ID W1Q6N7_ABIDE Unreviewed; 558 AA.
AC W1Q6N7;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, 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 ORFNames=GCWU000182_000300 {ECO:0000313|EMBL:ESK66609.1};
OS Abiotrophia defectiva ATCC 49176.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Aerococcaceae; Abiotrophia.
OX NCBI_TaxID=592010 {ECO:0000313|EMBL:ESK66609.1, ECO:0000313|Proteomes:UP000019050};
RN [1] {ECO:0000313|EMBL:ESK66609.1, ECO:0000313|Proteomes:UP000019050}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49176 {ECO:0000313|EMBL:ESK66609.1,
RC ECO:0000313|Proteomes:UP000019050};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (JUN-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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ESK66609.1}.
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DR EMBL; ACIN03000001; ESK66609.1; -; Genomic_DNA.
DR AlphaFoldDB; W1Q6N7; -.
DR STRING; 592010.GCWU000182_000300; -.
DR eggNOG; COG4477; Bacteria.
DR HOGENOM; CLU_034079_2_0_9; -.
DR Proteomes; UP000019050; 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 Reference proteome {ECO:0000313|Proteomes:UP000019050};
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 11..558
FT /note="Cytoplasmic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00728"
FT COILED 238..312
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00728"
FT COILED 365..420
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00728"
FT COILED 444..481
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00728"
SQ SEQUENCE 558 AA; 65724 MW; F5AD3D97088B7A2B CRC64;
MLGYFAYYFY RNKNTQSIRE LEARKEEMMA IPIANQLFLL KNMSLSGQTK RKYESLVNQW
QSITNFQFVE IESALVGAQQ YADQLNFMRT GRTIAQARQL IDETMVKVQD LHQDLSDLLQ
VEVDNNELNA ALHERYNAAR KNVMNHSFDY GPAIETLEKN LQYLELNFTK YNEYTENGDH
LEARDMLKTI DADMTSLEDI LERIPSMYDK IKNEYEDSLD DLREGYQKMV DSRFDFDGVA
ILEKVDEIQE KLNDAKNEIK NADLSEAKTL MDKAERDIKS LYDLMETEIE AKDYVNKNIQ
SLRRKIDEVA ENGRYAGIEV DRIAQSYILH ENEVDQIADL SDQIRHEYNR FKDLVAETEG
SAVVYTQAEG RIKKIRKRIE EIDEQVLAIT NKIAQLNTRE KDAKTNLDDY ELALRNIKRR
IEKSHLPGLS DSFYDQFYRV TDQIEHLAKQ LNRVRIDMDE IESLEDELER HLAALEEMTE
SVVDSAMLTE YMIQQSNRFR YDYPEVDAAI KEAQYLFHRE FKYQEALAVI EKSLRRVDQE
APTQVRRMYH QEKRSSQF
//
