EZRA_LISW6
ID EZRA_LISW6 Reviewed; 571 AA.
AC A0AJ43;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 1.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=Septation ring formation regulator EzrA {ECO:0000255|HAMAP-Rule:MF_00728};
GN Name=ezrA {ECO:0000255|HAMAP-Rule:MF_00728}; OrderedLocusNames=lwe1607;
OS Listeria welshimeri serovar 6b (strain ATCC 35897 / DSM 20650 / CIP 8149 /
OS NCTC 11857 / SLCC 5334 / V8).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=386043;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35897 / DSM 20650 / CIP 8149 / NCTC 11857 / SLCC 5334 / V8;
RX PubMed=16936040; DOI=10.1128/jb.00758-06;
RA Hain T., Steinweg C., Kuenne C.T., Billion A., Ghai R., Chatterjee S.S.,
RA Domann E., Kaerst U., Goesmann A., Bekel T., Bartels D., Kaiser O.,
RA Meyer F., Puehler A., Weisshaar B., Wehland J., Liang C., Dandekar T.,
RA Lampidis R., Kreft J., Goebel W., Chakraborty T.;
RT "Whole-genome sequence of Listeria welshimeri reveals common steps in
RT genome reduction with Listeria innocua as compared to Listeria
RT monocytogenes.";
RL J. Bacteriol. 188:7405-7415(2006).
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; AM263198; CAK21025.1; -; Genomic_DNA.
DR RefSeq; WP_011702392.1; NC_008555.1.
DR AlphaFoldDB; A0AJ43; -.
DR SMR; A0AJ43; -.
DR STRING; 386043.lwe1607; -.
DR EnsemblBacteria; CAK21025; CAK21025; lwe1607.
DR GeneID; 61189484; -.
DR KEGG; lwe:lwe1607; -.
DR eggNOG; COG4477; Bacteria.
DR HOGENOM; CLU_034079_2_0_9; -.
DR OMA; FRSQNHI; -.
DR OrthoDB; 670472at2; -.
DR Proteomes; UP000000779; Chromosome.
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..571
FT /note="Septation ring formation regulator EzrA"
FT /id="PRO_1000045900"
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 169..214
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
FT COILED 249..298
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
FT COILED 326..374
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
FT COILED 400..438
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
FT COILED 474..529
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00728"
SQ SEQUENCE 571 AA; 66796 MW; 35B814BFD8981305 CRC64;
MYYMLIGFII VVIAIISAGY ILKRKHYQRI NELEETKIKL RERPVIDELS KVKKLKLTGQ
TEALFESWRS SWDEIETRLF PDLEEVLLEA EMNTDRYKFR SATYVENDIE QMLVVIEKQM
DQILGGLKEL LISEEKNAKE SRMTKEKFAE LRREVLTRGF KLGDTLPYVE TKLDELAENL
NRYDLLTDQG DHLEAREIVL IVQKEMKVIE AQMERIPSLL HETDTILPEE MNKLRAGYEE
MVRKGYYLAQ MELDKEITRM KTQIDKMKRN VINLDLDEAE QGIEELHNEI DLFYDTLEHE
AEARHFVKEN HSPTSDKLQR QNTVSDALAE QITEVKQTYH VAEDDLAVYL KTSAKLSEAK
ENFEQLTALI ASGEIAYSAA QDTLKEIDAA LISIGAEQDK FAEELRSLRK DELEARDDAE
RMRRAIVTLD RKMERERLPG LPEEYLSLRE HMGESIDALE KRLEEKPLNM KAVTQDWRIA
EEDLNHLTEK AEEMMENVRL VEHVIQYANR YRLRNKELAD ELVQAENHFY NDYQYKKALE
IAVTALEKVE TGAFKKVEKA YESKVSVDDI E