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Database: UniProt
Entry: F0FE27_STRSA
LinkDB: F0FE27_STRSA
Original site: F0FE27_STRSA 
ID   F0FE27_STRSA            Unreviewed;       574 AA.
AC   F0FE27;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 50.
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:EGC22862.1};
GN   ORFNames=HMPREF9388_0959 {ECO:0000313|EMBL:EGC22862.1};
OS   Streptococcus sanguinis SK353.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=888815 {ECO:0000313|EMBL:EGC22862.1, ECO:0000313|Proteomes:UP000004185};
RN   [1] {ECO:0000313|EMBL:EGC22862.1, ECO:0000313|Proteomes:UP000004185}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK353 {ECO:0000313|EMBL:EGC22862.1,
RC   ECO:0000313|Proteomes:UP000004185};
RA   Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA   Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA   Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA   Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA   Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA   Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA   Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA   Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA   Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA   Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA   Petrosino J., Highlander S., Gibbs R.;
RL   Submitted (JAN-2011) 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:EGC22862.1}.
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DR   EMBL; AEWY01000004; EGC22862.1; -; Genomic_DNA.
DR   RefSeq; WP_002897820.1; NZ_GL872307.1.
DR   AlphaFoldDB; F0FE27; -.
DR   PATRIC; fig|888815.3.peg.940; -.
DR   HOGENOM; CLU_034079_2_0_9; -.
DR   Proteomes; UP000004185; 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..6
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00728"
FT   TOPO_DOM        27..574
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00728"
FT   COILED          117..183
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00728"
FT   COILED          268..342
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00728"
FT   COILED          381..415
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00728"
SQ   SEQUENCE   574 AA;  65961 MW;  C3EFE12510CBD7F1 CRC64;
     MSIGLVILVA VVALLLVVGY GTAVLMRKRN EALLQNLEER KEALYNLPVN DEVEEVKNMH
     LIGQSQVAFR EWNQKWVDLS LNSFADIENN LFEAEGYNNS FRFIKAKHAI GNIESQIDLI
     EEDIKMIRAA LEDLKEQESK NSGRVLHALD LFEKLQTQVA ENADSYGQAL AEIEKQLENI
     QSEFSQFVTL NSSGDPVEAA EILDKAEDHI LALTHIVEKV PAIVEELTVK LPDQLEDLES
     GHRKLLESGY HFIETDIESR FQQLHASLKR NEANISALEL DNAEYENEQA QEEINALYEI
     FTREIEAHKV VEKLIKNLPS YLAHTKENNQ QLQKEIERLS QTFLLSDTET SHVKELQAEL
     SAQEDVVLSA VEDSSETKQA YSVVQEELEA IQERLKEIED EQISLGEALA EIEKDDANAR
     QKVNIYANKL HTIKRYMEKR NLPGIPDSFL EIFFSTSNNI EELVKELEAT RVNIESVNRW
     LEILGNDMEQ LEEETYRIVQ DATLTEQLLQ YSNRYRSFDD NVQAAFNKSL YVFEHDYDYA
     QSLEIISKAL DLVEPGVTER FVTSYEKTRE NIRF
//
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