ID   GVPD_HALMT              Reviewed;         545 AA.
AC   Q02229; I3R593;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Protein GvpD;
GN   Name=gvpD; OrderedLocusNames=HFX_1697;
OS   Haloferax mediterranei (strain ATCC 33500 / DSM 1411 / JCM 8866 / NBRC
OS   14739 / NCIMB 2177 / R-4) (Halobacterium mediterranei).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Haloferax.
OX   NCBI_TaxID=523841;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4;
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]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4;
RX   PubMed=22843593; DOI=10.1128/jb.00880-12;
RA   Han J., Zhang F., Hou J., Liu X., Li M., Liu H., Cai L., Zhang B., Chen Y.,
RA   Zhou J., Hu S., Xiang H.;
RT   "Complete genome sequence of the metabolically versatile halophilic
RT   archaeon Haloferax mediterranei, a poly(3-hydroxybutyrate-co-3-
RT   hydroxyvalerate) producer.";
RL   J. Bacteriol. 194:4463-4464(2012).
CC   -!- FUNCTION: May play a role in an energy requiring process such as
CC       assembly of gas vesicles in addition to a possible structural or
CC       regulatory function.
CC   -!- SUBCELLULAR LOCATION: Vacuole, gas vesicle {ECO:0000305}.
CC   -!- DEVELOPMENTAL STAGE: Expressed only late in the growth cycle.
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DR   EMBL; X64701; CAA45946.1; -; Genomic_DNA.
DR   EMBL; CP001868; AFK19403.1; -; Genomic_DNA.
DR   PIR; S28117; S28117.
DR   RefSeq; WP_014732346.1; NZ_CP039139.1.
DR   AlphaFoldDB; Q02229; -.
DR   STRING; 523841.HFX_1697; -.
DR   EnsemblBacteria; AFK19403; AFK19403; HFX_1697.
DR   GeneID; 40157052; -.
DR   KEGG; hme:HFX_1697; -.
DR   eggNOG; arCOG01178; Archaea.
DR   HOGENOM; CLU_047518_0_0_2; -.
DR   OMA; YEPYMEY; -.
DR   OrthoDB; 13916at2157; -.
DR   Proteomes; UP000006469; Chromosome.
DR   GO; GO:0031411; C:gas vesicle; IEA:UniProtKB-SubCell.
DR   GO; GO:0005773; C:vacuole; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR009788; GvpD.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF07088; GvpD; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Gas vesicle; Nucleotide-binding; Vacuole.
FT   CHAIN           1..545
FT                   /note="Protein GvpD"
FT                   /id="PRO_0000182674"
FT   REGION          352..418
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        366..386
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         39..46
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   545 AA;  60652 MW;  965380E2C2EF7FDB CRC64;
     MPPPNPAYSP TEQQGRVLFP REVSRFFTGD PGHTLLVNGA PGTGKTLFTI RGLDVLERDG
     DVLYVSTRVD QDTVHEMYFR EHSSLDKTHI LDLSQDPFEL PLDVDVPFEK LGLDSLLEWI
     QQIKAASKRL TIAFDSWELI YEYLASRHDD SPDIETVTTQ LVSLARQENI RLLLVSETAD
     SSPLEYIVDG VVTLQVAEDE RGRTRRYLRL EKLRGVRIGN RLQPITLADG QFQAITPVEL
     PTVRTGANNG TWEPRTNTKA KFSTGIGDLD PILSGGYNRG SVIHLDLGTD LSRDAWSVLT
     LPTIRNFLAN EMGVAVVPPR EGSPGLLHND LNSVLTPRVF DTYCHVFETY AGPSRNRGTY
     EEDGQVETPL DTSQTATPSD AESPVGTETE LSEKVETELS EENPPAPGEV VDTERSTTIG
     KELESPVEGG QLDYEPYMEY VEEVRKQSDG PLLHVISMDT ARTAFETRLG DFANYVALHN
     DLAILITKPG TELRRRADRV ADMHFRLERS GEAIMLYGEN PLTPLLGIGI DRSQPIPEII
     LTEMV