ID GVPN2_HALSA Reviewed; 344 AA.
AC Q9HHS9; P33965;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 1.
DT 27-MAR-2024, entry version 114.
DE RecName: Full=Gas vesicle ATPase GvpN2 {ECO:0000250|UniProtKB:Q8YUT0};
DE EC=3.6.4.- {ECO:0000250|UniProtKB:Q8YUT0};
DE AltName: Full=Gas vesicle protein N2;
DE Short=GvpN2;
GN Name=gvpN2 {ECO:0000312|EMBL:AAG20897.1};
GN Synonyms=c-gvpN {ECO:0000303|PubMed:1404376};
GN OrderedLocusNames=VNG_6244G {ECO:0000312|EMBL:AAG20897.1};
OS Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS (Halobacterium halobium).
OG Plasmid pNRC200.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium; Halobacterium salinarum NRC-34001.
OX NCBI_TaxID=64091;
RN [1] {ECO:0000312|EMBL:CAA45994.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND GAS VESICLE GENE CLUSTER.
RC STRAIN=NRC-817;
RX PubMed=1404376; DOI=10.1016/0022-2836(92)90914-6;
RA Englert C., Krueger K., Offner S., Pfeifer F.;
RT "Three different but related gene clusters encoding gas vesicles in
RT halophilic archaea.";
RL J. Mol. Biol. 227:586-592(1992).
RN [2] {ECO:0000312|EMBL:CAA64341.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC STRAIN=PHH1 /PHH4;
RX PubMed=8763925; DOI=10.1128/jb.178.14.4012-4019.1996;
RA Krueger K., Pfeifer F.;
RT "Transcript analysis of the c-vac region and differential synthesis of the
RT two regulatory gas vesicle proteins GvpD and GvpE in Halobacterium
RT salinarium PHH4.";
RL J. Bacteriol. 178:4012-4019(1996).
RN [3] {ECO:0000312|EMBL:AAG20897.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700922 / JCM 11081 / NRC-1; PLASMID=pNRC200;
RX PubMed=11016950; DOI=10.1073/pnas.190337797;
RA Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D.,
RA Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D.,
RA Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R.,
RA Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P.,
RA Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M.,
RA Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J.,
RA Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L.,
RA DasSarma S.;
RT "Genome sequence of Halobacterium species NRC-1.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000).
RN [4]
RP FUNCTION IN BUOYANCY, AND POSSIBLE INDUCTION BY OXYGEN LIMITATION.
RC STRAIN=PHH1;
RX PubMed=33711860; DOI=10.1099/00221287-143-2-467;
RA Beard S.J., Hayes P.K., Walsby A.E.;
RT "Growth competition between Halobacterium salinarium strain PHH1 and
RT mutants affected in gas vesicle synthesis.";
RL Microbiology 143:467-473(1997).
RN [5]
RP FUNCTION.
RC STRAIN=PHH1;
RX PubMed=9611808; DOI=10.1099/00221287-144-5-1331;
RA Offner S., Ziese U., Wanner G., Typke D., Pfeifer F.;
RT "Structural characteristics of halobacterial gas vesicles.";
RL Microbiology 144:1331-1342(1998).
CC -!- FUNCTION: An ATPase that functions in gas vesicle formation (By
CC similarity). A minor component of the gas vesicle, also found in
CC soluble extracts (By similarity). Gas vesicles are hollow, gas filled
CC proteinaceous nanostructures found in several microbial planktonic
CC microorganisms. They allow positioning of halobacteria at the optimal
CC depth for growth in the poorly aerated, shallow brine pools of their
CC habitat (PubMed:33711860). {ECO:0000250|UniProtKB:Q8YUT0,
CC ECO:0000250|UniProtKB:Q9HI16, ECO:0000269|PubMed:33711860}.
CC -!- FUNCTION: Expression of 2 c-vac DNA fragments containing 2 divergently
CC transcribed regions (gvpE-gvpF-gvpG-gvpH-gvpI-gvpJ-gvpK-gvpL-gvpM and
CC gvpA-gvpC-gvpN-gvpO) allows H.volcanii to produce gas vesicles.
CC {ECO:0000269|PubMed:9611808}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:Q8YUT0};
CC -!- SUBUNIT: Forms homodimers, a GvpN-GvpO heterodimer, interacts with GvpC
CC and GvpL, might interact with GvpA. {ECO:0000250|UniProtKB:Q9HI16}.
CC -!- SUBCELLULAR LOCATION: Gas vesicle {ECO:0000250|UniProtKB:Q9HI16}.
CC Cytoplasm {ECO:0000250|UniProtKB:Q9HI16}.
CC -!- INDUCTION: In PHH4 (a deletion of the p-vac locus) not transcribed in
CC exponential phase, highly transcribed from stationary to mid-stationary
CC phase. Small amounts of longer transcripts that probably include gvpC-
CC gvpN-gvpO and further downstream are also seen (PubMed:8763925). Gas
CC vesicles appear earlier when grown in static culture, possibly due to
CC O(2)-limitation (PubMed:33711860). {ECO:0000269|PubMed:33711860,
CC ECO:0000269|PubMed:8763925}.
CC -!- MISCELLANEOUS: Encoded in a 14-gene locus called c-vac which produces
CC cylindrical gas vesicles only in the stationary growth phase.
CC {ECO:0000269|PubMed:1404376, ECO:0000269|PubMed:8763925}.
CC -!- SIMILARITY: Belongs to the CbbQ/NirQ/NorQ/GpvN family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X64730; CAA45994.1; -; Genomic_DNA.
DR EMBL; X94688; CAA64341.1; -; Genomic_DNA.
DR EMBL; AE004438; AAG20897.1; -; Genomic_DNA.
DR RefSeq; WP_010904110.1; NZ_BK010831.1.
DR AlphaFoldDB; Q9HHS9; -.
DR SMR; Q9HHS9; -.
DR GeneID; 68695201; -.
DR KEGG; hal:VNG_6244G; -.
DR PATRIC; fig|64091.14.peg.2245; -.
DR HOGENOM; CLU_051123_0_0_2; -.
DR InParanoid; Q9HHS9; -.
DR OrthoDB; 45425at2157; -.
DR PhylomeDB; Q9HHS9; -.
DR Proteomes; UP000000554; Plasmid pNRC200.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0031411; C:gas vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0031412; P:gas vesicle organization; IEA:InterPro.
DR CDD; cd00009; AAA; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011704; ATPase_dyneun-rel_AAA.
DR InterPro; IPR013462; Gas-vesicle_GvpN.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR02640; gas_vesic_GvpN; 1.
DR PANTHER; PTHR42759:SF1; MAGNESIUM-CHELATASE SUBUNIT CHLD; 1.
DR PANTHER; PTHR42759; MOXR FAMILY PROTEIN; 1.
DR Pfam; PF07728; AAA_5; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Gas vesicle; Hydrolase; Nucleotide-binding;
KW Plasmid; Reference proteome.
FT CHAIN 1..344
FT /note="Gas vesicle ATPase GvpN2"
FT /id="PRO_0000219568"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..48
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 89..96
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CONFLICT 323..327
FT /note="SDVEA -> KPSRP (in Ref. 1; CAA45994 and 2;
FT CAA64341)"
FT /evidence="ECO:0000305"
FT CONFLICT 336..337
FT /note="LA -> AGP (in Ref. 1; CAA45994 and 2; CAA64341)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 344 AA; 38077 MW; 1AD3463BD60B8D6E CRC64;
MTDTSRNRKV RGSKIRSSRS DKRQSRGSED KELKRLADAR DTDSEQAGDR VGDAFIPDEQ
SFIETDAVAR VTDRMRRWLS VDRPVHLIGP TGCGKTAVAM HVARTRDRPV VWVNGDADLT
TSDLVGEYAE TERISEHDQF IHNVVKRKDI VRDRWVDNPL TLAVQEGATL VYNEFSRTKP
VANNVLLSVF EEGVLELPGK RGASRYVDVH PAFRTILTSN SVEYAGVHEP QDALLDRLVG
LHMDFYDAET ETAIVRAHVE AADVPVAAIV GMMRELRERL EITVGTRAAI MAAEGLTAAD
DPDADTVVDV CTDVLASKVS QRSDVEALRD VIEETLADRG VTLS
//
