ID X2HCV6_9NEIS Unreviewed; 269 AA.
AC X2HCV6;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Phosphatidate cytidylyltransferase {ECO:0000256|ARBA:ARBA00019373, ECO:0000256|RuleBase:RU003938};
DE EC=2.7.7.41 {ECO:0000256|ARBA:ARBA00012487, ECO:0000256|RuleBase:RU003938};
GN ORFNames=SALWKB2_0044 {ECO:0000313|EMBL:AHN27426.1};
OS Snodgrassella alvi wkB2.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Snodgrassella.
OX NCBI_TaxID=1196094 {ECO:0000313|EMBL:AHN27426.1, ECO:0000313|Proteomes:UP000019668};
RN [1] {ECO:0000313|EMBL:AHN27426.1, ECO:0000313|Proteomes:UP000019668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WkB2 {ECO:0000313|EMBL:AHN27426.1};
RX PubMed=25053814;
RA Kwong W.K., Engel P., Koch H., Moran N.A.;
RT "Genomics and host specialization of honey bee and bumble bee gut
RT symbionts.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:11509-11514(2014).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphate + CTP + H(+) = a CDP-1,2-
CC diacyl-sn-glycerol + diphosphate; Xref=Rhea:RHEA:16229,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563,
CC ChEBI:CHEBI:58332, ChEBI:CHEBI:58608; EC=2.7.7.41;
CC Evidence={ECO:0000256|ARBA:ARBA00001698,
CC ECO:0000256|RuleBase:RU003938};
CC -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC diacylglycerol from sn-glycerol 3-phosphate: step 3/3.
CC {ECO:0000256|ARBA:ARBA00005119, ECO:0000256|RuleBase:RU003938}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the CDS family. {ECO:0000256|ARBA:ARBA00010185,
CC ECO:0000256|RuleBase:RU003938}.
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DR EMBL; CP007446; AHN27426.1; -; Genomic_DNA.
DR RefSeq; WP_025329699.1; NZ_CP091515.1.
DR AlphaFoldDB; X2HCV6; -.
DR STRING; 1196094.SALWKB2_0044; -.
DR GeneID; 32537202; -.
DR KEGG; salv:SALWKB2_0044; -.
DR PATRIC; fig|1196094.4.peg.44; -.
DR HOGENOM; CLU_037294_1_2_4; -.
DR OrthoDB; 9799199at2; -.
DR UniPathway; UPA00557; UER00614.
DR Proteomes; UP000019668; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0004605; F:phosphatidate cytidylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR000374; PC_trans.
DR PANTHER; PTHR46382; PHOSPHATIDATE CYTIDYLYLTRANSFERASE; 1.
DR PANTHER; PTHR46382:SF1; PHOSPHATIDATE CYTIDYLYLTRANSFERASE; 1.
DR Pfam; PF01148; CTP_transf_1; 1.
DR PROSITE; PS01315; CDS; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU003938};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003938};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU003938};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 5..21
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 56..73
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 79..97
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 109..127
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 133..154
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 175..196
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 202..222
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 269 AA; 29701 MW; F60E25BD7CEA8F41 CRC64;
MLKQRILTAL VLLPLMIGML FGANNSLWAA FSGLIALLAL WEYARIAHFT NIQNALYLLV
SAVGGGCLYF YYQQTALPLW TQIMVLLFWL IIVPVWLKFK WKIKANLSGV MIGWLLMVPF
WQALISLRPD TKAAGALLSI MALVWIADIA AYFVGRAVGK RKLAPTISPN KSWEGAIGAV
ICVAIYTIVL QQQGWLPFIL PWWQTLCLAF VLTAVSICGD LLESWLKRAG GVKDSSQLLP
GHGGVFDRID SLIAVLSVYA ALIACFSVK
//
