EZRA_STAES
ID EZRA_STAES Reviewed; 564 AA.
AC Q8CNW5;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=Septation ring formation regulator EzrA {ECO:0000255|HAMAP-Rule:MF_00728};
GN Name=ezrA {ECO:0000255|HAMAP-Rule:MF_00728}; OrderedLocusNames=SE_1393;
OS Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176280;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12228 / FDA PCI 1200;
RX PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT "Genome-based analysis of virulence genes in a non-biofilm-forming
RT Staphylococcus epidermidis strain (ATCC 12228).";
RL Mol. Microbiol. 49:1577-1593(2003).
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:0000255|HAMAP-
CC Rule:MF_00728}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein.
CC Note=Colocalized with FtsZ to the nascent septal site.
CC {ECO:0000255|HAMAP-Rule:MF_00728}.
CC -!- SIMILARITY: Belongs to the EzrA family. {ECO:0000255|HAMAP-
CC Rule:MF_00728}.
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DR EMBL; AE015929; AAO04992.1; -; Genomic_DNA.
DR RefSeq; NP_764948.1; NC_004461.1.
DR RefSeq; WP_001830796.1; NZ_WBME01000070.1.
DR AlphaFoldDB; Q8CNW5; -.
DR SMR; Q8CNW5; -.
DR STRING; 176280.SE_1393; -.
DR EnsemblBacteria; AAO04992; AAO04992; SE_1393.
DR KEGG; sep:SE_1393; -.
DR PATRIC; fig|176280.10.peg.1361; -.
DR eggNOG; COG4477; Bacteria.
DR HOGENOM; CLU_034079_1_0_9; -.
DR OMA; FRSQNHI; -.
DR Proteomes; UP000001411; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; Cell division; Cell membrane; Coiled coil; Membrane; Septation;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..564
FT /note="Septation ring formation regulator EzrA"
FT /id="PRO_0000172884"
FT TOPO_DOM 1..4
FT /note="Extracellular"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
FT TRANSMEM 5..23
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
FT TOPO_DOM 24..564
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
FT COILED 84..126
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
FT COILED 165..223
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
FT COILED 271..303
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
FT COILED 350..435
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
SQ SEQUENCE 564 AA; 66526 MW; 3DDA97647430452A CRC64;
MVLFIILAIL VVILIAIGVL FYMRSNKRNL IEKTEERKNE IEQLPLDDNL RKLTGLNLKG
ETKTKYDAMK KDNTETTNKY LAPVEEKIQN AEELLEKFKF TAAQTEIDDA HELMDQYEEN
YQHQVTQVDD IINLHKENEA LYEKCKVDYR EMKRDVLANR HQFGEAAEPL ENEIENYEPK
LNEYENLKSE GNYVQAHNHI AALEDQIKNL KSYMDEIPEL IRETQKELPG QFQDLKYGCR
DLKVEGYDLD HVKVDGTIQS LKTELSFVEP MISRLELDEA NNKLENINDK LDEMYDLIEY
EVKAKNEVEE TKDIITDDLF KAKDMNYTLQ TEIEYVRENY YINESDAQSV RQFENEIQSL
ISVYDDILKE TSKSAVRYSE VQDNLQYLED HVSVINKEQD KLQNHLIQLR EDEAEAEDNL
LRVQSKKEEV YRRLLASNLT SVPERFIIMK NEIDNEVREV NEQFRERPIH VKQLKDKVAK
IVIQMNTFED EANDVLVNAV YAEKLIQYGN RYRKDHHHVD KSLNEAERLF KNNRYKRAIE
IAEEALESVE PGITKHIEEQ VIKE