EZRA_GEOSW
ID EZRA_GEOSW Reviewed; 567 AA.
AC C5D695;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Septation ring formation regulator EzrA {ECO:0000255|HAMAP-Rule:MF_00728};
GN Name=ezrA {ECO:0000255|HAMAP-Rule:MF_00728}; OrderedLocusNames=GWCH70_2720;
OS Geobacillus sp. (strain WCH70).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC unclassified Geobacillus.
OX NCBI_TaxID=471223;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WCH70;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Brumm P., Mead D.A., Richardson P.;
RT "Complete sequence of chromosome of Geopacillus sp. WCH70.";
RL Submitted (JUN-2009) 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}.
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DR EMBL; CP001638; ACS25411.1; -; Genomic_DNA.
DR RefSeq; WP_015864817.1; NC_012793.1.
DR AlphaFoldDB; C5D695; -.
DR SMR; C5D695; -.
DR STRING; 471223.GWCH70_2720; -.
DR PRIDE; C5D695; -.
DR EnsemblBacteria; ACS25411; ACS25411; GWCH70_2720.
DR KEGG; gwc:GWCH70_2720; -.
DR eggNOG; COG4477; Bacteria.
DR HOGENOM; CLU_034079_1_0_9; -.
DR OMA; FRSQNHI; -.
DR OrthoDB; 670472at2; -.
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..567
FT /note="Septation ring formation regulator EzrA"
FT /id="PRO_1000212729"
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..567
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
FT COILED 97..188
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
FT COILED 254..465
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
SQ SEQUENCE 567 AA; 67026 MW; A889C300ADD183C5 CRC64;
MEIAVIVLLL LGGVMIYNHV YRKKMYSEID RLEAWKISIM NRPVPDELSK VKQLNMTGET
EQLFEKWRQK WDDLVAVKLP DVEEKLFDTE ELLDKYRYAK AKAVLREIDQ LLRQAEEEVQ
LIIDEVHELI GSEEQNRTEI EELRTMYREA KKTLLAYRYT FGVAAAKLDE KLEEIESKFK
QFEELTASGN YLAAREIVLS SKGELNKVTE MMSDIPELLT ECQTTIPAQL EELYDGYKEM
KQEGYILDHL QIDREIVQKR EKIEQCMQMI GDLQIEEAKQ GITEIKEEID TLYDLLEKEV
ISHHYIKTEM SRIEEMLNEL NEEAKETSEE TLFVQQSYRL STKDLEKYRS IEKQIHQLMK
RFEIIQARIL EAKTAHSLLK EELEQLLAQI EMMKEEHEEF RKMLQTLRKD ELVAREKLDE
MKKKLSEAMR LVQKSRLPGL PKSYELQLSE AKDSLMKVAV RLEEKPLNMS AVHQALEESG
NMVQRVYERT VEMIEQASLV EKVIQYGNRY RRRYPSVKEG LEEAEFLFRH YDYEQALEQA
VAALEKVEPG ALQRIQQIFR DERSKEE