ID   EZRA_STAA1              Reviewed;         564 AA.
AC   A7X3E7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=Septation ring formation regulator EzrA {ECO:0000255|HAMAP-Rule:MF_00728};
GN   Name=ezrA {ECO:0000255|HAMAP-Rule:MF_00728}; OrderedLocusNames=SAHV_1703;
OS   Staphylococcus aureus (strain Mu3 / ATCC 700698).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=418127;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mu3 / ATCC 700698;
RX   PubMed=17954695; DOI=10.1128/aac.00534-07;
RA   Neoh H.-M., Cui L., Yuzawa H., Takeuchi F., Matsuo M., Hiramatsu K.;
RT   "Mutated response regulator graR is responsible for phenotypic conversion
RT   of Staphylococcus aureus from heterogeneous vancomycin-intermediate
RT   resistance to vancomycin-intermediate resistance.";
RL   Antimicrob. Agents Chemother. 52:45-53(2008).
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 {ECO:0000255|HAMAP-Rule:MF_00728};
CC       Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00728}.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AP009324; BAF78586.1; -; Genomic_DNA.
DR   RefSeq; WP_000244866.1; NC_009782.1.
DR   PDB; 4UY3; X-ray; 2.60 A; A=24-214.
DR   PDBsum; 4UY3; -.
DR   AlphaFoldDB; A7X3E7; -.
DR   SMR; A7X3E7; -.
DR   KEGG; saw:SAHV_1703; -.
DR   HOGENOM; CLU_034079_1_0_9; -.
DR   OMA; FRSQNHI; -.
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   1: Evidence at protein level;
KW   3D-structure; Cell cycle; Cell division; Cell membrane; Coiled coil;
KW   Membrane; Septation; Transmembrane; Transmembrane helix.
FT   CHAIN           1..564
FT                   /note="Septation ring formation regulator EzrA"
FT                   /id="PRO_1000045901"
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"
FT   HELIX           24..41
FT                   /evidence="ECO:0007829|PDB:4UY3"
FT   HELIX           46..54
FT                   /evidence="ECO:0007829|PDB:4UY3"
FT   HELIX           60..80
FT                   /evidence="ECO:0007829|PDB:4UY3"
FT   TURN            81..83
FT                   /evidence="ECO:0007829|PDB:4UY3"
FT   HELIX           84..96
FT                   /evidence="ECO:0007829|PDB:4UY3"
FT   HELIX           100..158
FT                   /evidence="ECO:0007829|PDB:4UY3"
FT   HELIX           161..166
FT                   /evidence="ECO:0007829|PDB:4UY3"
FT   HELIX           167..175
FT                   /evidence="ECO:0007829|PDB:4UY3"
FT   HELIX           177..189
FT                   /evidence="ECO:0007829|PDB:4UY3"
FT   HELIX           193..213
FT                   /evidence="ECO:0007829|PDB:4UY3"
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