EZRA_BACCR
ID EZRA_BACCR Reviewed; 570 AA.
AC Q817A9;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=Septation ring formation regulator EzrA {ECO:0000255|HAMAP-Rule:MF_00728};
GN Name=ezrA {ECO:0000255|HAMAP-Rule:MF_00728}; OrderedLocusNames=BC_4649;
OS Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS 15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=226900;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373
RC / NCTC 2599 / NRRL B-3711;
RX PubMed=12721630; DOI=10.1038/nature01582;
RA Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.;
RT "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT anthracis.";
RL Nature 423:87-91(2003).
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; Single-pass membrane protein.
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; AE016877; AAP11556.1; -; Genomic_DNA.
DR RefSeq; NP_834355.1; NC_004722.1.
DR RefSeq; WP_000377302.1; NC_004722.1.
DR AlphaFoldDB; Q817A9; -.
DR SMR; Q817A9; -.
DR STRING; 226900.BC_4649; -.
DR EnsemblBacteria; AAP11556; AAP11556; BC_4649.
DR KEGG; bce:BC4649; -.
DR PATRIC; fig|226900.8.peg.4813; -.
DR HOGENOM; CLU_034079_1_0_9; -.
DR OMA; FRSQNHI; -.
DR Proteomes; UP000001417; 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..570
FT /note="Septation ring formation regulator EzrA"
FT /id="PRO_0000172868"
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; 66442 MW; 691B2A2EDC8E9D2B 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
EEAYTTVNGV AEMTEELIGQ AYLVEKLIQY GNRYRSHDEN LAESLNYAEK LFREYQYDAA
LEQAASVLEQ LEPGVVQKIA EYVDNDQTLS