ID   CDPAS_HALSA             Reviewed;         181 AA.
AC   Q9HNG1;
DT   21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   21-NOV-2003, sequence version 2.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=CDP-archaeol synthase {ECO:0000255|HAMAP-Rule:MF_01117};
DE            EC=2.7.7.67 {ECO:0000255|HAMAP-Rule:MF_01117};
DE   AltName: Full=CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol synthase {ECO:0000255|HAMAP-Rule:MF_01117};
GN   Name=carS {ECO:0000255|HAMAP-Rule:MF_01117}; OrderedLocusNames=VNG_2119C;
OS   Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS   (Halobacterium halobium).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halobacteriaceae; Halobacterium.
OX   NCBI_TaxID=64091;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
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).
CC   -!- FUNCTION: Catalyzes the formation of CDP-2,3-bis-(O-geranylgeranyl)-sn-
CC       glycerol (CDP-archaeol) from 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-
CC       phosphate (DGGGP) and CTP. This reaction is the third ether-bond-
CC       formation step in the biosynthesis of archaeal membrane lipids.
CC       {ECO:0000255|HAMAP-Rule:MF_01117}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + CTP +
CC         H(+) = CDP-2,3-bis-O-(geranylgeranyl)-sn-glycerol + diphosphate;
CC         Xref=Rhea:RHEA:25690, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:37563, ChEBI:CHEBI:58837, ChEBI:CHEBI:58838; EC=2.7.7.67;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01117};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01117};
CC   -!- PATHWAY: Membrane lipid metabolism; glycerophospholipid metabolism.
CC       {ECO:0000255|HAMAP-Rule:MF_01117}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01117};
CC       Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01117}.
CC   -!- SIMILARITY: Belongs to the CDP-archaeol synthase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01117}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG20259.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE004437; AAG20259.1; ALT_INIT; Genomic_DNA.
DR   PIR; G84361; G84361.
DR   RefSeq; WP_012289436.1; NC_002607.1.
DR   AlphaFoldDB; Q9HNG1; -.
DR   SMR; Q9HNG1; -.
DR   STRING; 64091.VNG_2119C; -.
DR   PaxDb; Q9HNG1; -.
DR   EnsemblBacteria; AAG20259; AAG20259; VNG_2119C.
DR   GeneID; 5954173; -.
DR   GeneID; 62887420; -.
DR   KEGG; hal:VNG_2119C; -.
DR   PATRIC; fig|64091.14.peg.1619; -.
DR   HOGENOM; CLU_105710_0_0_2; -.
DR   InParanoid; Q9HNG1; -.
DR   OrthoDB; 124973at2157; -.
DR   UniPathway; UPA00940; -.
DR   Proteomes; UP000000554; Chromosome.
DR   GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0043338; F:CTP:2,3-di-O-geranylgeranyl-sn-glycero-1-phosphate cytidyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046474; P:glycerophospholipid biosynthetic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01117; CDP_archaeol_synth; 1.
DR   InterPro; IPR032690; CarS.
DR   InterPro; IPR002726; CarS_archaea.
DR   PANTHER; PTHR39650; PTHR39650; 1.
DR   Pfam; PF01864; CarS-like; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Lipid biosynthesis; Lipid metabolism; Magnesium; Membrane;
KW   Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..181
FT                   /note="CDP-archaeol synthase"
FT                   /id="PRO_0000094168"
FT   TRANSMEM        7..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01117"
FT   TRANSMEM        55..75
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01117"
FT   TRANSMEM        80..100
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01117"
FT   TRANSMEM        128..148
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01117"
FT   TRANSMEM        150..170
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01117"
SQ   SEQUENCE   181 AA;  18243 MW;  29BD7F736040D521 CRC64;
     MDLVGTVVVA VWAMLPAYVP NNAAVLAGGG RPIDGGRSLG GRRLLGDGKT WRGTAVGTAA
     GVALAVALNA LRPAAADALG VVLPAFPPAA MGTLAFGAMV GDIAASFLKR RTGRQRGAAF
     PVVDQLDFVV VALALTALAV PAWVGDTFGL PVLVTVAVLT PALHLLTNGI AYALGVKDEP
     W