ID   EZRA_STRGC              Reviewed;         574 AA.
AC   A8AY51;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Septation ring formation regulator EzrA {ECO:0000255|HAMAP-Rule:MF_00728};
GN   Name=ezrA {ECO:0000255|HAMAP-Rule:MF_00728}; OrderedLocusNames=SGO_1431;
OS   Streptococcus gordonii (strain Challis / ATCC 35105 / BCRC 15272 / CH1 /
OS   DL1 / V288).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=467705;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Challis / ATCC 35105 / BCRC 15272 / CH1 / DL1 / V288;
RX   PubMed=17720781; DOI=10.1128/jb.01023-07;
RA   Vickerman M.M., Iobst S., Jesionowski A.M., Gill S.R.;
RT   "Genome-wide transcriptional changes in Streptococcus gordonii in response
RT   to competence signaling peptide.";
RL   J. Bacteriol. 189:7799-7807(2007).
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; CP000725; ABV09556.1; -; Genomic_DNA.
DR   RefSeq; WP_012130512.1; NC_009785.1.
DR   AlphaFoldDB; A8AY51; -.
DR   SMR; A8AY51; -.
DR   STRING; 467705.SGO_1431; -.
DR   EnsemblBacteria; ABV09556; ABV09556; SGO_1431.
DR   KEGG; sgo:SGO_1431; -.
DR   eggNOG; COG4477; Bacteria.
DR   HOGENOM; CLU_034079_2_0_9; -.
DR   OMA; FRSQNHI; -.
DR   Proteomes; UP000001131; 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_1000083322"
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          267..424
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
FT   COILED          456..524
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
SQ   SEQUENCE   574 AA;  66274 MW;  8982AD8FF7A3842A CRC64;
     MSNGLIILII VIAVALILAY VAAVVLRKRN ETLLDSLEER KEKLYNLPVN DEVEAIKNMH
     LIGQSQVTFR EWNQKWVDLS LNSFADIENN IFEAEGYNNS FRFLKAKHAI DSIESQINLV
     EEDIELIREA LADLEKQEAK NSGRVLHALE LFENLQVKVA EDTEKYGPAV QEIQKQLQNI
     ESEFSQFVTL NSSGDPVEAA DILDKTENHI LALTHIVDKV PSIVTELREV LPDQLEDLES
     GYRKLVEAGY HFVETDIESR FSQLHSNITQ NYENIAALEL DNAQYENTQI QEEINALYDI
     FTREIAAQKV VEKLQENLPA YLKHTKENNQ HLQSELDRLS KMYLLSDEED EKVRDLQSEL
     SALEAVVLAT VEDSAENKQA YSLTQEALEA TQERLKEIED EQITLGERLE RIEKDDDNAR
     QKVNIYINKL HTIKRYMEKR NLPGIPKSFL SLFFTASDHT EALLTELEQL RVNIDNVNLL
     LENVTNDIHD LETETYQIVQ YATLTEQLLQ YSNRYRSFDQ SIQEAFNKAL DIFENQFDYE
     SSFEVISQAL EVVEPGVTSR FVTSYEKTRE NIRF