EZRA_STAAW
ID EZRA_STAAW Reviewed; 564 AA.
AC Q8NW47;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=Septation ring formation regulator EzrA {ECO:0000255|HAMAP-Rule:MF_00728};
GN Name=ezrA {ECO:0000255|HAMAP-Rule:MF_00728}; OrderedLocusNames=MW1660;
OS Staphylococcus aureus (strain MW2).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=196620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MW2;
RX PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT "Genome and virulence determinants of high virulence community-acquired
RT MRSA.";
RL Lancet 359:1819-1827(2002).
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; BA000033; BAB95525.1; -; Genomic_DNA.
DR RefSeq; WP_000244865.1; NC_003923.1.
DR AlphaFoldDB; Q8NW47; -.
DR SMR; Q8NW47; -.
DR EnsemblBacteria; BAB95525; BAB95525; BAB95525.
DR KEGG; sam:MW1660; -.
DR HOGENOM; CLU_034079_1_0_9; -.
DR OMA; FRSQNHI; -.
DR Proteomes; UP000000418; 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_0000172883"
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 99..138
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
FT COILED 190..223
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
FT COILED 271..300
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
FT COILED 350..435
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
FT COILED 471..550
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
SQ SEQUENCE 564 AA; 66200 MW; 4DE5BC982B9E7489 CRC64;
MVLYIILAII VIILIAVGVL FYLRSNKRQI IEKAIERKNE IETLPFDQNL AQLSKLNLKG
ETKTKYDAMK KDNVESTNKY LAPVEEKIHN AEALLDKFSF NASQSEIDDA NELMDSYEQS
YQQQLEDVNE IIALYKDNDE LYDKCKVDYR EMKRDVLANR HQFGEAASLL ETEIEKFEPR
LEQYEVLKAD GNYVQAHNHI AALNEQMKQL RSYMEEIPEL IRETQKELPG QFQDLKYGCR
DLKVEGYDLD HVKVDSTLQS LKTELSFVEP LISRLELEEA NDKLANINDK LDDMYDLIEH
EVKAKNDVEE TKDIITDNLF KAKDMNYTLQ TEIEYVRENY YINESDAQSV RQFENEIQSL
ISVYDDILKE MSKSAVRYSE VQDNLQYLED HVTVINDKQE KLQNHLIQLR EDEAEAEDNL
LRVQSKKEEV YRRLLASNLT SVPERFIIMK NEIDHEVRDV NEQFSERPIH VKQLKDKVSK
IVIQMNTFED EANDVLVNAV YAEKLIQYGN RYRKDYSNVD KSLNEAERLF KNNRYKRAIE
IAEQALESVE PGVTKHIEEE VIKQ