ID   EZRA_STRPF              Reviewed;         574 AA.
AC   Q1J7I7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Septation ring formation regulator EzrA {ECO:0000255|HAMAP-Rule:MF_00728};
GN   Name=ezrA {ECO:0000255|HAMAP-Rule:MF_00728};
GN   OrderedLocusNames=MGAS10750_Spy0637;
OS   Streptococcus pyogenes serotype M4 (strain MGAS10750).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=370554;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGAS10750;
RX   PubMed=16636287; DOI=10.1073/pnas.0510279103;
RA   Beres S.B., Richter E.W., Nagiec M.J., Sumby P., Porcella S.F., DeLeo F.R.,
RA   Musser J.M.;
RT   "Molecular genetic anatomy of inter- and intraserotype variation in the
RT   human bacterial pathogen group A Streptococcus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:7059-7064(2006).
CC   -!- FUNCTION: Negative regulator of FtsZ ring formation; modulates the
CC       frequency and position of FtsZ ring formation. Inhibits FtsZ ring
CC       formation at polar sites. Interacts either with FtsZ or with one of its
CC       binding partners to promote depolymerization. {ECO:0000255|HAMAP-
CC       Rule:MF_00728}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00728};
CC       Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00728}.
CC       Note=Colocalized with FtsZ to the nascent septal site.
CC       {ECO:0000255|HAMAP-Rule:MF_00728}.
CC   -!- SIMILARITY: Belongs to the EzrA family. {ECO:0000255|HAMAP-
CC       Rule:MF_00728}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000262; ABF37587.1; -; Genomic_DNA.
DR   RefSeq; WP_011528447.1; NC_008024.1.
DR   AlphaFoldDB; Q1J7I7; -.
DR   SMR; Q1J7I7; -.
DR   EnsemblBacteria; ABF37587; ABF37587; MGAS10750_Spy0637.
DR   KEGG; spi:MGAS10750_Spy0637; -.
DR   HOGENOM; CLU_034079_2_0_9; -.
DR   OMA; FRSQNHI; -.
DR   Proteomes; UP000002434; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005940; C:septin ring; IEA:InterPro.
DR   GO; GO:0000917; P:division septum assembly; IEA:UniProtKB-KW.
DR   GO; GO:0000921; P:septin ring assembly; IEA:InterPro.
DR   HAMAP; MF_00728; EzrA; 1.
DR   InterPro; IPR010379; EzrA.
DR   Pfam; PF06160; EzrA; 1.
PE   3: Inferred from homology;
KW   Cell cycle; Cell division; Cell membrane; Coiled coil; Membrane; Septation;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..574
FT                   /note="Septation ring formation regulator EzrA"
FT                   /id="PRO_1000045910"
FT   TOPO_DOM        1..7
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
FT   TRANSMEM        8..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
FT   TOPO_DOM        27..574
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
FT   COILED          102..141
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
FT   COILED          274..350
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
FT   COILED          459..520
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
SQ   SEQUENCE   574 AA;  66043 MW;  17FF877D9586B821 CRC64;
     MSSGIILLIV AIVLLVIIAY LVGVIIRKRN DSLITSLEER KQALFALPVN DEIEEVKSLH
     LIGQSQTSFR EWNQKWVDLT VNSFADIENH IFEAENLNDT FNFIRAKHEI NSVESQLNLV
     EEDIASIREA LNILKEQEEK NSARVTHALD LYEKLQASIS ENEDNFGSTM PEIDKQMKNI
     ETEFSQFVAL NSSGDPVEAS EVLDRAEEHT IALGQITEQI PAIVAKLEDD FPDQLDDLET
     GYRRLLEENY HFPEKNIEAR FQEIRESIRA NSSELVTLDL DRAREENTHI QERIDSLYEV
     FEREIAAYKV AAKNSKMLPR YLAHVKHNNE QLKDEIARLS RKYILSETES LTVKAFEKDI
     KEIEDSTLAV AEQFGLQEKP FSELQVTFER SIKTLTNVES GQMDVFAAVK DIEKIESQAR
     HNLDVYVTQL HMIKRYMEKR HLPGIPQDFL SAFFTTSSQL EALMDELSRG RINIEAVSRL
     SEVATVAIAN LEDLTYQVVQ NATLTEQLLQ YSNRYRSFEA GVQSSFEHAL RLFEVENDYQ
     ASFDEISYAL ETVEPGVTDR FVNSYEKTRE HIRF