ID A0A377KGD8_9ENTE Unreviewed; 573 AA.
AC A0A377KGD8;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Septation ring formation regulator EzrA {ECO:0000256|HAMAP-Rule:MF_00728};
GN Name=ezrA {ECO:0000256|HAMAP-Rule:MF_00728,
GN ECO:0000313|EMBL:STP28260.1};
GN ORFNames=NCTC8129_00379 {ECO:0000313|EMBL:STP28260.1};
OS Enterococcus durans.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=53345 {ECO:0000313|EMBL:STP28260.1, ECO:0000313|Proteomes:UP000254070};
RN [1] {ECO:0000313|EMBL:STP28260.1, ECO:0000313|Proteomes:UP000254070}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC8129 {ECO:0000313|EMBL:STP28260.1,
RC ECO:0000313|Proteomes:UP000254070};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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; UGIF01000002; STP28260.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A377KGD8; -.
DR Proteomes; UP000254070; Unassembled WGS sequence.
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 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..8
FT /note="Extracellular"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00728"
FT TRANSMEM 6..27
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TOPO_DOM 28..573
FT /note="Cytoplasmic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00728"
FT COILED 111..166
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00728"
FT COILED 461..495
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00728"
SQ SEQUENCE 573 AA; 67347 MW; 1F69D6A220B39F7C CRC64;
MGNNVIIGIV IAIIIVAIVV FLVSYLMKKK NQDRLDALEK RKEELFDLPV IEEVDDVKKM
HLVGQSQNTF REWSQKWNDI STSSFAELES QIFEVENLNE SFRFLKGKKA VVEAENTMNQ
MEKEVSEIRE GLKELRETEE RNSLAVQQAL DIYEELKETI KEDEQSYGPA FPELQKQVKM
IESEFTQFVT LNTSGDPVEA REVLDKAEKH TYEVDALMKK IPPLYEDLAT TFPEQLEEID
DTYEKLMQEQ YVFPEEDLVG EIDKVRNRIQ GSLANLEKTE VETVEFENRE TANMIDALYD
ILEREIDAQN YVATNQSTIE QYIKHATKNN RQLLIELDHT AQSYALNHNE IGRVRGFQTE
VEEIERQNEQ MKPQIQQHTV PYSEVRTFYK KVFKILEDIE NQQVEIDDSL HELRKGEKEA
QEKIDTFEFK LRSLKRFVEK QRLPGLPNDY LEFFFVATER IEELSVVLNK IRVNMEEVNR
LVALCEEDLE LLDKKTHDLV DAAALTEQML QYANRYRHTH EEVKEAIDKS YFMFSKEYHY
QEALDEIGTA LERVEPGAFK RIEDFYFNHP DLV
//
