EZRA_STAAM
ID EZRA_STAAM Reviewed; 564 AA.
AC P64002; Q99TE6;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Septation ring formation regulator EzrA {ECO:0000255|HAMAP-Rule:MF_00728};
GN Name=ezrA {ECO:0000255|HAMAP-Rule:MF_00728}; OrderedLocusNames=SAV1717;
OS Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158878;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mu50 / ATCC 700699;
RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA Hiramatsu K.;
RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL Lancet 357:1225-1240(2001).
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; BA000017; BAB57879.1; -; Genomic_DNA.
DR RefSeq; WP_000244866.1; NC_002758.2.
DR AlphaFoldDB; P64002; -.
DR SMR; P64002; -.
DR PaxDb; P64002; -.
DR EnsemblBacteria; BAB57879; BAB57879; SAV1717.
DR KEGG; sav:SAV1717; -.
DR HOGENOM; CLU_034079_1_0_9; -.
DR OMA; FRSQNHI; -.
DR PhylomeDB; P64002; -.
DR BioCyc; SAUR158878:SAV_RS09215-MON; -.
DR Proteomes; UP000002481; 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_0000172879"
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; 66228 MW; 4DE5BC809CCE7489 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
IAEQVLESVE PGVTKHIEEE VIKQ