ID   EZRA_LISMH              Reviewed;         571 AA.
AC   B8DHE7;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 57.
DE   RecName: Full=Septation ring formation regulator EzrA {ECO:0000255|HAMAP-Rule:MF_00728};
GN   Name=ezrA {ECO:0000255|HAMAP-Rule:MF_00728}; OrderedLocusNames=LMHCC_0968;
OS   Listeria monocytogenes serotype 4a (strain HCC23).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=552536;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HCC23;
RX   PubMed=21602330; DOI=10.1128/jb.05236-11;
RA   Steele C.L., Donaldson J.R., Paul D., Banes M.M., Arick T., Bridges S.M.,
RA   Lawrence M.L.;
RT   "Genome sequence of lineage III Listeria monocytogenes strain HCC23.";
RL   J. Bacteriol. 193:3679-3680(2011).
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}.
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DR   EMBL; CP001175; ACK39316.1; -; Genomic_DNA.
DR   RefSeq; WP_003736737.1; NC_011660.1.
DR   AlphaFoldDB; B8DHE7; -.
DR   SMR; B8DHE7; -.
DR   KEGG; lmh:LMHCC_0968; -.
DR   HOGENOM; CLU_034079_2_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   3: Inferred from homology;
KW   Cell cycle; Cell division; Cell membrane; Coiled coil; Membrane; Septation;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..571
FT                   /note="Septation ring formation regulator EzrA"
FT                   /id="PRO_1000148070"
FT   TOPO_DOM        1..3
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
FT   TRANSMEM        4..22
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
FT   TOPO_DOM        23..571
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
FT   COILED          102..147
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
FT   COILED          248..298
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
FT   COILED          326..374
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
FT   COILED          400..437
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
FT   COILED          478..529
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
SQ   SEQUENCE   571 AA;  66477 MW;  87CFAFFED6A30082 CRC64;
     MYYMLIGFII VVIAVIGAGY ILKRKHYQRI NELEEKKIKL RERPVIDELS KVKKLKLTGQ
     TEALFESWRS SWDEIETRLF PDLEEVLLEA EMNTDRYKFR SATNAENDIE QMLVVIEKQM
     DQILGGLKEL LISEEKNAKE SRATKEKFAE LRREVLTRGF KLGETLPYVE AKLNELSESL
     NSYDSLTDQG DHLEAREIVI VVQKEMQVIE AQMERIPSLL HETDTILPEE MNKLRAGYEE
     MVRKGYYLAQ MELDKEISRM KNQIDKMKKN VINLDLDEAE QGVEELHNEI DLFYDTLEHE
     AEARHFVKEN HSPTSDKLQR QNAVSDALAE QITEVKQTYH VAEDDLAVYL KTSAKLSEAK
     ENFEQLTTLI ASGEIAYSAA QDTLKEIDAA LITISAEQDK FAEELRSLRK DELEARDDAE
     RMRRAIITLD RKMERERLPG LPEEYLSLRE HMGESIDTLE KRLEEKPLNM KAVSQDWRIA
     EEDLIHLTEK AEEMMENVRL VEHVIQYANR YRLRNKELAD ELVQAENHFY NDYQYKKALE
     IAVTALEKVE TGAFKKVEKA YASKVSVDDI E