ID Q04E67_OENOB Unreviewed; 567 AA.
AC Q04E67;
DT 14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 14-NOV-2006, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE RecName: Full=Septation ring formation regulator EzrA {ECO:0000256|HAMAP-Rule:MF_00728};
GN Name=ezrA {ECO:0000256|HAMAP-Rule:MF_00728};
GN OrderedLocusNames=OEOE_1393 {ECO:0000313|EMBL:ABJ57255.1};
OS Oenococcus oeni (strain ATCC BAA-331 / PSU-1).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Oenococcus.
OX NCBI_TaxID=203123 {ECO:0000313|EMBL:ABJ57255.1, ECO:0000313|Proteomes:UP000000774};
RN [1] {ECO:0000313|EMBL:ABJ57255.1, ECO:0000313|Proteomes:UP000000774}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-331 / PSU-1 {ECO:0000313|Proteomes:UP000000774};
RX PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA Makarova K., Slesarev A., Wolf Y., Sorokin A., Mirkin B., Koonin E.,
RA Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA Baldwin K., Lee J.H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J., Hutkins R.,
RA O'Sullivan D., Steele J., Unlu G., Saier M., Klaenhammer T., Richardson P.,
RA Kozyavkin S., Weimer B., Mills D.;
RT "Comparative genomics of the lactic acid bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006).
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}.
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DR EMBL; CP000411; ABJ57255.1; -; Genomic_DNA.
DR RefSeq; WP_011677695.1; NC_008528.1.
DR AlphaFoldDB; Q04E67; -.
DR STRING; 203123.OEOE_1393; -.
DR KEGG; ooe:OEOE_1393; -.
DR PATRIC; fig|203123.7.peg.1408; -.
DR eggNOG; COG4477; Bacteria.
DR HOGENOM; CLU_034079_1_0_9; -.
DR Proteomes; UP000000774; 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 {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:UP000000774};
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..3
FT /note="Extracellular"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00728"
FT TOPO_DOM 23..567
FT /note="Cytoplasmic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00728"
FT COILED 113..154
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00728"
FT COILED 310..337
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00728"
FT COILED 455..489
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00728"
SQ SEQUENCE 567 AA; 65247 MW; 6472AFFAFC4256A5 CRC64;
MIWVLLIISI ILLVSYLAAV LFQRSYAKRA NEVAEEKDKL AQINVRQALL DARKLSLTGK
SLHEYQQLEA DYNDIENSKF LHIDQLANSV VFDSRGLNVF KTRDEFNTLN STLKETKAKI
ASIQGGLEKL NEVDQEHRKA VDELRLRYDK LRKKILAGSF KYGPASEPLE NVLSGLEDNF
AKFVKLTESG DHTAATDVYE QLRVETNDLE KKMIDIPPLY DKLVNRYPTN FKELQNGADQ
LTKQGFVFDA DPNVVIADMK KSHSQILNAL KNLDMKKTAD AERILEVQIK TLYDTIENEY
GAEYDVKKND RRLTNQLKHV RAQNQELTLE IDRLAHRFTL SHSEVEDTRG WGEQIKSVSE
QNEESKKRWH EKKAPFTAIR EIQNGLFEQL DQIAKNQKDL YITISSYPQV FDDLKRISLQ
YSGELSNIRR ILEQVDMPGL PADYRLQFIS VQDEIKALNN MVSASRVNLD DAQRQAHEVT
TDLADLKSSS SELYVNANLA VELIHYANRF SDRQEIISAL QQARLYYERD LDYGRTVDLV
GRALDQVDPG SYERLKDGYT NRNQTPF
//
