EZRA_BACVZ
ID EZRA_BACVZ Reviewed; 563 AA.
AC A7Z7N6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Septation ring formation regulator EzrA {ECO:0000255|HAMAP-Rule:MF_00728};
GN Name=ezrA {ECO:0000255|HAMAP-Rule:MF_00728}; OrderedLocusNames=RBAM_026540;
OS Bacillus velezensis (strain DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42)
OS (Bacillus amyloliquefaciens subsp. plantarum).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus amyloliquefaciens group.
OX NCBI_TaxID=326423;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42;
RX PubMed=17704766; DOI=10.1038/nbt1325;
RA Chen X.H., Koumoutsi A., Scholz R., Eisenreich A., Schneider K.,
RA Heinemeyer I., Morgenstern B., Voss B., Hess W.R., Reva O., Junge H.,
RA Voigt B., Jungblut P.R., Vater J., Suessmuth R., Liesegang H.,
RA Strittmatter A., Gottschalk G., Borriss R.;
RT "Comparative analysis of the complete genome sequence of the plant growth-
RT promoting bacterium Bacillus amyloliquefaciens FZB42.";
RL Nat. Biotechnol. 25:1007-1014(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; CP000560; ABS75012.1; -; Genomic_DNA.
DR RefSeq; WP_012118185.1; NC_009725.2.
DR AlphaFoldDB; A7Z7N6; -.
DR SMR; A7Z7N6; -.
DR STRING; 326423.RBAM_026540; -.
DR EnsemblBacteria; ABS75012; ABS75012; RBAM_026540.
DR KEGG; bay:RBAM_026540; -.
DR HOGENOM; CLU_034079_1_0_9; -.
DR OMA; FRSQNHI; -.
DR Proteomes; UP000001120; 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; Septation;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..563
FT /note="Septation ring formation regulator EzrA"
FT /id="PRO_1000045890"
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..563
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
FT COILED 133..159
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
FT COILED 243..276
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
FT COILED 309..529
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
SQ SEQUENCE 563 AA; 65384 MW; A363A12BAA3ED4AB CRC64;
MELVIGLLVI LLALFAAGYF FRKKIYTEID RLESWKIEIL NRSIVEEMSK IKHLKMTGET
EEFFERWREE WDEIVTAHLP KVEELLYDAE ENADKYRFKK ANQVLVHIDD LLTAAESNIE
GILREISDLV TSEEKSRGEI EQVRERYSKA RKNLLAYSHL YGELYNSLET DLDEIWSGIK
EFEEETESGN YIKARKVLLE QDRRLDQLQT YIDDVPKLLA DCKQTVPNQI AKLKDGYREM
TEKGYKLEHI QIEKELDTLT NQVKRAENAL LEELDVDEAS AILQLIDETI QSMYEQLEGE
VEAGQSVLSK MPELIIAYEK LEEEKDRTKT ETELVKESYQ LTAGEIGRQH AFEKQLETIG
RLLEQAREKL DGEHVAYSLL IEEVEAIEKQ LEEAQKEHAE YRENLQALRK EELQARETLM
HLRKTISDTA RMLQKSNVPG IPEQVKDKLE TANHHIEETV SQLEELPLNM EEAAKHLDEA
EKVVEEVSEE AEDLVIQVKL IERIIQYGNR FRSQNHILSE QLKEAERLFY AYSYNEAYEM
AADAVEKAAP GAVKKIKADQ SAS