ID A0A268E0G8_9BACI Unreviewed; 563 AA.
AC A0A268E0G8;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
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=CHH83_23175 {ECO:0000313|EMBL:PAD66601.1};
OS Bacillus sp. 7586-K.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=2021690 {ECO:0000313|EMBL:PAD66601.1, ECO:0000313|Proteomes:UP000216230};
RN [1] {ECO:0000313|EMBL:PAD66601.1, ECO:0000313|Proteomes:UP000216230}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=7586-K {ECO:0000313|EMBL:PAD66601.1,
RC ECO:0000313|Proteomes:UP000216230};
RA Kalinowski J., Ahrens B., Al-Dilaimi A., Winkler A., Wibberg D.,
RA Schleenbecker U., Ruckert C., Wolfel R., Grass G.;
RT "Isolation and whole genome analysis of endospore-forming bacteria from
RT heroin.";
RL Submitted (JUL-2017) 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:PAD66601.1}.
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DR EMBL; NPCL01000131; PAD66601.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A268E0G8; -.
DR OrthoDB; 1654473at2; -.
DR Proteomes; UP000216230; 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:UP000216230};
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..563
FT /note="Cytoplasmic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00728"
FT COILED 249..276
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00728"
FT COILED 376..424
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00728"
SQ SEQUENCE 563 AA; 65813 MW; 242FF084A00855A8 CRC64;
MEVIIGLILL LCILFGVGYI LRRNIYKDVD RLEAWKIEIM NRSIIDELSK VKELKMIGQA
EELFEQWRSE WDEIITTQLP EVEELLYEAE ELADKYRFKK SKEVLQHIEN VLITVDENID
KIIEEINELV TSEEKNKVES EEVKELYKKL RKTLLAHSHQ FGKAYDKLDQ ILSGISDSLK
EFDSETNEGN YLSARKILVG LKSELNALQI KVNEIPKLLT DCNITKPNLL SELEDGYKEM
VGNGYFLEHI QVVQEIERMK KQLEGFRKQI EETEIEEVAE ALQGMQIAID SIYDLLEKEV
EASQFVKQKK STIDEKLTKL TEQKMATLEE TELVKQSYRL SENEVDKQKL IEKQISQIEK
KFAHIKQSLD SDHVAHSIMK EELEEIEKQI NKLFEEHNEY REMLQTLRKD ELEARERLNH
LKQILLETIR NVQQSNIPGL PEDFVKLIDK AKREVQKVTE KLEEIPLNMT TVNKLLEETV
QTVEEFKNTA EELIEQVFLV EQVIQYGNRY RSRNKQLSSS FSEAEMLFRN SEYGKSLEMA
ASALEQVEPG ALKKIKILIN DQT
//
