ID   EZRA_BACLD              Reviewed;         564 AA.
AC   Q65G47; Q62RK1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Septation ring formation regulator EzrA {ECO:0000255|HAMAP-Rule:MF_00728};
GN   Name=ezrA {ECO:0000255|HAMAP-Rule:MF_00728};
GN   OrderedLocusNames=BLi03105, BL00433;
OS   Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 /
OS   NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=279010;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC   / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
RX   PubMed=15383718; DOI=10.1159/000079829;
RA   Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P.,
RA   Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.;
RT   "The complete genome sequence of Bacillus licheniformis DSM13, an organism
RT   with great industrial potential.";
RL   J. Mol. Microbiol. Biotechnol. 7:204-211(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC   / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
RX   PubMed=15461803; DOI=10.1186/gb-2004-5-10-r77;
RA   Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J.,
RA   Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B.,
RA   Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A.,
RA   Bolotin A., Lapidus A., Galleron N., Ehrlich S.D., Berka R.M.;
RT   "Complete genome sequence of the industrial bacterium Bacillus
RT   licheniformis and comparisons with closely related Bacillus species.";
RL   Genome Biol. 5:R77.1-R77.12(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; CP000002; AAU24609.1; -; Genomic_DNA.
DR   EMBL; AE017333; AAU41967.1; -; Genomic_DNA.
DR   RefSeq; WP_003184408.1; NC_006322.1.
DR   AlphaFoldDB; Q65G47; -.
DR   SMR; Q65G47; -.
DR   STRING; 279010.BL00433; -.
DR   EnsemblBacteria; AAU24609; AAU24609; BL00433.
DR   GeneID; 66214918; -.
DR   KEGG; bld:BLi03105; -.
DR   KEGG; bli:BL00433; -.
DR   eggNOG; COG4477; Bacteria.
DR   HOGENOM; CLU_034079_1_0_9; -.
DR   OMA; FRSQNHI; -.
DR   OrthoDB; 670472at2; -.
DR   BioCyc; BLIC279010:BLI_RS15360-MON; -.
DR   Proteomes; UP000000606; 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..564
FT                   /note="Septation ring formation regulator EzrA"
FT                   /id="PRO_1000045895"
FT   TOPO_DOM        1..2
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
FT   TRANSMEM        3..21
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
FT   TOPO_DOM        22..564
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
FT   COILED          99..159
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
FT   COILED          243..281
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
FT   COILED          310..498
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
SQ   SEQUENCE   564 AA;  65816 MW;  042486B969CBED6F CRC64;
     MEFVIGLLAL FLILFATGYL FRKNIYKEID RLEAWKIEIM NRSIVEEMSK IKHLKMTGQT
     EEFFERWRRE WDEIVTSHMP KVEELLFEAE DCADKYRFQK SKQVLAHIEN LLSAAESNIE
     DILKEIADLV SSEEQNRKEI EEVKERYTKV RKNLLAYSHL YGDLYAKIEA DLDTVWEGIK
     QFEEETEGGN YIEARKVLLA QDRLLEELQS YIDDVPKLLA SCKQTVPQEI AKLKAGYQEM
     IDKGYKLDHI QVEKELENLL KELKRAEDAL LDELDLEEAA AIVQIIDETI QTLYNQLEHE
     VEAGQEILGK VPELAAALEK LEASKKDTEA ETELVKKGYR LTTGELEKQQ SYEKRLEMIE
     KQFEQVRERL DQKHVAYSLL KEELADIEKQ MEAAQREHDE YRDMLQMLRK EELQARELLK
     QLKQTIKDTA RSLEKSNVPG IPEAITEKIR QSQTTVQKVT EQLNELPLNM DAVNERLQEA
     EQLVTEVKTK TDELVELVLL IERIIQYGNR FRSQDRILSE QLKEAENCFY AYQYEEAYDI
     AARAVEKASP GAVARLEADA KQPE