ID   EZRA_BACSU              Reviewed;         562 AA.
AC   O34894;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 130.
DE   RecName: Full=Septation ring formation regulator EzrA;
GN   Name=ezrA {ECO:0000303|PubMed:10449747}; Synonyms=ytwP;
GN   OrderedLocusNames=BSU29610;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9387221; DOI=10.1099/00221287-143-11-3431;
RA   Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.;
RT   "Sequencing and functional annotation of the Bacillus subtilis genes in the
RT   200 kb rrnB-dnaB region.";
RL   Microbiology 143:3431-3441(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND TOPOLOGY.
RC   STRAIN=168 / JH642;
RX   PubMed=10449747; DOI=10.1073/pnas.96.17.9642;
RA   Levin P.A., Kurtser I.G., Grossman A.D.;
RT   "Identification and characterization of a negative regulator of FtsZ ring
RT   formation in Bacillus subtilis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:9642-9647(1999).
RN   [4]
RP   SUBCELLULAR LOCATION.
RC   STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC   3610 / NRRL NRS-744 / VKM B-501;
RX   PubMed=22882210; DOI=10.1111/j.1365-2958.2012.08205.x;
RA   Yepes A., Schneider J., Mielich B., Koch G., Garcia-Betancur J.C.,
RA   Ramamurthi K.S., Vlamakis H., Lopez D.;
RT   "The biofilm formation defect of a Bacillus subtilis flotillin-defective
RT   mutant involves the protease FtsH.";
RL   Mol. Microbiol. 86:457-471(2012).
RN   [5]
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=168 / PY79;
RX   PubMed=23249255; DOI=10.1186/1471-2180-12-298;
RA   Dempwolff F., Wischhusen H.M., Specht M., Graumann P.L.;
RT   "The deletion of bacterial dynamin and flotillin genes results in
RT   pleiotrophic effects on cell division, cell growth and in cell shape
RT   maintenance.";
RL   BMC Microbiol. 12:298-298(2012).
RN   [6]
RP   SUBCELLULAR LOCATION, AND POSSIBLE DEGRADATION BY FTSH.
RC   STRAIN=168 / PY79;
RX   PubMed=24222488; DOI=10.1128/mbio.00719-13;
RA   Mielich-Suess B., Schneider J., Lopez D.;
RT   "Overproduction of flotillin influences cell differentiation and shape in
RT   Bacillus subtilis.";
RL   MBio 4:0-0(2013).
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.
CC       {ECO:0000269|PubMed:10449747}.
CC   -!- INTERACTION:
CC       O34894; P28264: ftsA; NbExp=5; IntAct=EBI-1567579, EBI-2122615;
CC       O34894; P17865: ftsZ; NbExp=4; IntAct=EBI-1567579, EBI-1569853;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22882210,
CC       ECO:0000269|PubMed:24222488, ECO:0000305|PubMed:10449747}; Single-pass
CC       membrane protein {ECO:0000255}. Membrane raft
CC       {ECO:0000269|PubMed:22882210, ECO:0000269|PubMed:24222488}; Single-pass
CC       membrane protein {ECO:0000255}. Note=Cell membrane associated, also
CC       colocalizes with FtsZ to the nascent septal site (PubMed:10449747).
CC       Present in detergent-resistant membrane (DRM) fractions that may be
CC       equivalent to eukaryotic membrane rafts; these rafts include proteins
CC       involved in signaling, molecule trafficking and protein secretion
CC       (PubMed:22882210, PubMed:24222488). {ECO:0000269|PubMed:10449747,
CC       ECO:0000269|PubMed:22882210, ECO:0000269|PubMed:24222488}.
CC   -!- PTM: May be degraded by FtsH protease. {ECO:0000305|PubMed:24222488}.
CC   -!- DISRUPTION PHENOTYPE: Suppresses temperature-sensitive mutation in
CC       FtsZ, in a wild-type FtsZ background increases the number and alters
CC       the position of FtsZ rings (PubMed:10449747). In minimal medium cells
CC       elongate and occasionally form minicells. Double dynA-ezrA mutants have
CC       longer cells with more double septa than either deletion alone
CC       (PubMed:23249255). {ECO:0000269|PubMed:10449747,
CC       ECO:0000269|PubMed:23249255}.
CC   -!- SIMILARITY: Belongs to the EzrA family. {ECO:0000305}.
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DR   EMBL; AF008220; AAC00306.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14939.1; -; Genomic_DNA.
DR   PIR; G70002; G70002.
DR   RefSeq; NP_390839.1; NC_000964.3.
DR   RefSeq; WP_003229320.1; NZ_JNCM01000036.1.
DR   PDB; 4UXV; X-ray; 3.96 A; A=22-562.
DR   PDBsum; 4UXV; -.
DR   AlphaFoldDB; O34894; -.
DR   SMR; O34894; -.
DR   IntAct; O34894; 10.
DR   STRING; 224308.BSU29610; -.
DR   jPOST; O34894; -.
DR   PaxDb; O34894; -.
DR   PRIDE; O34894; -.
DR   EnsemblBacteria; CAB14939; CAB14939; BSU_29610.
DR   GeneID; 937337; -.
DR   KEGG; bsu:BSU29610; -.
DR   PATRIC; fig|224308.179.peg.3217; -.
DR   eggNOG; COG4477; Bacteria.
DR   InParanoid; O34894; -.
DR   OMA; FRSQNHI; -.
DR   PhylomeDB; O34894; -.
DR   BioCyc; BSUB:BSU29610-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
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:0051781; P:positive regulation of cell division; IMP:CACAO.
DR   GO; GO:0000921; P:septin ring assembly; IMP:CACAO.
DR   HAMAP; MF_00728; EzrA; 1.
DR   InterPro; IPR010379; EzrA.
DR   Pfam; PF06160; EzrA; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell cycle; Cell division; Cell membrane; Coiled coil;
KW   Membrane; Reference proteome; Septation; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..562
FT                   /note="Septation ring formation regulator EzrA"
FT                   /id="PRO_0000172870"
FT   TOPO_DOM        1..2
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3..21
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        22..562
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:10449747"
FT   COILED          109..158
FT                   /evidence="ECO:0000255"
FT   COILED          239..275
FT                   /evidence="ECO:0000255"
FT   COILED          311..340
FT                   /evidence="ECO:0000255"
FT   COILED          376..529
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   562 AA;  64996 MW;  9AD2D58A76A08FDF CRC64;
     MEFVIGLLIV LLALFAAGYF FRKKIYAEID RLESWKIEIL NRSIVEEMSK IKHLKMTGQT
     EEFFEKWREE WDEIVTAHMP KVEELLYDAE ENADKYRFKK ANQVLVHIDD LLTAAESSIE
     KILREISDLV TSEEKSREEI EQVRERYSKS RKNLLAYSHL YGELYDSLEK DLDEIWSGIK
     QFEEETEGGN YITARKVLLE QDRNLERLQS YIDDVPKLLA DCKQTVPGQI AKLKDGYGEM
     KEKGYKLEHI QLDKELENLS NQLKRAEHVL MTELDIDEAS AILQLIDENI QSVYQQLEGE
     VEAGQSVLSK MPELIIAYDK LKEEKEHTKA ETELVKESYR LTAGELGKQQ AFEKRLDEIG
     KLLSSVKDKL DAEHVAYSLL VEEVASIEKQ IEEVKKEHAE YRENLQALRK EELQARETLS
     NLKKTISETA RLLKTSNIPG IPSHIQEMLE NAHHHIQETV NQLNELPLNM EEAGAHLKQA
     EDIVNRASRE SEELVEQVIL IEKIIQFGNR FRSQNHILSE QLKEAERRFY AFDYDDSYEI
     AAAAVEKAAP GAVEKIKADI SA