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Database: UniProt
Entry: F2I5R4_AERUA
LinkDB: F2I5R4_AERUA
Original site: F2I5R4_AERUA 
ID   F2I5R4_AERUA            Unreviewed;       573 AA.
AC   F2I5R4; A0A9Q4DB35;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 51.
DE   RecName: Full=Septation ring formation regulator EzrA {ECO:0000256|HAMAP-Rule:MF_00728};
GN   Name=ezrA {ECO:0000256|HAMAP-Rule:MF_00728,
GN   ECO:0000313|EMBL:AEA01195.1};
GN   OrderedLocusNames=HMPREF9243_1398 {ECO:0000313|EMBL:AEA01195.1};
GN   ORFNames=ODY48_08140 {ECO:0000313|EMBL:MCY3055699.1};
OS   Aerococcus urinae (strain CCUG 59500 / ACS-120-V-Col10a).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Aerococcaceae; Aerococcus;
OC   Aerococcus incertae sedis.
OX   NCBI_TaxID=2976812 {ECO:0000313|EMBL:AEA01195.1, ECO:0000313|Proteomes:UP000008129};
RN   [1] {ECO:0000313|Proteomes:UP000008129}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACS-120-V-Col10a {ECO:0000313|Proteomes:UP000008129};
RA   Durkin A.S., Madupu R., Radune D., Hostetler J., Torralba M., Gillis M.,
RA   Methe B., Sutton G., Nelson K.E.;
RT   "Complete genome sequence of Aerococcus urinae strain ACS-120-V-Col10a.";
RL   Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AEA01195.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ACS-120-V-Col10a {ECO:0000313|EMBL:AEA01195.1};
RA   Durkin A.S., Madupu R., Radune D., Hostetler J., Torralba M., Gillis M.,
RA   Methe B., Sutton G., Nelson K.E.;
RL   Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:MCY3055699.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CDC-1656-U92 {ECO:0000313|EMBL:MCY3055699.1};
RA   Christensen J., Senneby E.;
RT   "Aerococcus urinae taxonomy study.";
RL   Submitted (SEP-2022) 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}.
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DR   EMBL; CP002512; AEA01195.1; -; Genomic_DNA.
DR   EMBL; JAOTMI010000030; MCY3055699.1; -; Genomic_DNA.
DR   RefSeq; WP_013669430.1; NC_015278.1.
DR   AlphaFoldDB; F2I5R4; -.
DR   STRING; 866775.HMPREF9243_1398; -.
DR   KEGG; aur:HMPREF9243_1398; -.
DR   PATRIC; fig|866775.3.peg.1306; -.
DR   eggNOG; COG4477; Bacteria.
DR   HOGENOM; CLU_034079_2_0_9; -.
DR   OMA; FRSQNHI; -.
DR   Proteomes; UP000008129; Chromosome.
DR   Proteomes; UP001075187; 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:UP000008129};
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   TRANSMEM        6..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TOPO_DOM        25..573
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00728"
FT   COILED          452..500
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00728"
SQ   SEQUENCE   573 AA;  66949 MW;  6AE251047F7B81EB CRC64;
     MGFIIALIII IVIILIGYGL LYYLGRKQSK TNLELDEKKQ EIMAIPVADK LYTIRNKNVS
     GNTRRLFEAE QAKWQTIKQY KLPEIEAALV QAQADADKFS LIKSRKTAEE TEKLIYDTLQ
     DVQNINQSLE ELLASESKNE AYFQEINDRY AKIRKQLLAH GYAYGDSQET LEKHLSYIEL
     DFTKYNTLMS DADYLAAHDV LDQTKEDIEA LEAMMEEIPK LLDKIDNEYE EQLEDLKSGY
     SQMLDMDFQF PSGVRVDEEI QQVEKGIEQC YAALAECDLS ETSSLMSATE AQIDRSYELM
     EVELRAKEYI EKNQGNLEQR INQVRQSNRY GSLEIDRVSQ NYLLHDNELG KLQDYAAQID
     RIHEEVDTVN QRLGAHVIAY TDMQSVYKDK YEQLNEIDKA QSHIVGSLAN LRQKERDARD
     MLYTFDLDMR NMKRRVNQYH LPGLPDAYLD RYFATEDKVE ELERKMNRVK LDMDEIDQLV
     NEVSEAIERL DLETENMIDQ ALLTEQTVQY ANRYRANHPE LNQAIEKSSY YFNQTFDYKK
     AHQTISQAVD QLESGASNKV ENQYRQEKEE RLY
//
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