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Database: UniProt
Entry: F1YZK3_9STRE
LinkDB: F1YZK3_9STRE
Original site: F1YZK3_9STRE 
ID   F1YZK3_9STRE            Unreviewed;       264 AA.
AC   F1YZK3;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 56.
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   Name=cdsA {ECO:0000313|EMBL:EGE53940.1};
GN   ORFNames=SPB_1733 {ECO:0000313|EMBL:EGE53940.1};
OS   Streptococcus parauberis NCFD 2020.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=873447 {ECO:0000313|EMBL:EGE53940.1, ECO:0000313|Proteomes:UP000003732};
RN   [1] {ECO:0000313|EMBL:EGE53940.1, ECO:0000313|Proteomes:UP000003732}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCFD 2020 {ECO:0000313|EMBL:EGE53940.1,
RC   ECO:0000313|Proteomes:UP000003732};
RA   Stanhope M.J., Durkin A.S., Hostetler J., Kim M., Radune D., Singh I.,
RA   Town C.D.;
RL   Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EGE53940.1}.
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DR   EMBL; AEUT02000001; EGE53940.1; -; Genomic_DNA.
DR   RefSeq; WP_003104075.1; NZ_AEUT02000001.1.
DR   AlphaFoldDB; F1YZK3; -.
DR   GeneID; 66815545; -.
DR   eggNOG; COG4589; Bacteria.
DR   HOGENOM; CLU_037294_2_2_9; -.
DR   UniPathway; UPA00557; UER00614.
DR   Proteomes; UP000003732; Unassembled WGS sequence.
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   Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209};
KW   Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264};
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        6..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        49..68
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        74..97
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        109..129
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        135..152
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        173..191
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        197..217
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   264 AA;  29111 MW;  5A4B97BCF8D49348 CRC64;
     MKERVIWGLI AAVIFLPFLV FGSLPFQLFV GGLAMIAVSE MFKMKRLEIF SFEGALAMMA
     AFVLTIPMDS YLTFLPIDAS FACYGLFVFL ILAGTVINSE RYSFDDAAFP IAASLYVGIG
     FQNLVHARMA GIDKVLLALF IVWATDIGAY LIGRQYGKRK LLPKVSPNKT IEGSLGGILS
     AVVVALIFML VDKAVYAPFN FFLMLIFVAC FSVFAQFGDL VESSIKRHFG VKDSGKLIPG
     HGGILDRFDS MIFVFPIMHL FGLF
//
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