ID EZRA_BACP2 Reviewed; 567 AA.
AC A8FG97;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE RecName: Full=Septation ring formation regulator EzrA {ECO:0000255|HAMAP-Rule:MF_00728};
GN Name=ezrA {ECO:0000255|HAMAP-Rule:MF_00728}; OrderedLocusNames=BPUM_2606;
OS Bacillus pumilus (strain SAFR-032).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=315750;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAFR-032;
RX PubMed=17895969; DOI=10.1371/journal.pone.0000928;
RA Gioia J., Yerrapragada S., Qin X., Jiang H., Igboeli O.C., Muzny D.,
RA Dugan-Rocha S., Ding Y., Hawes A., Liu W., Perez L., Kovar C., Dinh H.,
RA Lee S., Nazareth L., Blyth P., Holder M., Buhay C., Tirumalai M.R., Liu Y.,
RA Dasgupta I., Bokhetache L., Fujita M., Karouia F., Eswara Moorthy P.,
RA Siefert J., Uzman A., Buzumbo P., Verma A., Zwiya H., McWilliams B.D.,
RA Olowu A., Clinkenbeard K.D., Newcombe D., Golebiewski L., Petrosino J.F.,
RA Nicholson W.L., Fox G.E., Venkateswaran K., Highlander S.K.,
RA Weinstock G.M.;
RT "Paradoxical DNA repair and peroxide resistance gene conservation in
RT Bacillus pumilus SAFR-032.";
RL PLoS ONE 2:E928-E928(2007).
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; CP000813; ABV63264.1; -; Genomic_DNA.
DR RefSeq; WP_012010900.1; NZ_VEIC01000003.1.
DR AlphaFoldDB; A8FG97; -.
DR SMR; A8FG97; -.
DR STRING; 315750.BPUM_2606; -.
DR KEGG; bpu:BPUM_2606; -.
DR eggNOG; COG4477; Bacteria.
DR HOGENOM; CLU_034079_1_0_9; -.
DR OrthoDB; 1654473at2; -.
DR Proteomes; UP000001355; Chromosome.
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_1000062106"
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 108..185
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
FT COILED 243..375
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
FT COILED 402..529
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
SQ SEQUENCE 567 AA; 66335 MW; 0E34F5C63BAC581C CRC64;
MEFIIGLIVI LLALFSVGYF LRKNIYKEID RLEAWKIEIL NRSIVEEISK IKHLKMTGET
EQFFERWRAE WDDIVTAHLP KVEELLYDAE EYSDKYRFSK AKQVLTHIED LLSAADSNIE
DILKEIADLV TSEEQNRKDI EKVKEQYQTV RKNLLAYSHL YGTLYDKMEQ DLDEAWEGIK
QYEEETENGN YMKARKILLE QDRRLDQLQL YINDVPKLIA DCKQTVPGQL TKLKDGYQEM
SEKGYKLEHI QITKELETLN KQLARAEKLL IDELNLEEAS SILQMIDDAI ETLYDQLEAE
VEAGQEIKSR MPELTEAFEK LEQDHTQTKA ETALVKESYK LTAGELDQQK AFEKRLEEIE
KLMKQIREKL DRDHVAYSLL MDEINQLETF IEDAKALHDT FKGHLQSLRK EELQARETLA
ELKTMLTDTV RQLHKSNIPG VPAEMKERAE KAQEMIHQVH EQLENLPLNM PAVNQQLKEA
SDTVRNVVDE TEEMLSKVDQ IERIIQYGNR FRSQNHILSE QLKEAERRFY AYDYNGSFDI
AAAAVEKASP GAVQKLLAQQ EKEYQHQ
//
