EZRA_BACC4
ID EZRA_BACC4 Reviewed; 570 AA.
AC B7H705;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 62.
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=BCB4264_A4758;
OS Bacillus cereus (strain B4264).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=405532;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B4264;
RA Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A.,
RA Ravel J., Sutton G.;
RT "Genome sequence of Bacillus cereus B4264.";
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001176; ACK59013.1; -; Genomic_DNA.
DR RefSeq; WP_000377304.1; NZ_VEHB01000005.1.
DR AlphaFoldDB; B7H705; -.
DR SMR; B7H705; -.
DR EnsemblBacteria; ACK59013; ACK59013; BCB4264_A4758.
DR KEGG; bcb:BCB4264_A4758; -.
DR HOGENOM; CLU_034079_1_0_9; -.
DR OMA; FRSQNHI; -.
DR Proteomes; UP000007096; 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_1000132704"
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; 66486 MW; 6901EA3407FE87EB CRC64;
MDSILTIVII VVSSILVLLM IELVIRNRSY KDIEALEQWK QEIKDKPVAD ELKRVKDLNM
TGQTEELFGK WREEWDEIVS TTLPKADKDL AQARKFASQF SFRKAKHAMN ESISGLDDAD
NRITDILNEL QQLLESHEKN SSEIEGLRDT YRSMKKSVLA HRHMYGAAEQ KIEEMLDAES
EKFKTFEEAT NNGDYLKARE IVISLEEGLA DLEIIIHQIP DLLVECQATL PVQLEDLLHG
HNDMVRQGYV LDYLEVPKEV RDMTKQLQTC LMDIQELHIT EAAEKVENLK TRLDGFYDQL
EQEVHARHYV EQKTLSVYDD LEEMRIETIE TKTETQLVKQ SYQLQDKDIE SQKVIEKQMH
ILTKRFEMLQ LRVAEQDIAF SIIREELEEV YEQCETLKVL HAEYKEMLQA MRKEEFEARE
KLQEMRNTIF ETKRFMQKSN LPGLPESIME DLKRGQMAMQ AVYEQLEVKP LNMNAVNSSL
EEAYTTVNSV AEMTEELIGQ AYLVEKLIQY GNRYRSHDEN LAESLNYAEK LFREYQYDAA
LEQAASVLEQ LEPGVVQKIA EYVDNEQTLS