MAPZ_STRR6
ID MAPZ_STRR6 Reviewed; 464 AA.
AC Q8DR55;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=Mid-cell-anchored protein Z {ECO:0000255|HAMAP-Rule:MF_01941, ECO:0000303|PubMed:25470041};
GN Name=mapZ {ECO:0000255|HAMAP-Rule:MF_01941, ECO:0000303|PubMed:25470041};
GN Synonyms=locZ {ECO:0000303|PubMed:25550321};
GN OrderedLocusNames=spr0334 {ECO:0000312|EMBL:AAK99138.1};
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 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 [3]
RP FUNCTION, INTERACTION WITH FTSZ, SUBCELLULAR LOCATION, TOPOLOGY, DOMAIN,
RP PHOSPHORYLATION AT THR-67 AND THR-78, AND DISRUPTION PHENOTYPE.
RC STRAIN=R6 / R800;
RX PubMed=25470041; DOI=10.1038/nature13966;
RA Fleurie A., Lesterlin C., Manuse S., Zhao C., Cluzel C., Lavergne J.P.,
RA Franz-Wachtel M., Macek B., Combet C., Kuru E., VanNieuwenhze M.S.,
RA Brun Y.V., Sherratt D., Grangeasse C.;
RT "MapZ marks the division sites and positions FtsZ rings in Streptococcus
RT pneumoniae.";
RL Nature 516:259-262(2014).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-67 AND THR-78,
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF THR-67 AND THR-78.
RC STRAIN=ATCC BAA-255 / R6, D39, and Rx1;
RX PubMed=25550321; DOI=10.1128/mbio.01700-14;
RA Holeckova N., Doubravova L., Massidda O., Molle V., Buriankova K.,
RA Benada O., Kofronova O., Ulrych A., Branny P.;
RT "LocZ is a new cell division protein involved in proper septum placement in
RT Streptococcus pneumoniae.";
RL MBio 6:E01700-E01700(2015).
CC -!- FUNCTION: Early cell division protein that marks the future cell
CC division site and supports proper FtsZ ring positioning.
CC {ECO:0000255|HAMAP-Rule:MF_01941, ECO:0000269|PubMed:25470041,
CC ECO:0000269|PubMed:25550321}.
CC -!- SUBUNIT: Interacts with FtsZ. {ECO:0000255|HAMAP-Rule:MF_01941,
CC ECO:0000269|PubMed:25470041}.
CC -!- INTERACTION:
CC Q8DR55; Q8DNV9: ftsZ; NbExp=2; IntAct=EBI-16131327, EBI-16131344;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01941,
CC ECO:0000269|PubMed:25470041}; Single-pass membrane protein
CC {ECO:0000255, ECO:0000255|HAMAP-Rule:MF_01941}. Note=In newborn cells,
CC forms a ring positioned at mid-cell. Soon after cell division starts
CC and the cells begin elongating, the ring splits into two rings that, as
CC elongation proceeds, move along and mark the future division sites
CC (PubMed:25470041, PubMed:25550321). Targeting to mid-cell does not
CC depend on StkP and/or phosphorylation state (PubMed:25550321).
CC {ECO:0000269|PubMed:25470041, ECO:0000269|PubMed:25550321}.
CC -!- DOMAIN: The N-terminal domain is required for interaction with FtsZ.
CC The C-terminal domain efficiently binds peptidoglycan and is required
CC for septal localization. Both domains are required for MapZ cellular
CC function. {ECO:0000269|PubMed:25470041}.
CC -!- PTM: Phosphorylated on Thr residues by StkP (PubMed:20453092,
CC PubMed:25470041, PubMed:25550321). Both phosphorylated and non-
CC phosphorylated forms of MapZ are required for proper Z-ring formation
CC and dynamics (PubMed:25470041). Phosphorylation probably occurs during
CC the predivisional stage (PubMed:25550321).
CC {ECO:0000269|PubMed:20453092, ECO:0000269|PubMed:25470041,
CC ECO:0000269|PubMed:25550321}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutant exhibits a variety of aberrant
CC cell shapes and sizes, is more sensitive to heat stress and shows lower
CC survival after exposure to oxidative stress (PubMed:25470041,
CC PubMed:25550321). Mutants show severe cell division defects, with cells
CC dividing asymmetrically, generating daughter cells of unequal size
CC (PubMed:25550321). Cells have mispositioned division septa and form
CC grape-like clusters (PubMed:25470041). They exhibit severe alterations
CC of FtsZ ring morphology and localization (PubMed:25470041,
CC PubMed:25550321). FtsA and other cell division proteins are also
CC mislocalized (PubMed:25550321). {ECO:0000269|PubMed:25470041,
CC ECO:0000269|PubMed:25550321}.
CC -!- SIMILARITY: Belongs to the MapZ family. {ECO:0000255|HAMAP-
CC Rule:MF_01941, ECO:0000305}.
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DR EMBL; AE007317; AAK99138.1; -; Genomic_DNA.
DR PIR; F97913; F97913.
DR RefSeq; NP_357928.1; NC_003098.1.
DR RefSeq; WP_000039255.1; NC_003098.1.
DR PDB; 2ND9; NMR; -; A=182-313.
DR PDB; 2NDA; NMR; -; A=355-464.
DR PDBsum; 2ND9; -.
DR PDBsum; 2NDA; -.
DR AlphaFoldDB; Q8DR55; -.
DR BMRB; Q8DR55; -.
DR SMR; Q8DR55; -.
DR DIP; DIP-61348N; -.
DR IntAct; Q8DR55; 2.
DR STRING; 171101.spr0334; -.
DR iPTMnet; Q8DR55; -.
DR EnsemblBacteria; AAK99138; AAK99138; spr0334.
DR GeneID; 60234341; -.
DR KEGG; spr:spr0334; -.
DR PATRIC; fig|171101.6.peg.373; -.
DR eggNOG; ENOG5032TWV; Bacteria.
DR HOGENOM; CLU_037017_0_0_9; -.
DR OMA; NPAWAFN; -.
DR Proteomes; UP000000586; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01941; MapZ; 1.
DR InterPro; IPR030858; MapZ.
DR InterPro; IPR040532; MapZ_C2.
DR InterPro; IPR041295; MapZ_EC1.
DR Pfam; PF18708; MapZ_C2; 1.
DR Pfam; PF18041; MapZ_EC1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Cell membrane; Membrane;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..464
FT /note="Mid-cell-anchored protein Z"
FT /id="PRO_0000418152"
FT TOPO_DOM 1..158
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:25470041"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01941"
FT TOPO_DOM 180..464
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:25470041"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 91..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 314..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..138
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 67
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:25470041,
FT ECO:0000269|PubMed:25550321"
FT MOD_RES 78
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:25470041,
FT ECO:0000269|PubMed:25550321"
FT MUTAGEN 67
FT /note="T->A: Partial inhibition of phosphorylation. Almost
FT loss of phosphorylation; when associated with A-78."
FT /evidence="ECO:0000269|PubMed:25550321"
FT MUTAGEN 78
FT /note="T->A: Partial inhibition of phosphorylation. Almost
FT loss of phosphorylation; when associated with A-67."
FT /evidence="ECO:0000269|PubMed:25550321"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:2ND9"
FT HELIX 200..213
FT /evidence="ECO:0007829|PDB:2ND9"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:2ND9"
FT HELIX 225..229
FT /evidence="ECO:0007829|PDB:2ND9"
FT HELIX 230..240
FT /evidence="ECO:0007829|PDB:2ND9"
FT HELIX 245..267
FT /evidence="ECO:0007829|PDB:2ND9"
FT STRAND 270..272
FT /evidence="ECO:0007829|PDB:2ND9"
FT STRAND 277..279
FT /evidence="ECO:0007829|PDB:2ND9"
FT HELIX 300..310
FT /evidence="ECO:0007829|PDB:2ND9"
FT HELIX 381..384
FT /evidence="ECO:0007829|PDB:2NDA"
FT TURN 385..388
FT /evidence="ECO:0007829|PDB:2NDA"
FT HELIX 390..392
FT /evidence="ECO:0007829|PDB:2NDA"
FT HELIX 398..409
FT /evidence="ECO:0007829|PDB:2NDA"
FT STRAND 418..423
FT /evidence="ECO:0007829|PDB:2NDA"
FT STRAND 430..434
FT /evidence="ECO:0007829|PDB:2NDA"
FT STRAND 440..445
FT /evidence="ECO:0007829|PDB:2NDA"
FT TURN 446..448
FT /evidence="ECO:0007829|PDB:2NDA"
SQ 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
