ID   EZRA_STRPJ              Reviewed;         575 AA.
AC   B8ZNG7;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 62.
DE   RecName: Full=Septation ring formation regulator EzrA {ECO:0000255|HAMAP-Rule:MF_00728};
GN   Name=ezrA {ECO:0000255|HAMAP-Rule:MF_00728}; OrderedLocusNames=SPN23F07360;
OS   Streptococcus pneumoniae (strain ATCC 700669 / Spain 23F-1).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=561276;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700669 / Spain 23F-1;
RX   PubMed=19114491; DOI=10.1128/jb.01343-08;
RA   Croucher N.J., Walker D., Romero P., Lennard N., Paterson G.K., Bason N.C.,
RA   Mitchell A.M., Quail M.A., Andrew P.W., Parkhill J., Bentley S.D.,
RA   Mitchell T.J.;
RT   "Role of conjugative elements in the evolution of the multidrug-resistant
RT   pandemic clone Streptococcus pneumoniae Spain23F ST81.";
RL   J. Bacteriol. 191:1480-1489(2009).
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; FM211187; CAR68580.1; -; Genomic_DNA.
DR   RefSeq; WP_000064817.1; NC_011900.1.
DR   AlphaFoldDB; B8ZNG7; -.
DR   SMR; B8ZNG7; -.
DR   KEGG; sne:SPN23F07360; -.
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..575
FT                   /note="Septation ring formation regulator EzrA"
FT                   /id="PRO_1000148073"
FT   TOPO_DOM        1..8
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
FT   TRANSMEM        9..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
FT   TOPO_DOM        28..575
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
FT   COILED          110..191
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
FT   COILED          265..301
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
FT   COILED          354..416
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
FT   COILED          456..526
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
SQ   SEQUENCE   575 AA;  66522 MW;  05017F59636D6E5C CRC64;
     MSNGQLIYLM VAIAVILVLA YVVAIFLRKR NEGRLEALEE RKEELYNLPV NDEVEAVKNM
     HLIGQSQVAF REWNQKWVDL SLNSFADIEN NLFEAEGYNH SFRFLKASHQ IDQIESQITL
     IDEDIAAIRN ALADLEKQES KNSGRVLHAL DLFEELQHRV AENSEQYGQA LDEIEKQLEN
     IQSEFSQFVT LNSSGDPVEA AVILDNTENH ILALSHIVDR VPALVTTLST ELPDQLQDLE
     SGYRKLIDAN YHFVETDIEA RFHLLYEAFK KNQENIRQLE LDNAEYENGQ AQEEINALYD
     IFTREIAAQK VVENLLATLP TYLQHMKENN TLLGEDIARL NKTYLLPETA ASHVRRIQTE
     LESFEAAIVE VTSNQEEPTQ AYSVLEENLE DLQTQLKDIE DEQISVSERL TQIEKDDINA
     RQKANVYVNR LHTIKRYMEK RNLPGIPQTF LKLFFTASNN TEDLMVELEQ KMINIESVTR
     VLEIATNDME ALETETYNIV QYATLTEQLL QYSNRYRSFD ERIQEAFNEA LDIFEKEFDY
     HASFDKISQA LEVAEPGVTN RFVTSYEKTR ETIRF