EZRA_STRSV
ID EZRA_STRSV Reviewed; 574 AA.
AC A3CMA0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=Septation ring formation regulator EzrA {ECO:0000255|HAMAP-Rule:MF_00728};
GN Name=ezrA {ECO:0000255|HAMAP-Rule:MF_00728}; OrderedLocusNames=SSA_0879;
OS Streptococcus sanguinis (strain SK36).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=388919;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK36;
RX PubMed=17277061; DOI=10.1128/jb.01808-06;
RA Xu P., Alves J.M., Kitten T., Brown A., Chen Z., Ozaki L.S., Manque P.,
RA Ge X., Serrano M.G., Puiu D., Hendricks S., Wang Y., Chaplin M.D., Akan D.,
RA Paik S., Peterson D.L., Macrina F.L., Buck G.A.;
RT "Genome of the opportunistic pathogen Streptococcus sanguinis.";
RL J. Bacteriol. 189:3166-3175(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; CP000387; ABN44305.1; -; Genomic_DNA.
DR RefSeq; WP_011836769.1; NC_009009.1.
DR RefSeq; YP_001034855.1; NC_009009.1.
DR AlphaFoldDB; A3CMA0; -.
DR SMR; A3CMA0; -.
DR STRING; 388919.SSA_0879; -.
DR EnsemblBacteria; ABN44305; ABN44305; SSA_0879.
DR KEGG; ssa:SSA_0879; -.
DR PATRIC; fig|388919.9.peg.840; -.
DR eggNOG; COG4477; Bacteria.
DR HOGENOM; CLU_034079_2_0_9; -.
DR OMA; FRSQNHI; -.
DR OrthoDB; 670472at2; -.
DR Proteomes; UP000002148; 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..574
FT /note="Septation ring formation regulator EzrA"
FT /id="PRO_1000045914"
FT TOPO_DOM 1..7
FT /note="Extracellular"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
FT TRANSMEM 8..26
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
FT TOPO_DOM 27..574
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
FT COILED 26..47
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
FT COILED 105..189
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
FT COILED 258..346
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
FT COILED 375..415
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
FT COILED 455..494
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
SQ SEQUENCE 574 AA; 65961 MW; B12606BB692D9295 CRC64;
MSIGLVILVA VVALLLVVGY GTAVLMRKRN EALLQNLEER KEALYNLPVN DEVEEVKNMH
LIGQSQVAFR EWNQKWVDLS LNSFADIENN LFEAEGYNNS FRFIKAKHAI GNIESQIDLI
EEDIKMIRAA LEDLKEQESK NSGRVLHALD LFEKLQTQVA ENADSYGQAL AEIEKQLENI
QSEFSQFVTL NSSGDPVEAA EILDKAEDHI LALTHIVEKV PAIVEELTVK LPDQLEDLES
GHRKLLESGY HFIETDIESR FQQLHASLKR NEANISALEL DNAEYENEQA QEEINALYEI
FTREIEAHKV VEKLIKNLPS YLAHTKENNQ QLQKEIERLS QTFLISDTET SHVKELQAEL
SAQEDVVLSA VEDSSETKQA YSVVQEELEA IQERLKEIED EQISLGEALA EIEKDDANAR
QKVNIYANKL HTIKRYMEKR NLPGIPDSFL EIFFSTSNNI EELVKELEAT RVNIESVNRW
LEILGNDMEQ LEEETYRIVQ DATLTEQLLQ YSNRYRSFDD NVQAAFNKSL YVFEHDYDYA
QSLEIISKAL DLVEPGVTER FVTSYEKTRE NIRF