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Database: UniProt
Entry: D4YRW3_9LACO
LinkDB: D4YRW3_9LACO
Original site: D4YRW3_9LACO 
ID   D4YRW3_9LACO            Unreviewed;       620 AA.
AC   D4YRW3;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   24-JAN-2024, entry version 52.
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:EFG56057.1};
GN   ORFNames=HMPREF0493_0241 {ECO:0000313|EMBL:EFG56057.1};
OS   Lactobacillus amylolyticus DSM 11664.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=585524 {ECO:0000313|EMBL:EFG56057.1, ECO:0000313|Proteomes:UP000004069};
RN   [1] {ECO:0000313|EMBL:EFG56057.1, ECO:0000313|Proteomes:UP000004069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11664 {ECO:0000313|EMBL:EFG56057.1,
RC   ECO:0000313|Proteomes:UP000004069};
RA   Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA   Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA   Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA   Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA   Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA   Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA   Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA   Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA   Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA   Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA   Petrosino J., Highlander S., Gibbs R.;
RL   Submitted (APR-2010) 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:EFG56057.1}.
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DR   EMBL; ADNY01000011; EFG56057.1; -; Genomic_DNA.
DR   AlphaFoldDB; D4YRW3; -.
DR   STRING; 83683.B1745_04180; -.
DR   eggNOG; COG4477; Bacteria.
DR   Proteomes; UP000004069; 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   Reference proteome {ECO:0000313|Proteomes:UP000004069};
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..56
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00728"
FT   TRANSMEM        56..74
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TOPO_DOM        76..620
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00728"
FT   COILED          219..279
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00728"
FT   COILED          310..349
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00728"
FT   COILED          523..550
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00728"
SQ   SEQUENCE   620 AA;  72108 MW;  C226110EE4BFE04C CRC64;
     MLTFLSLIAA NILHEYYYKR QIRINQEKAR FYPVFSVFWY NYGSFGGYTM SSVQTLIIIA
     IIILIILIVG FIIIQNRKHL HEIEAIDNSV DKIAKMHLER DIKRLDKMDL AGESLTTLNT
     WRKCYQDAAT SKIPEVQHLL ELAADENASY HLFKARKNIK KAQEIINSTL DDMKNTHDVF
     NDLLESNREN QLQYDALIKT YRSMRKNILA DSFNYGSALN QLENKLSSME SDFDEAKNLS
     SQGDHVEAKR VLTKIKVALN ELKEQLPKIK EAEHQLETVF QDQLSELSDA YKKMISEKFY
     INKVNVLDEI KKIHEEIDSA RNLLAGLKID ELDKENKKIA SQIDDLYNVL ATEYKARPFV
     EENQSKMFTL ISHQQIASKK LVEKLRHIDE SYELTHGELD ESKHLEQEVN DMNRQYTVDT
     QNIADGKGVY SEIQNSWLAM LDRLRQIDAE QKQMSQDVDG LYDSENVAND SIKHFKQEVS
     LVYRRLQRRK LPGNPDSFVQ MYTLVVNEIG HVSEQLSEVR INMEKISNEL IQISDDVERL
     KREADDIINS ANLVELTMQY SNKYSDRDAI QKAQDKAMKL YQRNYDYKNA LDTIATALEK
     AEPGAYQRLE NSYYSEKNNK
//
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