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Database: UniProt
Entry: I2J062_9STRE
LinkDB: I2J062_9STRE
Original site: I2J062_9STRE 
ID   I2J062_9STRE            Unreviewed;       575 AA.
AC   I2J062;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   24-JAN-2024, entry version 48.
DE   RecName: Full=Septation ring formation regulator EzrA {ECO:0000256|HAMAP-Rule:MF_00728};
GN   Name=ezrA {ECO:0000256|HAMAP-Rule:MF_00728,
GN   ECO:0000313|EMBL:EIF36364.1};
GN   ORFNames=HMPREF1116_0028 {ECO:0000313|EMBL:EIF36364.1};
OS   Streptococcus sp. SK140.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1095726 {ECO:0000313|EMBL:EIF36364.1, ECO:0000313|Proteomes:UP000003237};
RN   [1] {ECO:0000313|EMBL:EIF36364.1, ECO:0000313|Proteomes:UP000003237}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK140 {ECO:0000313|EMBL:EIF36364.1,
RC   ECO:0000313|Proteomes:UP000003237};
RA   Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., Sutton G.,
RA   Nelson K.E.;
RL   Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-
CC       Rule:MF_00728}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00728};
CC       Single-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_00728}.
CC       Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004167}. Note=Colocalized with FtsZ to the
CC       nascent septal site. {ECO:0000256|HAMAP-Rule:MF_00728}.
CC   -!- SIMILARITY: Belongs to the EzrA family. {ECO:0000256|HAMAP-
CC       Rule:MF_00728}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EIF36364.1}.
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DR   EMBL; AJML01000040; EIF36364.1; -; Genomic_DNA.
DR   RefSeq; WP_001282633.1; NZ_AJML01000040.1.
DR   AlphaFoldDB; I2J062; -.
DR   PATRIC; fig|1095726.3.peg.1620; -.
DR   eggNOG; COG4477; Bacteria.
DR   Proteomes; UP000003237; Unassembled WGS sequence.
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 {ECO:0000256|HAMAP-Rule:MF_00728};
KW   Cell division {ECO:0000256|HAMAP-Rule:MF_00728};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_00728};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|HAMAP-
KW   Rule:MF_00728};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00728};
KW   Septation {ECO:0000256|ARBA:ARBA00023210, ECO:0000256|HAMAP-Rule:MF_00728};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW   Rule:MF_00728};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW   Rule:MF_00728}.
FT   TOPO_DOM        1..8
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00728"
FT   TRANSMEM        6..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TOPO_DOM        28..575
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00728"
FT   COILED          111..138
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00728"
FT   COILED          262..416
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00728"
SQ   SEQUENCE   575 AA;  66410 MW;  D57122DE121E25B4 CRC64;
     MSDNLLIITM IAIAALLIIA YVVAVLLRKR NEKRLAVLEE RKEELYNLPV NDEVEAVKNM
     HLIGQSQIAF REWNQKWVDL SLNSFADIEN NLFEAEGYNN SFRFLKAQHK IDQIESQITL
     IEEDIASIRN ALADLEKQES KNSGRVLHAL DLFESLQKSV VEDSEKYGQA LLEIEKQIEN
     IQSEFSQFVT LNSSGDPVEA AGILDNAENH ILALTHIVER IPAIVTKLTT ELPDQLEDLE
     AGYRKLLDAN YHFVETDIES RLQLLYEALK NNQENIKKLE LDNAEYENNQ IQEEINALYN
     IFTREIASQK VVENLLSTLP TYLDHLKDNN QVLVKDIERL SKTYLMAESD VNHVRRLQVD
     LDSLELTVSD LTSEQEEYSE AYSVLEERLE NVQATLKEIE DDQVSVSERL VQIEKDDVNA
     RQKANVYVNR LHTIKRYMEK RNLPGIPQNF LKLFFAASHS TEDLMAELEQ SQVNIESVNR
     ILEIASHDME VLETETYSIV QYATLTEQLL QYSNRYRSFD EGIQQAFHES LEIFENAFDY
     QASFEKISQA LEVAEPGVTN RFVSSYEKTR EIIRF
//
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