ID A8UBL9_9LACT Unreviewed; 573 AA.
AC A8UBL9;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 03-MAY-2023, entry version 66.
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=CAT7_08000 {ECO:0000313|EMBL:EDP67521.1};
OS Carnobacterium sp. AT7.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Carnobacterium.
OX NCBI_TaxID=333990 {ECO:0000313|EMBL:EDP67521.1, ECO:0000313|Proteomes:UP000005587};
RN [1] {ECO:0000313|EMBL:EDP67521.1, ECO:0000313|Proteomes:UP000005587}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AT7 {ECO:0000313|EMBL:EDP67521.1,
RC ECO:0000313|Proteomes:UP000005587};
RA Bartlett D., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (OCT-2007) 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:EDP67521.1}.
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DR EMBL; ABHH01000026; EDP67521.1; -; Genomic_DNA.
DR RefSeq; WP_007724836.1; NZ_ABHH01000026.1.
DR AlphaFoldDB; A8UBL9; -.
DR Proteomes; UP000005587; 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..5
FT /note="Extracellular"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00728"
FT TOPO_DOM 25..573
FT /note="Cytoplasmic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00728"
FT COILED 115..188
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00728"
FT COILED 394..421
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00728"
FT COILED 459..486
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00728"
SQ SEQUENCE 573 AA; 66649 MW; 6E2C17E03A61A25B CRC64;
MKMEIILISI IVIAVAAYVT SYFMKKKHYQ TINKLEQQKF ELMDTSVAET IQNVKNLSLT
GQTEKNFEQW KDKWKQIELT AFPDIENLLF DAEQATDRLQ LVKASKAETK SSELIENTKK
KIKEIQLALN ELLKSEEKNN QAIKKVQEMY QGIRKKLLTQ SFSFGPALDK LENRLTFLEL
SFANFSELTT SGDHIEAEEV LKKVSIETKD LNDAVVTIPN LVKEVNTEFP SQVQELKEGY
HELKDVQHFI FLEDTLTADI AEIEQDVKQS GKLIKQCEIE KVEKLNSIIE EKINHLYDVM
EAEITAKEMV AKEQPILAEF ITFVNKRNQQ LLIEIDRVSQ SYTLDDTVLK QTKDMQEQIE
EVQLDFETFM SGIEKNQAVY TVVADSYAES GEKLTQIEKK QEALINQLTD LRKEETEVKE
KIDDFEFNMR GIKRYIEKQH LPGLPEEYLD LFFVTTERIE KLAKELNKLK IDMTEIKNMC
EMCEDDVELL IDKTEEIVDS ALLTEYMMQY ANRYRNDHPQ IGEAILESND LFNKEFQYKE
SLEVISTALE AIEPGSFKKV ETQYFEEKAR NAK
//
