ID U5P4T5_9STRE Unreviewed; 574 AA.
AC U5P4T5;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE RecName: Full=Septation ring formation regulator EzrA {ECO:0000256|HAMAP-Rule:MF_00728};
GN Name=ezrA {ECO:0000256|HAMAP-Rule:MF_00728};
GN ORFNames=N597_06020 {ECO:0000313|EMBL:AGY38515.1};
OS Streptococcus ilei.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1156431 {ECO:0000313|EMBL:AGY38515.1, ECO:0000313|Proteomes:UP000017124};
RN [1] {ECO:0000313|EMBL:AGY38515.1, ECO:0000313|Proteomes:UP000017124}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=I-P16 {ECO:0000313|Proteomes:UP000017124};
RA Hyun D.-W.;
RT "Genome sequence of Streptococcus SP. I-P16 isolated from human ileal
RT fluid.";
RL Submitted (SEP-2013) 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; CP006776; AGY38515.1; -; Genomic_DNA.
DR RefSeq; WP_023023812.1; NC_022582.1.
DR AlphaFoldDB; U5P4T5; -.
DR STRING; 1156433.N597_06020; -.
DR KEGG; sip:N597_06020; -.
DR PATRIC; fig|1156433.3.peg.1174; -.
DR HOGENOM; CLU_034079_2_0_9; -.
DR Proteomes; UP000017124; 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 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..7
FT /note="Extracellular"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00728"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TOPO_DOM 27..574
FT /note="Cytoplasmic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00728"
FT COILED 322..415
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00728"
SQ SEQUENCE 574 AA; 65697 MW; 9551C6442D662B72 CRC64;
MSRGLIILII VIGVLLVLGY VVAVLLRKRN EALLAALEER KEELYNLPVN DEVEAVKNMH
LIGQSQVAFR EWNQKWVDLS LNSFADIENN LFEAEGYNNS FRFLKAKQAI GNIESQVQLI
DEDIKAIRQA LSELKEKEEM NSGRVVHALD MFENLQKQVA SDPDAYGPAL PEIEKQSEKI
QDEFSKFVTL NSSGDPVEAA EILDTAENHI VALTHIVEKV PAIVKDLQTT LPDQLEDLES
GYRKLLESGY HFTETDLEAR FQQLHAALKA NLANVAALEL DNALYENEQI QEEINALYDI
FTREIESHKV VEKLVKALPG YLAHAKENNK SLAEEVERLS KIFESKVLKE NHLKELEAEL
TAQELVVEDA LNDTSETQKA YSILQEELEA IEERLKEIED DQIALSETLS KIEKDDTNAR
QKVNIYANRL HAIKRYMDKR NLPGIPQSFL TIFFTASDNT EALLAELEGR RVNIENVNRL
LDILTNDMTE LEEETYKLVQ YATLTEQLLQ YSNRYRSFDD HVQAAFDEAL YIFEKEYDYP
ASFKVISEAL ETVEPGVTER FVSSYEKTRE SIRF
//
