ID A0A0B0CYX0_9BACI Unreviewed; 563 AA.
AC A0A0B0CYX0;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=Septation ring formation regulator EzrA {ECO:0000256|HAMAP-Rule:MF_00728};
GN Name=ezrA {ECO:0000256|HAMAP-Rule:MF_00728};
GN ORFNames=LD39_15355 {ECO:0000313|EMBL:KHE68056.1};
OS Halobacillus sp. BBL2006.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halobacillus.
OX NCBI_TaxID=1543706 {ECO:0000313|EMBL:KHE68056.1, ECO:0000313|Proteomes:UP000030879};
RN [1] {ECO:0000313|EMBL:KHE68056.1, ECO:0000313|Proteomes:UP000030879}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BBL2006 {ECO:0000313|EMBL:KHE68056.1,
RC ECO:0000313|Proteomes:UP000030879};
RA Kirchner G., Treves D., Francis J.III.;
RT "Draft Genome Sequence of the Halophilic Bacterium Halobacillus sp. Strain
RT BBL2006.";
RL Submitted (SEP-2014) 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:0000256|HAMAP-
CC Rule:MF_00728}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00728};
CC Single-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_00728}.
CC Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004167}. Note=Colocalized with FtsZ to the
CC nascent septal site. {ECO:0000256|HAMAP-Rule:MF_00728}.
CC -!- SIMILARITY: Belongs to the EzrA family. {ECO:0000256|HAMAP-
CC Rule:MF_00728}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KHE68056.1}.
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DR EMBL; JRNX01000534; KHE68056.1; -; Genomic_DNA.
DR RefSeq; WP_035549152.1; NZ_JRNX01000534.1.
DR AlphaFoldDB; A0A0B0CYX0; -.
DR OrthoDB; 1654473at2; -.
DR Proteomes; UP000030879; Unassembled WGS sequence.
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.
DR SUPFAM; SSF57997; Tropomyosin; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|HAMAP-Rule:MF_00728};
KW Cell division {ECO:0000256|HAMAP-Rule:MF_00728};
KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_00728};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|HAMAP-
KW Rule:MF_00728};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00728};
KW Reference proteome {ECO:0000313|Proteomes:UP000030879};
KW Septation {ECO:0000256|ARBA:ARBA00023210, ECO:0000256|HAMAP-Rule:MF_00728};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_00728};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_00728}.
FT TOPO_DOM 1..2
FT /note="Extracellular"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00728"
FT TOPO_DOM 22..563
FT /note="Cytoplasmic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00728"
FT COILED 105..136
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00728"
FT COILED 376..465
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00728"
SQ SEQUENCE 563 AA; 66620 MW; 7F0BEF7E4250291E CRC64;
MKYVIGAILL LIALFIIGLI WRKKVYDEVD RLESWKMDIM NRRVTEELSK VKSLNLSGET
QERFEKWRSR WDRILTKELP ALEEDLFDAE EAADKYQWKR VKKVLADTEK KLLNIEEDIQ
KMFEELENLL DSEKNSRIEI ESLEPELKEL SKTLIHSRHQ FGKAVYVFEK RVEELKGKLQ
QYEQLTEQGN YLEANSLVQS IRDELLILQD EIAYFPERYR KAHSELPDLL NELKSGIEEM
EGEGYRISHL DYYPEIEKYE EMLKESVIKL EKADQSDVEE LILEIETSIQ EMYEVLENEA
VAHNYVDKHY KPIQAQLDRL SQVLSGTERE LEETQTAYQL DDQDVEAYRG IKSWYNQMKN
KVSSVDHKRQ DGKTAYTEIR EQLELVKQQL DEIQEKHEHF NERIQTLRKD EVEAKTKLSN
MEQLLLDTHR RLKRSNIPGI PTSIYENMKT ASEQMDEAFQ SLEKQPLDMV EVHAKLQEAA
ALTENLHEHA EKIMEKACYT ERLIQYGNRY KSKYPILAAR LLEAENEFRS YHYEEALEIA
SEAIKEVDPE ALSRIEEKEQ VLV
//