ID   EZRA_GEOKA              Reviewed;         567 AA.
AC   Q5KW53;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Septation ring formation regulator EzrA {ECO:0000255|HAMAP-Rule:MF_00728};
GN   Name=ezrA {ECO:0000255|HAMAP-Rule:MF_00728}; OrderedLocusNames=GK2798;
OS   Geobacillus kaustophilus (strain HTA426).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC   Geobacillus thermoleovorans group.
OX   NCBI_TaxID=235909;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTA426;
RX   PubMed=15576355; DOI=10.1093/nar/gkh970;
RA   Takami H., Takaki Y., Chee G.-J., Nishi S., Shimamura S., Suzuki H.,
RA   Matsui S., Uchiyama I.;
RT   "Thermoadaptation trait revealed by the genome sequence of thermophilic
RT   Geobacillus kaustophilus.";
RL   Nucleic Acids Res. 32:6292-6303(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; BA000043; BAD77083.1; -; Genomic_DNA.
DR   RefSeq; WP_011232272.1; NC_006510.1.
DR   AlphaFoldDB; Q5KW53; -.
DR   SMR; Q5KW53; -.
DR   STRING; 235909.GK2798; -.
DR   EnsemblBacteria; BAD77083; BAD77083; GK2798.
DR   KEGG; gka:GK2798; -.
DR   PATRIC; fig|235909.7.peg.2984; -.
DR   eggNOG; COG4477; Bacteria.
DR   HOGENOM; CLU_034079_1_0_9; -.
DR   OMA; FRSQNHI; -.
DR   Proteomes; UP000001172; 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..567
FT                   /note="Septation ring formation regulator EzrA"
FT                   /id="PRO_1000045896"
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          98..159
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
FT   COILED          251..497
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
SQ   SEQUENCE   567 AA;  66465 MW;  DAD1D17DF6B9DAFE CRC64;
     MGMAWIVLLL GAGAIIYNHV YRKRMYREID RLEEWKINLM NRPVPDELAK VKQLNMTGET
     EQLFERWRQQ WDDIVAVKLP NVEEQLFDAE RLLDKYRYRQ ARRLLGQIAD GLRRLEEEVH
     EIIHEVNELI GSEEQSRAEI EELRAAHREA KKALLAYRYT FGSAADLLDV RLTEAEKQFQ
     RFAELTEAGN YLAARDVVLT LKEELGRLTA MMEEIPKLLG ECQTSLPAQL AELADGYREM
     EERGYILDHL HMERTLQEKR EKIEQCLAMI HELRIEEAKQ IVAELKEEID ALYDLLENEV
     LAHQYVQTEM PRLSGMLQEL AAEAKETEAE ALFVQQSYHL APSDLEKYRS IEKQLHQLQK
     RFFLIQDRVA EAKTAYSLLK EELEQLVSQI DLMKEEHEQF RTMLQTLRKD ELIAREKLDG
     MRKTLAEALR LVQKSRLPGL PEPYALELAE ARRSLQAVAA RLEEKPLDMP AVDQALEEAK
     AAVERLYERT VEMIEQATLA ERTIQYGNRY RRRYPAVRKG LEEAEFLFRH YDYEEALRQA
     VAAVEEVEPG AFDRVQKLWQ EDNSREQ