ID A0A1I1TRA3_9BACI Unreviewed; 564 AA.
AC A0A1I1TRA3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
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=SAMN05216238_102413 {ECO:0000313|EMBL:SFD61236.1};
OS Lentibacillus persicus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lentibacillus.
OX NCBI_TaxID=640948 {ECO:0000313|EMBL:SFD61236.1, ECO:0000313|Proteomes:UP000199474};
RN [1] {ECO:0000313|EMBL:SFD61236.1, ECO:0000313|Proteomes:UP000199474}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22530 {ECO:0000313|EMBL:SFD61236.1,
RC ECO:0000313|Proteomes:UP000199474};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FOMR01000002; SFD61236.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I1TRA3; -.
DR STRING; 640948.SAMN05216238_102413; -.
DR OrthoDB; 1654473at2; -.
DR Proteomes; UP000199474; 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..2
FT /note="Extracellular"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00728"
FT TOPO_DOM 22..564
FT /note="Cytoplasmic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00728"
FT COILED 105..143
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00728"
FT COILED 317..425
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00728"
SQ SEQUENCE 564 AA; 65940 MW; 4176F937D209C22C CRC64;
MAYLIGSILI VIALIITGLI MRKRVYDEVD RLESWKMEIM NRNIASELSR IKGLNLSGET
QEKFESWKAR WERIVTKELP DIEEYLFDAE EAADRFRFPS AKKTLRNVDQ TMQSIEQSIE
DILEELNQLM NSEESSRKEI ERIEPDLKAL RKTLSQNRHQ YGEAEKVFDS ELDELVQQLE
HYHEMVNSGD YTQARNVVEE LKLKLDNLKS TMEEFPAIYQ KSKYDLPQEL NELLSGLREM
KEGGYRIEHL GFEKEVQHHK NKLEECMEYL KSGEISQAKA AVPEIEERIA EMYQLLEKEA
IARNYVEAKI GPYQEALNNM IEKFDVTKEE VETLKESYYL EDSDMEKYFT LEKTLTHLRK
QLEETAEAVE ADNSSAHSDL RLEIENGFNE LETIEEKHEE FKERIRNLRK DELEAKESLQ
NLRNQLYQVN RKLNKSNIPG VPTFLWNKMD EAAGKNSHVM TALEKQPLDM TEVQNALAEA
KTAIDYVIEE TEKILDQAQL TEQVIQYANR YRSQYPELAA KLAEAERLFR SYEYELALEH
AARAVEGIEP GALKHIEQFQ KTAN
//
