ID EZRA_LISMF Reviewed; 571 AA.
AC Q71Z73;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE RecName: Full=Septation ring formation regulator EzrA {ECO:0000255|HAMAP-Rule:MF_00728};
GN Name=ezrA {ECO:0000255|HAMAP-Rule:MF_00728};
GN OrderedLocusNames=LMOf2365_1616;
OS Listeria monocytogenes serotype 4b (strain F2365).
OC Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=265669;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F2365;
RX PubMed=15115801; DOI=10.1093/nar/gkh562;
RA Nelson K.E., Fouts D.E., Mongodin E.F., Ravel J., DeBoy R.T., Kolonay J.F.,
RA Rasko D.A., Angiuoli S.V., Gill S.R., Paulsen I.T., Peterson J.D.,
RA White O., Nelson W.C., Nierman W.C., Beanan M.J., Brinkac L.M.,
RA Daugherty S.C., Dodson R.J., Durkin A.S., Madupu R., Haft D.H.,
RA Selengut J., Van Aken S.E., Khouri H.M., Fedorova N., Forberger H.A.,
RA Tran B., Kathariou S., Wonderling L.D., Uhlich G.A., Bayles D.O.,
RA Luchansky J.B., Fraser C.M.;
RT "Whole genome comparisons of serotype 4b and 1/2a strains of the food-borne
RT pathogen Listeria monocytogenes reveal new insights into the core genome
RT components of this species.";
RL Nucleic Acids Res. 32:2386-2395(2004).
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; Single-pass membrane protein.
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; AE017262; AAT04391.1; -; Genomic_DNA.
DR RefSeq; WP_003726006.1; NC_002973.6.
DR AlphaFoldDB; Q71Z73; -.
DR SMR; Q71Z73; -.
DR DNASU; 2798773; -.
DR KEGG; lmf:LMOf2365_1616; -.
DR HOGENOM; CLU_034079_2_0_9; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005940; C:septin ring; IEA:InterPro.
DR GO; GO:0000918; P:division septum site selection; ISS:JCVI.
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_0000172875"
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 22..43
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
FT COILED 127..147
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
FT COILED 194..214
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; 66489 MW; 0B479E8B15106AF5 CRC64;
MYYMLIGFII VVIAVIGAGY ILKRKHYQRI NELEEKKIKL RERPVIDELS KVKKLKLTGQ
TEALFESWRS SWDEIETRLF PDLEEVLLEA EMNTDRYKFR SATHAENDIE QMLVVIEKQM
DQILGGLKEL LISEEKNAKE SRATKEKFAE LRREVLTRGF KLGETLPYIE TKLSELSESL
NSYDSLTDQG DHLEAREIVI VVQKEMQVIE AQMERIPSLL HETDTILPEE MTKLRAGYEE
MVRKGYYLAQ MELDKEISRM KNQIDKMKKN VINLDLDEAE QGVEELHNEI DLFYDTLEHE
AEARHFVKEN HSPTSDKLQR QNAVSDALAE QITEVKQTYH VAEDDLAVYL KTSAKLSEAK
ENFEQLTALI ASGEIAYSAA QDTLKEIDAA LITISAEQDK FAEELRSLRK DELEARDDAE
RMRRAIITLD RKMERERLPG LPEEYLSLRE HMGESINALE KRLEEKPLNM KAVSQDWRIA
EEDLTHLTEK AEEMMENVRL VEHVIQYANR YRLRNKELAD ELVQAENHFY NDYQYKKALE
IAVTALEKVE TGAFKKVEKA YESKVSVDDI E
//