EZRA_BACCZ
ID EZRA_BACCZ Reviewed; 570 AA.
AC Q633E6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=Septation ring formation regulator EzrA {ECO:0000255|HAMAP-Rule:MF_00728};
GN Name=ezrA {ECO:0000255|HAMAP-Rule:MF_00728}; OrderedLocusNames=BCE33L4393;
OS Bacillus cereus (strain ZK / E33L).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=288681;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZK / E33L;
RX PubMed=16621833; DOI=10.1128/jb.188.9.3382-3390.2006;
RA Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Bruce D.,
RA Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C.,
RA Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A.,
RA Hill K.K., Hitchcock P., Jackson P.J., Keim P., Kewalramani A.R.,
RA Longmire J., Lucas S., Malfatti S., McMurry K., Meincke L.J., Misra M.,
RA Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., Parson-Quintana B.,
RA Reilly L.P., Richardson P., Robinson D.L., Rubin E., Saunders E., Tapia R.,
RA Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L.,
RA Brettin T.S., Gilna P.;
RT "Pathogenomic sequence analysis of Bacillus cereus and Bacillus
RT thuringiensis isolates closely related to Bacillus anthracis.";
RL J. Bacteriol. 188:3382-3390(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; CP000001; AAU15877.1; -; Genomic_DNA.
DR RefSeq; WP_000377289.1; NZ_CP009968.1.
DR AlphaFoldDB; Q633E6; -.
DR SMR; Q633E6; -.
DR EnsemblBacteria; AAU15877; AAU15877; BCE33L4393.
DR GeneID; 45024522; -.
DR KEGG; bcz:BCE33L4393; -.
DR PATRIC; fig|288681.22.peg.978; -.
DR OMA; FRSQNHI; -.
DR Proteomes; UP000002612; 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_1000045893"
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 272..304
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
FT COILED 355..429
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
SQ SEQUENCE 570 AA; 66436 MW; FA24F41AADACC769 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 LDYLEVPKEV RDMTKQLQTC LIDIQELHIT EAAEKVENLK TRLDGFYDQL
EQEVHARHYV EQKTLSVYED LEEIRTETIE TKAETQLVKQ SYQLQDKDIE SQKVIEKQMH
ILTKRFEMLQ LRVAEQDIAF SIIREELEEI YEQCETLKVL HAEYKEMLQT MRKEEFEARE
KLQEMRNTIF ETKRFMQKSN LPGLPESIME DLKRGQMAMQ AVYEQLEVKP LNMNAVNSSL
EEAYTTVNGV AEMTEELIGQ AYLVEKLIQY GNRYRSHDEN LAESLNYAEK LFREYQYDAA
LEQAASVLEQ LEPGVVQKIA EYVDNEQTLS