ID   EZRA_STRS7              Reviewed;         574 AA.
AC   C0MH92;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   25-MAY-2022, entry version 60.
DE   RecName: Full=Septation ring formation regulator EzrA {ECO:0000255|HAMAP-Rule:MF_00728};
GN   Name=ezrA {ECO:0000255|HAMAP-Rule:MF_00728}; OrderedLocusNames=SZO_11860;
OS   Streptococcus equi subsp. zooepidemicus (strain H70).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=553483;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H70;
RX   PubMed=19325880; DOI=10.1371/journal.ppat.1000346;
RA   Holden M.T.G., Heather Z., Paillot R., Steward K.F., Webb K., Ainslie F.,
RA   Jourdan T., Bason N.C., Holroyd N.E., Mungall K., Quail M.A., Sanders M.,
RA   Simmonds M., Willey D., Brooks K., Aanensen D.M., Spratt B.G., Jolley K.A.,
RA   Maiden M.C.J., Kehoe M., Chanter N., Bentley S.D., Robinson C.,
RA   Maskell D.J., Parkhill J., Waller A.S.;
RT   "Genomic evidence for the evolution of Streptococcus equi: host
RT   restriction, increased virulence, and genetic exchange with human
RT   pathogens.";
RL   PLoS Pathog. 5:E1000346-E1000346(2009).
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}.
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DR   EMBL; FM204884; CAW99643.1; -; Genomic_DNA.
DR   AlphaFoldDB; C0MH92; -.
DR   SMR; C0MH92; -.
DR   EnsemblBacteria; CAW99643; CAW99643; SZO_11860.
DR   KEGG; seq:SZO_11860; -.
DR   eggNOG; COG4477; Bacteria.
DR   HOGENOM; CLU_034079_2_0_9; -.
DR   OMA; FRSQNHI; -.
DR   Proteomes; UP000001368; 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_1000212731"
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..131
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
FT   COILED          161..190
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
FT   COILED          276..379
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
FT   COILED          459..493
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
SQ   SEQUENCE   574 AA;  66075 MW;  BB83CBFF54DF76CF CRC64;
     MSSGIILLIV AIVLLVIIAY LVGVIIRKRN DTLITSLEER KQALFGLPVN DEIEEVKSLH
     LIGQSQTSFR EWNQKWVDLT LNTFTDIEKH IFEAEHLNDT FNFIRAKHEI NSVESQLNLV
     EEDITAIREA LGILKEQEEK NSARVTHALD LYEKLQASVA ENEDNFGSTM AEIEKQMKNI
     EAEFSQFVAL NSSGDPVEAA EVLDKAEEHT IALGQITEQI PAIVAKLEDD FPDQLDDLET
     GYRRLLEENY HFPEKNIEAR FQEIRESIRA NSSELVTLDL DRARDENTHI QERIDSLYEL
     FEREIAAYKV VAKNSKILPR YLAHAKHNNE QLKHEIARLS RKYILSENEG LNIKAFDKDL
     KDIEDNVLEI AEAFDQQEKP FSELQLILDR SIKTLASVES GQMDVFAAVK DIEKIESQAR
     QHLEIYVTQL HMIKRYMEKR NLPGIPQDFL STFFTTSSQL EALMDELSRG RINIEAVSRL
     SEVATAAIAN LEELTYQVVQ HATLTEQLLQ YSNRYRSFEA GVQNSFEHAL KLFEVDNDYQ
     ASFDEISYAL ETVEPGVTER FVNSYEKTRE RIRF