ID A0A060M5D1_9BACI Unreviewed; 565 AA.
AC A0A060M5D1;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 40.
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=BleG1_2744 {ECO:0000313|EMBL:AIC95309.1};
OS Shouchella lehensis G1.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Shouchella.
OX NCBI_TaxID=1246626 {ECO:0000313|EMBL:AIC95309.1, ECO:0000313|Proteomes:UP000027142};
RN [1] {ECO:0000313|EMBL:AIC95309.1, ECO:0000313|Proteomes:UP000027142}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G1 {ECO:0000313|EMBL:AIC95309.1,
RC ECO:0000313|Proteomes:UP000027142};
RX PubMed=24811681; DOI=10.1016/j.gene.2014.05.012;
RA Noor Y.M., Samsulrizal N.H., Jema'on N.A., Low K.O., Ramli A.N.,
RA Alias N.I., Damis S.I., Fuzi S.F., Isa M.N., Murad A.M., Raih M.F.,
RA Bakar F.D., Najimudin N., Mahadi N.M., Illias R.M.;
RT "A comparative genomic analysis of the alkalitolerant soil bacterium
RT Bacillus lehensis G1.";
RL Gene 545:253-261(2014).
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; CP003923; AIC95309.1; -; Genomic_DNA.
DR RefSeq; WP_051667580.1; NZ_CP003923.1.
DR AlphaFoldDB; A0A060M5D1; -.
DR STRING; 1246626.BleG1_2744; -.
DR KEGG; ble:BleG1_2744; -.
DR PATRIC; fig|1246626.3.peg.2736; -.
DR eggNOG; COG4477; Bacteria.
DR HOGENOM; CLU_034079_1_0_9; -.
DR OrthoDB; 1654473at2; -.
DR Proteomes; UP000027142; 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:UP000027142};
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..6
FT /note="Extracellular"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00728"
FT TRANSMEM 6..25
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TOPO_DOM 26..565
FT /note="Cytoplasmic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00728"
FT COILED 272..365
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00728"
FT COILED 391..428
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00728"
SQ SEQUENCE 565 AA; 64981 MW; 0FB051B6FE2F84D5 CRC64;
MDIIVGIVVV LLIVVVIGTV AGMLIRRTIH KSVDELDNRK NQILNRNISE EISKVKKLKM
SGETEQKFES WRKDWDEILE SILPSVEEQL IEVEELAGKY RITKAKDQLK WVENRLLSVE
QQLDLMVEDI DKLVSAEEKN RSEIAVIKEL YQTLSAELLK KRGSFGESIK ALDEEMSHAK
QALLAFEEST QNGSYLQARK QLLQIKDSLY ILNEKMERIP HLLMQVRSTL PGELSNLQLG
IKEMEEDGYH LETFSFGSKI SMQKEEIDQA YIALKELNVD EAASALESLQ TEIDEMYETL
EKEANYKSKL LAQVPALKAQ VEKAYQNMKQ LIDETTQVEK SYMIAEEEIQ LQQTLQKNLR
NVQSQLTLIM DVFENRKQSF SSIFEMTEEW RKQMEELSSG IEESIDRLKR LRKDEIQAQE
TVSQLRELVL ESKRLLYKSN LPGVPVTYLE ALDEAEGNIN RAIEGLESFP LEMTEVEALV
QDAVRVVEGN SAAIKEMVET AQMAELAIQY SNRYRGQDDA VRKELDEAEQ AFLEYDYEKA
LAIVQEAVQR YEPDLLNKVT KHLSA
//
