ID   EZRA_LACLS              Reviewed;         576 AA.
AC   Q02VY0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=Septation ring formation regulator EzrA {ECO:0000255|HAMAP-Rule:MF_00728};
GN   Name=ezrA {ECO:0000255|HAMAP-Rule:MF_00728}; OrderedLocusNames=LACR_2453;
OS   Lactococcus lactis subsp. cremoris (strain SK11).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus; Lactococcus cremoris subsp. cremoris.
OX   NCBI_TaxID=272622;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK11;
RX   PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA   Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V.,
RA   Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA   Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA   Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA   Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA   Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA   Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R.,
RA   O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T.,
RA   Richardson P., Kozyavkin S., Weimer B.C., Mills D.A.;
RT   "Comparative genomics of the lactic acid bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(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}.
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DR   EMBL; CP000425; ABJ73892.1; -; Genomic_DNA.
DR   RefSeq; WP_011677205.1; NC_008527.1.
DR   AlphaFoldDB; Q02VY0; -.
DR   SMR; Q02VY0; -.
DR   EnsemblBacteria; ABJ73892; ABJ73892; LACR_2453.
DR   KEGG; llc:LACR_2453; -.
DR   HOGENOM; CLU_034079_2_0_9; -.
DR   OMA; FRSQNHI; -.
DR   Proteomes; UP000000240; 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..576
FT                   /note="Septation ring formation regulator EzrA"
FT                   /id="PRO_1000045899"
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..576
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
FT   COILED          105..134
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
FT   COILED          254..305
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
SQ   SEQUENCE   576 AA;  66321 MW;  075C5A4CDE2A2FA7 CRC64;
     MSSTVIILIV VLLVILVAFY AFAILMRKKT EDRILALEER KESLFDLPVQ EEIDSVKKMH
     LVGQSQTIFR EWNQKWLDLS SNSFADLEEH IFEAEQLNDS FHFFRARESV ADSEAQIEMM
     EGDVEGIRQG VAQLVEQEKR NSNKIQESLD LYDNLRSDIA DNADLYGTVI TELEKHLANI
     ETEFSQFVTL NSTGDPIEAA EVLETAEEHT IALRAITEQI PSFIKTIEKD VPKRLEELQE
     ASDKFIAEDY ILPENVNLKE RMDDLQHHLE ESSSLLEQFE LDRVEAELDL IQERVEELYS
     IFEREYSARR NVEKRSSVLK EYIEHIRVNN KNLLLEIDHV TQAYILSGNE KGYVRGYQEH
     LESLDADVDE IIANIEAKAI PYSSLSRRVN SVVNSLEDIE KNQIKISETL SGLRDEERAA
     QEIAERFDSE LRTIKRYVEK CNLPGLPKDY LDLFFMTGDR VQNLFKELGR VRINIDTINH
     LVDVSTEDMH VLKEATTNLT DHAVLAEQLI QYANRYKASN EQVAQGISRA LQLFENSRDY
     DGSFDEISKT LEIVEPGAAS RISGVYFKNK PTPDYL