ID   EZRA_STRZT              Reviewed;         575 AA.
AC   C1CS76;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   25-MAY-2022, entry version 61.
DE   RecName: Full=Septation ring formation regulator EzrA {ECO:0000255|HAMAP-Rule:MF_00728};
GN   Name=ezrA {ECO:0000255|HAMAP-Rule:MF_00728}; OrderedLocusNames=SPT_1392;
OS   Streptococcus pneumoniae (strain Taiwan19F-14).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=487213;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Taiwan19F-14;
RX   PubMed=21034474; DOI=10.1186/gb-2010-11-10-r107;
RA   Donati C., Hiller N.L., Tettelin H., Muzzi A., Croucher N.J.,
RA   Angiuoli S.V., Oggioni M., Dunning Hotopp J.C., Hu F.Z., Riley D.R.,
RA   Covacci A., Mitchell T.J., Bentley S.D., Kilian M., Ehrlich G.D.,
RA   Rappuoli R., Moxon E.R., Masignani V.;
RT   "Structure and dynamics of the pan-genome of Streptococcus pneumoniae and
RT   closely related species.";
RL   Genome Biol. 11:R107.1-R107.19(2010).
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; CP000921; ACO23080.1; -; Genomic_DNA.
DR   RefSeq; WP_000064821.1; NC_012469.1.
DR   AlphaFoldDB; C1CS76; -.
DR   SMR; C1CS76; -.
DR   GeneID; 60233380; -.
DR   GeneID; 66805953; -.
DR   KEGG; snt:SPT_1392; -.
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_1000148077"
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          105..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;  66520 MW;  34B838FD0B5D5DD5 CRC64;
     MSNGQLIYLM VAIAVILVLA YVVAIFLRKR NEGRLEALEE RKEELYNLPV NDEVEAVKNM
     HLIGQSQVAF REWNQKWVDL SLNSFADIEN NLFEAEGYNH SFRFLKASHQ IDQIESQITL
     IEEDIAAIRN ALADLEKQES KNSGRVLHAL DLFEELQHRV AENSEQYGQA LDEIEKQLEN
     IQSEFSQFVT LNSSGDPVEA AVILDNTENH ILALSHIVDR VPALVTTLST ELPDQLQDLE
     AGYRKLIDAN 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