ID A0A0A5GQ20_9BACI Unreviewed; 564 AA.
AC A0A0A5GQ20;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 37.
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=N781_09805 {ECO:0000313|EMBL:KGX93343.1};
OS Pontibacillus halophilus JSM 076056 = DSM 19796.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Pontibacillus.
OX NCBI_TaxID=1385510 {ECO:0000313|EMBL:KGX93343.1, ECO:0000313|Proteomes:UP000030528};
RN [1] {ECO:0000313|EMBL:KGX93343.1, ECO:0000313|Proteomes:UP000030528}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JSM 076056 {ECO:0000313|EMBL:KGX93343.1,
RC ECO:0000313|Proteomes:UP000030528};
RA Huang J., Wang G.;
RL Submitted (AUG-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:KGX93343.1}.
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DR EMBL; AVPE01000002; KGX93343.1; -; Genomic_DNA.
DR RefSeq; WP_026801908.1; NZ_KE384328.1.
DR AlphaFoldDB; A0A0A5GQ20; -.
DR STRING; 1385510.GCA_000425205_00872; -.
DR eggNOG; COG4477; Bacteria.
DR OrthoDB; 1654473at2; -.
DR Proteomes; UP000030528; 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:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0000917; P:division septum assembly; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; 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}; Kinase {ECO:0000313|EMBL:KGX93343.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00728};
KW Reference proteome {ECO:0000313|Proteomes:UP000030528};
KW Septation {ECO:0000256|ARBA:ARBA00023210, ECO:0000256|HAMAP-Rule:MF_00728};
KW Transferase {ECO:0000313|EMBL:KGX93343.1};
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 TRANSMEM 6..22
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TOPO_DOM 22..564
FT /note="Cytoplasmic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00728"
FT COILED 253..424
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00728"
SQ SEQUENCE 564 AA; 66991 MW; 19C8C1084B7F141A CRC64;
MEYIIGVIVI VIVGMIVGFI MRKRIYDEVD RLENWKLSIM NREVAEELAK VKSLNLSGQT
QERFEAWRDE WDRILSKQLP ELEEILYDAE EKADKYRFQS AKKVLGQLEQ HLLEIDQSID
NMFQELETLL SSERDGREEM EEILPQIKKL RKQLLQHRHH YGKSEAHFEQ QLNEIAEETN
AFHEHIENGN YLEAHELVQQ LKEQLDAISV QIEEFPKLFR AVKQEYPSQL DELLAGVKEM
TEDDYRIEQF QYEQEITEYK ELLQKDLQKL EQVELKEVRE HLEELDQRIQ DIYAQLEREA
LARSYIEKQQ PILMDKMEET IESAQGTKKE VNILQTTYYL KEKDIETFLG MEQWLKKLLM
QFEDIQNQID GSEELYSSIR EQMEEWETQF DKLVRQHNDY KEFLHTLRKD EWEAKEKIDE
MKQDLVLIHR KLKKSNIPGV PIYLQEVLQH ASNSLEQVAT SLDSEPFNLS EMQEELNQAV
QSVDRAKEQT NLVLDQADFA ETLIQYANRY RSKNPSLAKA LHDSEQAFRQ YDYDRAVQQA
SDALERVEPG AVKRLEELEE VSIV
//
