ID   EZRA_BACCN              Reviewed;         569 AA.
AC   A7GTT0;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Septation ring formation regulator EzrA {ECO:0000255|HAMAP-Rule:MF_00728};
GN   Name=ezrA {ECO:0000255|HAMAP-Rule:MF_00728}; OrderedLocusNames=Bcer98_3321;
OS   Bacillus cytotoxicus (strain DSM 22905 / CIP 110041 / 391-98 / NVH 391-98).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=315749;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22905 / CIP 110041 / 391-98 / NVH 391-98;
RX   PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003;
RA   Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C.,
RA   Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V.,
RA   Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "Extending the Bacillus cereus group genomics to putative food-borne
RT   pathogens of different toxicity.";
RL   Chem. Biol. Interact. 171:236-249(2008).
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; CP000764; ABS23538.1; -; Genomic_DNA.
DR   RefSeq; WP_012095779.1; NC_009674.1.
DR   AlphaFoldDB; A7GTT0; -.
DR   SMR; A7GTT0; -.
DR   STRING; 315749.Bcer98_3321; -.
DR   EnsemblBacteria; ABS23538; ABS23538; Bcer98_3321.
DR   GeneID; 56418864; -.
DR   KEGG; bcy:Bcer98_3321; -.
DR   eggNOG; COG4477; Bacteria.
DR   HOGENOM; CLU_034079_1_0_9; -.
DR   OMA; FRSQNHI; -.
DR   OrthoDB; 670472at2; -.
DR   Proteomes; UP000002300; 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..569
FT                   /note="Septation ring formation regulator EzrA"
FT                   /id="PRO_1000083318"
FT   TOPO_DOM        1..6
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
FT   TRANSMEM        7..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
FT   TOPO_DOM        26..569
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
FT   COILED          103..149
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
FT   COILED          273..336
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
FT   COILED          383..440
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
SQ   SEQUENCE   569 AA;  66413 MW;  C0B8A4E8AF3D0FB0 CRC64;
     MDSILTIVII VVSSILVLLM IELMIRNRSY KDIEALEQWQ QEIKDKPVAD ELKRVKDLNM
     TGQTEELFGK WREDWDEIVA TILPKAEKDL EGARKYASQF SFRKAKYAMN EAISNLDEAD
     NRITDILNEL QQLLESHEKN SAEIDGLRDV YRNMKKSVLA HRHMYGAAEQ KIEELLDVES
     DKFQKFEEAT ANGDYLKARD IVMSLEEGLS NLEGMIQEVP DLLVECQATL PVQLEDLLQG
     HDEMKKQGYV LNHLEIPKEV RDMTKQLQTC LIDIQELHIT EAAEKIEALK TRLDTLYDQL
     EKEVHAKYYV EQKTIRVYDD LEEIHEQALE TKAETQFVKQ SYQLQDKDIE SQKIIEKQMH
     ILMKRFEVLQ LRVAEQDIAF SVIREELEEI YEQCETLKVL HAEYKEMLQA MRKEEFEARE
     KLQEMRNMIL ETKRLMQKSN LPGLPESIME ELQKGQEAMQ AVYGHLELKP LNMHVVNSEL
     EEAYAIVNDV SERTQDVIGQ AYLVEKLIQY GNRYRSQDMD LAYSLDNAER LFREYEYDAA
     LEQAASVLEQ LEPGVVQKIA EFVDNEQTS