EZRA_STRU0
ID EZRA_STRU0 Reviewed; 574 AA.
AC B9DRR4;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 25-MAY-2022, entry version 67.
DE RecName: Full=Septation ring formation regulator EzrA {ECO:0000255|HAMAP-Rule:MF_00728};
GN Name=ezrA {ECO:0000255|HAMAP-Rule:MF_00728}; OrderedLocusNames=SUB0650;
OS Streptococcus uberis (strain ATCC BAA-854 / 0140J).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=218495;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-854 / 0140J;
RX PubMed=19175920; DOI=10.1186/1471-2164-10-54;
RA Ward P.N., Holden M.T.G., Leigh J.A., Lennard N., Bignell A., Barron A.,
RA Clark L., Quail M.A., Woodward J., Barrell B.G., Egan S.A., Field T.R.,
RA Maskell D., Kehoe M., Dowson C.G., Chanter N., Whatmore A.M., Bentley S.D.,
RA Parkhill J.;
RT "Evidence for niche adaptation in the genome of the bovine pathogen
RT Streptococcus uberis.";
RL BMC Genomics 10:54-54(2009).
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; AM946015; CAR41505.1; -; Genomic_DNA.
DR RefSeq; WP_012658169.1; NC_012004.1.
DR AlphaFoldDB; B9DRR4; -.
DR SMR; B9DRR4; -.
DR STRING; 218495.SUB0650; -.
DR EnsemblBacteria; CAR41505; CAR41505; SUB0650.
DR KEGG; sub:SUB0650; -.
DR eggNOG; COG4477; Bacteria.
DR HOGENOM; CLU_034079_2_0_9; -.
DR OMA; FRSQNHI; -.
DR OrthoDB; 670472at2; -.
DR Proteomes; UP000000449; 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_1000148074"
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 102..140
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
FT COILED 243..379
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
FT COILED 459..520
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
SQ SEQUENCE 574 AA; 66465 MW; 8FBAF1EFC456D42E CRC64;
MSSGIILLIV AIVLLVIIAY LIGVIIRKRN DSMIGTLEDR KQHLFGLPVN EEIEEVKELH
LIGQSQTSFR EWNQKWVDLT LNSFADIENH LFEAEKYNDT FNFIRAKHEI NNVESQLNLV
EEDITSIREA LSILKEQEEK NSARVTHALD LYEKLQSSVA ENDSHFGTTK PEIEKQMKNI
ETEFSQFVTL NSSGDPVEAS EVLDRAEEHT IALGQITEQI PAIVAKLEDE FPDQLDDLES
GYRRLLEDNY HFAENNIEEK FQEIREAIRS NASELVSLDL DRAREENSHI QERIDNMYAL
FEHEIKAFKV SAKHSKIIPS YLEHAKSNND KLKEEMTRLS RKYILNENQA STVQGFEKEI
EDVEKNVLEL AKDFKGQEIP YSELQVVFEK NLKTLSAVES GQMEVFESIK NIENIEEDAR
KEADLYVTQL HMIKRFMEKR HLPGIPQDYL NVFFTTSTQL EALMDELSKG KINIEAVSRL
RDVASASIAN LEDYTYQVVE NATLTEQLLQ YSNRYRSFEA GVQNSFEIAM HLFEVEYDYQ
ASFDEISYAL ETVEPGVTDR FVSSYERTRE HIRF