ID   EZRA_BACCQ              Reviewed;         570 AA.
AC   B9J153;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 54.
DE   RecName: Full=Septation ring formation regulator EzrA {ECO:0000255|HAMAP-Rule:MF_00728};
GN   Name=ezrA {ECO:0000255|HAMAP-Rule:MF_00728}; OrderedLocusNames=BCQ_4465;
OS   Bacillus cereus (strain Q1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=361100;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Q1;
RX   PubMed=19060151; DOI=10.1128/jb.01629-08;
RA   Xiong Z., Jiang Y., Qi D., Lu H., Yang F., Yang J., Chen L., Sun L., Xu X.,
RA   Xue Y., Zhu Y., Jin Q.;
RT   "Complete genome sequence of the extremophilic Bacillus cereus strain Q1
RT   with industrial applications.";
RL   J. Bacteriol. 191:1120-1121(2009).
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; CP000227; ACM14891.1; -; Genomic_DNA.
DR   RefSeq; WP_000377296.1; NC_011969.1.
DR   AlphaFoldDB; B9J153; -.
DR   SMR; B9J153; -.
DR   EnsemblBacteria; ACM14891; ACM14891; BCQ_4465.
DR   KEGG; bcq:BCQ_4465; -.
DR   HOGENOM; CLU_034079_1_0_9; -.
DR   OMA; FRSQNHI; -.
DR   Proteomes; UP000000441; 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_1000148069"
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;  66525 MW;  B63D1301543DF563 CRC64;
     MDSILTIVII VVSSILVLLM IELVIRNRSY KDIEALEQWK QEIKDKPVAD ELKRVKDLNM
     TGQTEELFGK WREEWDEIVS TTIPKAEKDL AQARKFASQF SFRKAKHAMN ESISGLDDAD
     NRITDILNEL QQLLESHEKN SSEIEGLRDT YRSMKKSVLA HRHMYGAAEQ KIEEMLDAES
     EKFKTFEEAT NNGDYLKARE IVISLEEGLA DLEIIIHQIP DLLVECQATL PVQLEDLLHG
     HNDMVRQGYV LEYLEIPKEV RDMKKQLQIC LMDIQELHIT EAAEKVENLK TSLDSFYDQL
     EQEVHARHYV EQKTLSVYED LEEIRIETIE TKAETQLVKQ SYQLQDKDIE SQKVIEKQMH
     ILMKRFEMLQ LRVAEQDIAF SIIREELEEI YEQCETLKVL HAEYKEMLQT MRKEEFEARE
     KLQEMRNTIF ETKRFMQKSN LPGLPESIME DLKRGQMAMQ AVYEQLEVKP LNMNAVNSSL
     EEAYTTVNGV AEMTEELIGQ AYLVEKLIQY GNRYRSHDEN LADSLNYAEK LFREYQYDAA
     LEQAASVLEQ LEPGVVQKIA EYVDNEQTLS