ID   EZRA_BACC1              Reviewed;         570 AA.
AC   Q72Z83;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Septation ring formation regulator EzrA {ECO:0000255|HAMAP-Rule:MF_00728};
GN   Name=ezrA {ECO:0000255|HAMAP-Rule:MF_00728}; OrderedLocusNames=BCE_4786;
OS   Bacillus cereus (strain ATCC 10987 / NRS 248).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=222523;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10987 / NRS 248;
RX   PubMed=14960714; DOI=10.1093/nar/gkh258;
RA   Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L.,
RA   Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F.,
RA   Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.;
RT   "The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic
RT   adaptations and a large plasmid related to Bacillus anthracis pXO1.";
RL   Nucleic Acids Res. 32:977-988(2004).
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; AE017194; AAS43687.1; -; Genomic_DNA.
DR   RefSeq; WP_000377292.1; NC_003909.8.
DR   AlphaFoldDB; Q72Z83; -.
DR   SMR; Q72Z83; -.
DR   EnsemblBacteria; AAS43687; AAS43687; BCE_4786.
DR   GeneID; 59154764; -.
DR   KEGG; bca:BCE_4786; -.
DR   HOGENOM; CLU_034079_1_0_9; -.
DR   OMA; FRSQNHI; -.
DR   Proteomes; UP000002527; 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..570
FT                   /note="Septation ring formation regulator EzrA"
FT                   /id="PRO_1000045892"
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..570
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
FT   COILED          115..149
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
FT   COILED          275..303
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
FT   COILED          355..429
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
SQ   SEQUENCE   570 AA;  66513 MW;  627A99BF771C72D0 CRC64;
     MDSILTIVII VVSSILVLLM IELVIRNRSY KDIEALEQWK QEIKDKPVAD ELKRVKDLNM
     TGQTEELFGK WREEWDEIVS TTIPKADKDL AQARKFASQF SFRKAKHAMN ESISGLDDAD
     NRITDILNEL QQLLESHEKN SSEIEGLRDT YRSMKKSVLA HRHMYGAAEQ KIEEMLDAES
     EKFKTFEEAT NNGDYLKARE IVISLEEGLA DLEIIIHQIP DLLVECQATL PVQLEDLLHG
     HNDMVRQGYV LEYLEIPKEV RDMKKQLQIC LMDIQELHIT EAAEKVENLK TSLDSFYDQL
     EQEVHARHYV EQKTLSVYED LEEIRTETIE TKAETQLVKQ SYQLQDKDIE SQKVIEKQMH
     ILMKRFEMLQ LRVAEQDIAF SIIREELEEI YEQCETLKVL HAEYKEMLQT MRKEEFEARE
     KLQEMRNTIF ETKRFMQKSN LPGLPESIME DLKRGQMAMQ AVYEQLEVKP LNMNAVNSSL
     EEAYTTVNGV AEMTEELIGQ AYLVEKLIQY GNRYRSHDEN LAESLNYAEK LFREYQYDAA
     LEQAASVLEQ LEPGVVQKIA EYVDNEQTLS