ID   EZRA_ENTFA              Reviewed;         578 AA.
AC   Q838R5;
DT   21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Septation ring formation regulator EzrA {ECO:0000255|HAMAP-Rule:MF_00728};
GN   Name=ezrA {ECO:0000255|HAMAP-Rule:MF_00728}; OrderedLocusNames=EF_0370;
OS   Enterococcus faecalis (strain ATCC 700802 / V583).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=226185;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700802 / V583;
RX   PubMed=12663927; DOI=10.1126/science.1080613;
RA   Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
RA   Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA   Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C.,
RA   DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., Nelson W.C.,
RA   Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M.,
RA   Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT   "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT   faecalis.";
RL   Science 299:2071-2074(2003).
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; AE016830; AAO80232.1; -; Genomic_DNA.
DR   RefSeq; NP_814161.1; NC_004668.1.
DR   RefSeq; WP_002355233.1; NZ_KE136524.1.
DR   AlphaFoldDB; Q838R5; -.
DR   SMR; Q838R5; -.
DR   STRING; 226185.EF_0370; -.
DR   EnsemblBacteria; AAO80232; AAO80232; EF_0370.
DR   GeneID; 60892822; -.
DR   KEGG; efa:EF0370; -.
DR   PATRIC; fig|226185.45.peg.2959; -.
DR   eggNOG; COG4477; Bacteria.
DR   HOGENOM; CLU_034079_2_0_9; -.
DR   OMA; FRSQNHI; -.
DR   Proteomes; UP000001415; 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..578
FT                   /note="Septation ring formation regulator EzrA"
FT                   /id="PRO_0000172871"
FT   TOPO_DOM        1..8
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
FT   TRANSMEM        9..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
FT   TOPO_DOM        28..578
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
FT   COILED          103..165
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
FT   COILED          256..285
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
FT   COILED          394..490
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
SQ   SEQUENCE   578 AA;  68153 MW;  6E35951442889F76 CRC64;
     MKNNWIIILV LVIVIIAAVL YLIGYFMRKK NQEQLDELEV RKEALFDLPV FEEIDDIKKM
     HLVGQSQNSF REWNQRWVEL STRSFAELES QIYEVENQNE IFRFMKAKKA VVEANETMTE
     MEAEVEVIRN GLKELRESEE RNSLEVQKAL DVYEELSKSL KDDKASFGPA YSEIQKQLRN
     VEIEFTQFVT LNTSGDPIEA REVLEDAERH TYELEDLMKR IPPMYEELNE TFPDQLKEIE
     EGYNQLLADD YVFPEQNFAE EIQHAKKRVE NSMADLEKTE IAAVEVANRD TATAIDALYE
     VMEREIEAKK YVVTNQKIID DYISHSLKNN RQLMIELDHV SQSYTLNNNE LGRSRGFQTE
     IEEIIRRQKD LEPRMKEHTV PYSEIQAFYK ECYKILDDIE NQQLEIDASL KELRKGEKVA
     QEKVDEYEFR LRSIKRYVEK QRLPGLSADY LEFFYVATDR IEDLSRALNK MRINMDEINR
     LCDLCEDDLE LLDKKTKDLV NAAALTEQMM QYANRYRHTH ENIRAALDKS MYLFSTEFRY
     QDALDEIGTA LEAVEPGAFK RIEDFYFKNI NNPNLTAI