeaster K., Mundy C.W., Nicas T.I.,
Norris F.H., O'Gara M., Peery R.B., Robertson G.T., Rockey P.,
Sun P.-M., Winkler M.E., Yang Y., Young-Bellido M., Zhao G.,
Zook C.A., Baltz R.H., Jaskunas S.R., Rosteck P.R. Jr., Skatrud P.L.,
Glass J.I.;
"Genome of the bacterium Streptococcus pneumoniae strain R6.";
J. Bacteriol. 183:5709-5717(2001).
[2]
PHOSPHORYLATION BY STKP, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=20453092; DOI=10.1128/JB.01564-09;
Novakova L., Bezouskova S., Pompach P., Spidlova P., Saskova L.,
Weiser J., Branny P.;
"Identification of multiple substrates of the StkP Ser/Thr protein
kinase in Streptococcus pneumoniae.";
J. Bacteriol. 192:3629-3638(2010).
[3]
FUNCTION, INTERACTION WITH FTSZ, SUBCELLULAR LOCATION, TOPOLOGY,
DOMAIN, PHOSPHORYLATION AT THR-67 AND THR-78, AND DISRUPTION
PHENOTYPE.
STRAIN=R6 / R800;
PubMed=25470041; DOI=10.1038/nature13966;
Fleurie A., Lesterlin C., Manuse S., Zhao C., Cluzel C.,
Lavergne J.P., Franz-Wachtel M., Macek B., Combet C., Kuru E.,
VanNieuwenhze M.S., Brun Y.V., Sherratt D., Grangeasse C.;
"MapZ marks the division sites and positions FtsZ rings in
Streptococcus pneumoniae.";
Nature 516:259-262(2014).
[4]
FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-67 AND THR-78,
DISRUPTION PHENOTYPE, AND MUTAGENESIS OF THR-67 AND THR-78.
STRAIN=ATCC BAA-255 / R6, D39, and Rx1;
PubMed=25550321; DOI=10.1128/mBio.01700-14;
Holeckova N., Doubravova L., Massidda O., Molle V., Buriankova K.,
Benada O., Kofronova O., Ulrych A., Branny P.;
"LocZ is a new cell division protein involved in proper septum
placement in Streptococcus pneumoniae.";
MBio 6:E01700-E01700(2015).
-!- FUNCTION: Early cell division protein that marks the future cell
division site and supports proper FtsZ ring positioning.
{ECO:0000255|HAMAP-Rule:MF_01941, ECO:0000269|PubMed:25470041,
ECO:0000269|PubMed:25550321}.
-!- SUBUNIT: Interacts with FtsZ. {ECO:0000255|HAMAP-Rule:MF_01941,
ECO:0000269|PubMed:25470041}.
-!- INTERACTION:
Q8DNV9:ftsZ; NbExp=2; IntAct=EBI-16131327, EBI-16131344;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-
Rule:MF_01941, ECO:0000269|PubMed:25470041}; Single-pass membrane
protein {ECO:0000255, ECO:0000255|HAMAP-Rule:MF_01941}. Note=In
newborn cells, forms a ring positioned at mid-cell. Soon after
cell division starts and the cells begin elongating, the ring
splits into two rings that, as elongation proceeds, move along and
mark the future division sites (PubMed:25470041, PubMed:25550321).
Targeting to mid-cell does not depend on StkP and/or
phosphorylation state (PubMed:25550321).
{ECO:0000269|PubMed:25470041, ECO:0000269|PubMed:25550321}.
-!- DOMAIN: The N-terminal domain is required for interaction with
FtsZ. The C-terminal domain efficiently binds peptidoglycan and is
required for septal localization. Both domains are required for
MapZ cellular function. {ECO:0000269|PubMed:25470041}.
-!- PTM: Phosphorylated on Thr residues by StkP (PubMed:20453092,
PubMed:25470041, PubMed:25550321). Both phosphorylated and non-
phosphorylated forms of MapZ are required for proper Z-ring
formation and dynamics (PubMed:25470041). Phosphorylation probably
occurs during the predivisional stage (PubMed:25550321).
{ECO:0000269|PubMed:20453092, ECO:0000269|PubMed:25470041,
ECO:0000269|PubMed:25550321}.
-!- DISRUPTION PHENOTYPE: Deletion mutant exhibits a variety of
aberrant cell shapes and sizes, is more sensitive to heat stress
and shows lower survival after exposure to oxidative stress
(PubMed:25470041, PubMed:25550321). Mutants show severe cell
division defects, with cells dividing asymmetrically, generating
daughter cells of unequal size (PubMed:25550321). Cells have
mispositioned division septa and form grape-like clusters
(PubMed:25470041). They exhibit severe alterations of FtsZ ring
morphology and localization (PubMed:25470041, PubMed:25550321).
FtsA and other cell division proteins are also mislocalized
(PubMed:25550321). {ECO:0000269|PubMed:25470041,
ECO:0000269|PubMed:25550321}.
-!- SIMILARITY: Belongs to the MapZ family. {ECO:0000255|HAMAP-
Rule:MF_01941, ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AE007317; AAK99138.1; -; Genomic_DNA.
PIR; F97913; F97913.
RefSeq; NP_357928.1; NC_003098.1.
RefSeq; WP_000039255.1; NC_003098.1.
PDB; 2ND9; NMR; -; A=182-313.
PDB; 2NDA; NMR; -; A=355-464.
PDBsum; 2ND9; -.
PDBsum; 2NDA; -.
SMR; Q8DR55; -.
DIP; DIP-61348N; -.
IntAct; Q8DR55; 2.
STRING; 171101.spr0334; -.
iPTMnet; Q8DR55; -.
EnsemblBacteria; AAK99138; AAK99138; spr0334.
GeneID; 934807; -.
KEGG; spr:spr0334; -.
PATRIC; fig|171101.6.peg.373; -.
eggNOG; ENOG41070VT; Bacteria.
eggNOG; ENOG410YUH9; LUCA.
HOGENOM; HOG000235207; -.
KO; K20073; -.
OMA; NPAWAFN; -.
Proteomes; UP000000586; Chromosome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
HAMAP; MF_01941; MapZ; 1.
InterPro; IPR030858; MapZ.
1: Evidence at protein level;
3D-structure; Cell cycle; Cell division; Cell membrane;
Complete proteome; Membrane; Phosphoprotein; Reference proteome;
Transmembrane; Transmembrane helix.
CHAIN 1 464 Mid-cell-anchored protein Z.
/FTId=PRO_0000418152.
TOPO_DOM 1 158 Cytoplasmic.
{ECO:0000269|PubMed:25470041}.
TRANSMEM 159 179 Helical. {ECO:0000255|HAMAP-
Rule:MF_01941}.
TOPO_DOM 180 464 Extracellular.
{ECO:0000269|PubMed:25470041}.
COMPBIAS 311 365 Ser-rich. {ECO:0000255}.
MOD_RES 67 67 Phosphothreonine.
{ECO:0000269|PubMed:25470041,
ECO:0000269|PubMed:25550321}.
MOD_RES 78 78 Phosphothreonine.
{ECO:0000269|PubMed:25470041,
ECO:0000269|PubMed:25550321}.
MUTAGEN 67 67 T->A: Partial inhibition of
phosphorylation. Almost loss of
phosphorylation; when associated with A-
78. {ECO:0000269|PubMed:25550321}.
MUTAGEN 78 78 T->A: Partial inhibition of
phosphorylation. Almost loss of
phosphorylation; when associated with A-
67. {ECO:0000269|PubMed:25550321}.
STRAND 193 195 {ECO:0000244|PDB:2ND9}.
HELIX 200 213 {ECO:0000244|PDB:2ND9}.
STRAND 214 216 {ECO:0000244|PDB:2ND9}.
HELIX 225 229 {ECO:0000244|PDB:2ND9}.
HELIX 230 240 {ECO:0000244|PDB:2ND9}.
HELIX 245 267 {ECO:0000244|PDB:2ND9}.
STRAND 270 272 {ECO:0000244|PDB:2ND9}.
STRAND 277 279 {ECO:0000244|PDB:2ND9}.
HELIX 300 310 {ECO:0000244|PDB:2ND9}.
HELIX 381 384 {ECO:0000244|PDB:2NDA}.
TURN 385 388 {ECO:0000244|PDB:2NDA}.
HELIX 390 392 {ECO:0000244|PDB:2NDA}.
HELIX 398 409 {ECO:0000244|PDB:2NDA}.
STRAND 418 423 {ECO:0000244|PDB:2NDA}.
STRAND 430 434 {ECO:0000244|PDB:2NDA}.
STRAND 440 445 {ECO:0000244|PDB:2NDA}.
TURN 446 448 {ECO:0000244|PDB:2NDA}.
SEQUENCE 464 AA; 51542 MW; 859BF979D81E3FDE CRC64;
MSKKRRNRHK KEAQEPQFDF DEAKELTVGQ AIRKNEEVEA GVLPEDSILD KYVKQHRDEI
EADKFATRQY KKEEFVETQS LDDLIQEMRE AVEKSEASSE EVPSSEDILL PLPLDDEEQG
LDPLLLDDEN PTEMTEEVEE EQNLSRLDQE DSEKKSKKGF ILTVLALVSV IICVSAYYVY
RQVARSTKEI ETSQSTTANQ SDVDDFNTLY DAFYTNSNKT ALKNSQFDKL SQLKTLLDKL
EGSREHTLAK SKYDSLATQI KAIQDVNAQF EKPAIVDGVL DTNAKAKSDA KFTDIKTGNT
ELDKVLDKAI SLGKSQQTST SSSSSSQTSS SSSSQASSNT TSEPKPSSSN ETRSSRSEVN
MGLSSAGVAV QRSASRVAYN QSAIDDSNNS AWDFADGVLE QILATSRSRG YITGDQYILE
RVNIVNGNGY YNLYKPDGTY LFTLNCKTGY FVGNGAGHAD DLDY


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