DYNA_BACSU
ID DYNA_BACSU Reviewed; 1193 AA.
AC P54159;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Dynamin-like protein A {ECO:0000303|PubMed:21205012};
DE Short=DynA {ECO:0000303|PubMed:21205012};
GN Name=dynA {ECO:0000303|PubMed:21205012}; Synonyms=ypbR;
GN OrderedLocusNames=BSU22030;
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 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=8969496; DOI=10.1099/13500872-142-11-3005;
RA Capuano V., Galleron N., Pujic P., Sorokin A., Ehrlich S.D.;
RT "Organization of the Bacillus subtilis 168 chromosome between kdg and the
RT attachment site of the SP beta prophage: use of long accurate PCR and yeast
RT artificial chromosomes for sequencing.";
RL Microbiology 142:3005-3015(1996).
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, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION,
RP DOMAIN, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF LYS-65 AND LYS-625.
RC STRAIN=168;
RX PubMed=21205012; DOI=10.1111/j.1365-2958.2011.07523.x;
RA Buermann F., Ebert N., van Baarle S., Bramkamp M.;
RT "A bacterial dynamin-like protein mediating nucleotide-independent membrane
RT fusion.";
RL Mol. Microbiol. 79:1294-1304(2011).
RN [4]
RP INTERACTION WITH RNY; YNEK AND YWPG, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=168;
RX PubMed=23060960; DOI=10.4161/cib.20215;
RA Buermann F., Sawant P., Bramkamp M.;
RT "Identification of interaction partners of the dynamin-like protein DynA
RT from Bacillus subtilis.";
RL Commun. Integr. Biol. 5:362-369(2012).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND 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 DISRUPTION PHENOTYPE.
RC STRAIN=168 / PY79;
RX PubMed=26842743; DOI=10.4161/cib.29578;
RA Dempwolff F., Graumann P.L.;
RT "Genetic links between bacterial dynamin and flotillin proteins.";
RL Commun. Integr. Biol. 7:0-0(2014).
RN [7]
RP LIPID-BINDING.
RC STRAIN=168;
RX PubMed=25635948; DOI=10.1371/journal.pone.0116750;
RA Bach J.N., Bramkamp M.;
RT "Dissecting the molecular properties of prokaryotic flotillins.";
RL PLoS ONE 10:e0116750-e0116750(2015).
RN [8]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=168 / PSB025 / 25152;
RX PubMed=26530236; DOI=10.1111/1462-2920.13110;
RA Sawant P., Eissenberger K., Karier L., Mascher T., Bramkamp M.;
RT "A dynamin-like protein involved in bacterial cell membrane surveillance
RT under environmental stress.";
RL Environ. Microbiol. 18:2705-2720(2016).
RN [9]
RP FUNCTION, DOMAIN, AND MUTAGENESIS OF LYS-56 AND LYS-625.
RC STRAIN=168;
RX PubMed=31361971; DOI=10.1096/fj.201900844rr;
RA Guo L., Bramkamp M.;
RT "Bacterial dynamin-like protein DynA mediates lipid and content mixing.";
RL FASEB J. 33:11746-11757(2019).
CC -!- FUNCTION: Mediates lipid mixing of vesicles and full mixing of their
CC contents in the absence and presence of GTP. Tethers and mixes small
CC vesicles better than larger ones, indicating a curvature preference.
CC GTP slows down DynA-mediated lipid fusion, perhaps controlling its
CC activity. Prefers phospholipid composition close to the B.subtilis
CC membrane; requires phosphatidylglycerol for fusion has no activity on
CC pure phosphatidylethanolamine vesicles (PubMed:31361971). Regulates
CC membrane lipid diffusion. Required to prevent membrane damage when
CC exposed to low levels of membrane-damaging antibiotics or to
CC bacteriophage. Probably surveys the cell membrane for stress; localizes
CC to sites of membrane damage (treatment with nisin) and forms foci in
CC cells treated with pore-forming compounds (CCCP). May assist membrane
CC repair, possibly by membrane tethering and fusion (PubMed:26530236).
CC Probably functions both in early and late cell division, affects the
CC proper formation of the FtsZ ring. Plays a non-redundant role with
CC flottilin (floT) in membrane dynamics and cell shape. Probably able to
CC bend membranes (PubMed:23249255). Tethers liposomes and mediates their
CC fusion; this does not require GTPase activity or the presence of GTP.
CC Both GTPase domains (dynamin-type G) are required for GTPase activity
CC (PubMed:21205012). {ECO:0000269|PubMed:21205012,
CC ECO:0000269|PubMed:23249255, ECO:0000269|PubMed:26530236,
CC ECO:0000269|PubMed:31361971}.
CC -!- FUNCTION: Has intrinsic affinity for membranes and membrane distortion
CC capability; causes tubulation and membrane distortion when expressed in
CC a Drosophila cell line. {ECO:0000269|PubMed:23249255}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC Evidence={ECO:0000269|PubMed:21205012};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:21205012};
CC Note=Requires Mg(2+) for membrane fusion.
CC {ECO:0000269|PubMed:21205012};
CC -!- SUBUNIT: Homodimer in solution (Probable). Both D1 and D2 domains
CC interact with YwpG, YneK interacts only with D1 while RNase Y (rny)
CC only interacts with whole protein (PubMed:23060960). Probably
CC oligomerizes at damaged membrane sites (Probable).
CC {ECO:0000269|PubMed:23060960, ECO:0000305|PubMed:21205012,
CC ECO:0000305|PubMed:26530236}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21205012,
CC ECO:0000269|PubMed:23060960, ECO:0000305|PubMed:26530236}; Peripheral
CC membrane protein {ECO:0000305}. Note=Found at the division septum; in
CC the absence of minJ dispersed along membrane. Associates with the cell
CC membrane via the D1 domain, D2 does not associate with membranes
CC (PubMed:21205012, PubMed:23060960). In growing cells forms foci at
CC midcell, colocalizes with FtsZ. Membrane localized in non-growing cells
CC (PubMed:23249255). Localized uniformly along cell membrane where it is
CC highly dynamic, DynA localizes to regions of membrane deformation upon
CC nisin treatment and remains at those sites. Localizes into foci upon
CC membrane potential dissipation (CCCP treatment, forms membrane pores)
CC (PubMed:26530236). {ECO:0000269|PubMed:21205012,
CC ECO:0000269|PubMed:23060960, ECO:0000269|PubMed:23249255,
CC ECO:0000269|PubMed:26530236}.
CC -!- DOMAIN: Has 2 similar domains, D1 (approximately residues 1-600) and D2
CC (approximately residues 601-1193). D1 is able to bind membranes, tether
CC liposomes and cause membrane fusion in the absence of D2; both regions
CC are required for GTPase activity. Possibly the fusion of 2 dynamin-like
CC genes (PubMed:21205012). D1 alone promotes membrane tethering but
CC requires D2 for stable tethering and content mixing (PubMed:31361971).
CC {ECO:0000269|PubMed:21205012, ECO:0000269|PubMed:31361971}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype (PubMed:21205012). 5% of
CC cells have a double septa, 2% of cells are very long. Double dynA-ezrA
CC mutants have longer cells with more double septa than either deletion
CC alone. Double dynA-floT deletions are highly elongated, filamentous and
CC have strong defects in cell shape; cells grow very slowly with an
CC extended lag phase. Double dynA-mreB deletions have strong cell shape
CC defects (PubMed:23249255). Double dynA-floT deletions are less motile
CC than single floT deletions (PubMed:26842743). Increased lipid mobility
CC in the cell membrane. Severe decrease in growth on nisin (causes
CC membrane pore formation) with significant membrane deformation and
CC damage, intermediate decrease in growth on antibiotics acting on lipid
CC II or the membrane (bacitracin and daptomycin). No effect on growth on
CC vancomycin (blocks peptidoglycan cross-links) or gramicidin D (makes
CC small pores). 20-50% increased susceptibility to phage phi29 and SPbeta
CC (PubMed:26530236). {ECO:0000269|PubMed:21205012,
CC ECO:0000269|PubMed:23249255, ECO:0000269|PubMed:26530236,
CC ECO:0000269|PubMed:26842743}.
CC -!- MISCELLANEOUS: Strain PSB025 / 25152 does not have the SP-beta
CC prophage. {ECO:0000269|PubMed:26530236}.
CC -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
CC superfamily. Dynamin/Fzo/YdjA family. {ECO:0000305}.
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DR EMBL; L77246; AAA96615.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14120.1; -; Genomic_DNA.
DR PIR; E69933; E69933.
DR RefSeq; NP_390085.1; NC_000964.3.
DR RefSeq; WP_003230755.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; P54159; -.
DR IntAct; P54159; 1.
DR STRING; 224308.BSU22030; -.
DR PaxDb; P54159; -.
DR PRIDE; P54159; -.
DR EnsemblBacteria; CAB14120; CAB14120; BSU_22030.
DR GeneID; 939071; -.
DR KEGG; bsu:BSU22030; -.
DR PATRIC; fig|224308.179.peg.2407; -.
DR eggNOG; COG0699; Bacteria.
DR OMA; FYVMDYN; -.
DR PhylomeDB; P54159; -.
DR BioCyc; BSUB:BSU22030-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0090529; P:cell septum assembly; IMP:CACAO.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR045063; Dynamin_N.
DR InterPro; IPR027094; Mitofusin_fam.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR10465; PTHR10465; 2.
DR Pfam; PF00350; Dynamin_N; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cell membrane; Cell shape; GTP-binding;
KW Hydrolase; Lipid-binding; Membrane; Nucleotide-binding; Reference proteome;
KW Repeat.
FT CHAIN 1..1193
FT /note="Dynamin-like protein A"
FT /id="PRO_0000049682"
FT REGION 1..609
FT /note="D1, associates with and fuses membranes, tethers
FT lipsomes"
FT /evidence="ECO:0000305|PubMed:21205012"
FT REGION 50..57
FT /note="G1 motif D1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055,
FT ECO:0000305"
FT REGION 76..78
FT /note="G2 motif D1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055,
FT ECO:0000305"
FT REGION 141..144
FT /note="G3 motif D1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055,
FT ECO:0000305"
FT REGION 199..202
FT /note="G4 motif D1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055,
FT ECO:0000305"
FT REGION 561..1193
FT /note="D2, does not associate with membranes"
FT /evidence="ECO:0000305|PubMed:21205012"
FT REGION 619..626
FT /note="G1 motif D2"
FT /evidence="ECO:0000305"
FT REGION 645..647
FT /note="G2 motif D2"
FT /evidence="ECO:0000305"
FT REGION 774..777
FT /note="G3 motif D2"
FT /evidence="ECO:0000305"
FT REGION 837..840
FT /note="G4 motif D2"
FT /evidence="ECO:0000305"
FT MUTAGEN 56
FT /note="K->A: No change in membrane fusion. Still binds GTP,
FT no GTPase activity. No longer binds GTP, no GTPase
FT activity; when associated with A-56. Double mutant causes
FT better vesicle and content mixing than wild-type."
FT /evidence="ECO:0000269|PubMed:21205012,
FT ECO:0000269|PubMed:31361971"
FT MUTAGEN 625
FT /note="K->A: No change in membrane fusion. Still binds GTP,
FT no GTPase activity. No longer binds GTP, no GTPase
FT activity; when associated with A-625. Double mutant causes
FT better vesicle and content mixing than wild-type."
FT /evidence="ECO:0000269|PubMed:21205012,
FT ECO:0000269|PubMed:31361971"
SQ SEQUENCE 1193 AA; 137385 MW; 33DCDE5B6E93D7AB CRC64;
MTDQNRKELL HKTGELYKQF IENQDEQRAA KLAAVMKKAA DEEVYIAFTG HYSAGKSSLL
NCLLMENILP TSPIPTSANL VVIRNGEKRV RLHTTDGACA ELEGTYQKDK VQQYCKDGEQ
IESVEIFDRY TEIDSGVAYI DTPGIDSTDD AHFLSAASIL HQADALFYVV HYNHVHAEEN
VKFLRSIKES IPNVYFIVNQ IDRHDETETK FGDYQAQVEE MLCNEGISRE ALYFTSVTEP
DHPFNQMGAL REELSRIEQQ SKSNMQALTE QKVRNLLKEH TEMLKKDETG APSFAEQLNI
HTGLVQSLRD QLDEAEKQMT EAEKRMQEEI NRILKNANLT PFEMRELAAA FLESQEPSFK
TGFFFSKAKT AQERDKRRNA FFSDVAKRTE AEADWHMIDT LHKLAKVFDV YTAESEKLIQ
AYRTPLDISI IEHAVKHGAA FSSEYVLQYT KDLAELIRKE AKREAADIIK VLSAMVKERV
SKDVQTINDR LVQESEKLVF LQEQARLENN AREKTDRLWA IWEEESACPM HIDTEWFKSK
KTRVAAPEQK QGRSQLTAQP MPKSEIKMEQ EMPLQDQIKR FYTLSDILGE CSMLLKQTSA
FRERVKRLEE RKFTLALFGG FSSGKSSFAN ALVGERVLPS SPTPTTATIN KITKPINGNL
NKTANVVFKT EDDLTAEILQ LTGIPKEPAG RSFTEKWEKA VKKNRLQEEH VKLISNFLLA
YEKYQQYIQE QKKLTIPLSE LKPYVAEETT ACAVKEVTVY YTCPLTEKGI TIVDTPGASS
MNKRHTELAF QYIKDADAFF YMTYYQHSFS KGDRSFLRKL GLVKESLSMD KMFFIINAAD
LAKDKTELET VTDYVSAELV KEGVYEPQLF TVSSKEELVG KPESFYNQFS KVRKHLDRFI
EVDVKKASAA QLSSEADKLC ETVFQLHQSQ HQSREEKEAQ KQCLMLSFER TAADIEKRRN
SKTIIEKVKK DTREQLYHIA QRLSYFANDL LKSAFHPGLQ NGDWKKNVSK AMTTALHEYL
FEYIQEIKTL DVRMSGFIER HINEEWLDHF QKTLNEDGYF SVYAGDQHSN GIQLKEVEPE
IEERAFEQEL KEIKSPKQFF EQKGKATFIE AVRMKLTKIT EAWIKNEEES LISHYTAHLR
RLQEDMGEKA IAQITDQKET YLRGYAEGEH AKEIEMAYQA CISWKNSDNT IKM
