ID   EZRA_STRA5              Reviewed;         574 AA.
AC   Q8E0U6;
DT   21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=Septation ring formation regulator EzrA {ECO:0000255|HAMAP-Rule:MF_00728};
GN   Name=ezrA {ECO:0000255|HAMAP-Rule:MF_00728}; OrderedLocusNames=SAG0624;
OS   Streptococcus agalactiae serotype V (strain ATCC BAA-611 / 2603 V/R).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=208435;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-611 / 2603 V/R;
RX   PubMed=12200547; DOI=10.1073/pnas.182380799;
RA   Tettelin H., Masignani V., Cieslewicz M.J., Eisen J.A., Peterson S.N.,
RA   Wessels M.R., Paulsen I.T., Nelson K.E., Margarit I., Read T.D.,
RA   Madoff L.C., Wolf A.M., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA   DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Lewis M.R., Radune D.,
RA   Fedorova N.B., Scanlan D., Khouri H.M., Mulligan S., Carty H.A.,
RA   Cline R.T., Van Aken S.E., Gill J., Scarselli M., Mora M., Iacobini E.T.,
RA   Brettoni C., Galli G., Mariani M., Vegni F., Maione D., Rinaudo D.,
RA   Rappuoli R., Telford J.L., Kasper D.L., Grandi G., Fraser C.M.;
RT   "Complete genome sequence and comparative genomic analysis of an emerging
RT   human pathogen, serotype V Streptococcus agalactiae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:12391-12396(2002).
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; Single-pass membrane protein.
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; AE009948; AAM99520.1; -; Genomic_DNA.
DR   RefSeq; NP_687648.1; NC_004116.1.
DR   RefSeq; WP_000094341.1; NC_004116.1.
DR   AlphaFoldDB; Q8E0U6; -.
DR   SMR; Q8E0U6; -.
DR   STRING; 208435.SAG0624; -.
DR   EnsemblBacteria; AAM99520; AAM99520; SAG0624.
DR   GeneID; 66885537; -.
DR   KEGG; sag:SAG0624; -.
DR   PATRIC; fig|208435.3.peg.624; -.
DR   HOGENOM; CLU_034079_2_0_9; -.
DR   OMA; FRSQNHI; -.
DR   Proteomes; UP000000821; 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;
KW   Reference proteome; Septation; Transmembrane; Transmembrane helix.
FT   CHAIN           1..574
FT                   /note="Septation ring formation regulator EzrA"
FT                   /id="PRO_0000172887"
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          104..141
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
FT   COILED          275..343
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
FT   COILED          473..525
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
SQ   SEQUENCE   574 AA;  66495 MW;  96319A3D461CF467 CRC64;
     MSSGIILLLV AIVLLVIIAY VVGVVIRKRN DTLIANLETR KQELVDLPVQ EEIEQVKLLH
     LIGQSQSTFR EWNQKWTDLS TNSFKDIDFH LVEAENLNDS FNFVRAKHEI DNVDSQLTII
     EEDIVSIREA LEVLKEQEEK NSARVTHALD LYETLQKSIS EKEDNYGTTM PEIEKQLKNI
     EAEFSHFVTL NSTGDPIEAS EVLNKAEEHT IALGQITEQI PAIVAKLEDD FPDQLDDLET
     GYRRLLEENY HFPEKDIEQR FQEVREAIRS NSDGLVSLDL DRARDENEHI QEKIDKLYDI
     FEREIAAYKV AHKDSKIIPQ FLAHAKSNNE QLGHEIKRLS AKYILNENES LSLRSFTNDL
     EEIETKVLPS VENFGQEASP YTHLQILFER TLKTLTTVEE NQMEVFEAVK TIESVETRAR
     QNMDKYVNKL HMIKRFMEKR NLPGIPQDFL STFFTTSSQI EALINELSRG RIDIEAVSRL
     NDVTTNAIAN LEQATYLVVQ DATLTEQLLQ YSNRYRSFEQ NVQKSFEQAL YLFEVEHNYK
     ASFDEISYAL ETVEPGVTDR FVTSYEKTQE RIRF