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Database: UniProt
Entry: A0A1Q5DBV3_9ACTN
LinkDB: A0A1Q5DBV3_9ACTN
Original site: A0A1Q5DBV3_9ACTN 
ID   A0A1Q5DBV3_9ACTN        Unreviewed;       243 AA.
AC   A0A1Q5DBV3;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=CDP-alcohol phosphatidyltransferase {ECO:0000313|EMBL:OKI93327.1};
GN   ORFNames=AMK18_31570 {ECO:0000313|EMBL:OKI93327.1};
OS   Streptomyces sp. CB01249.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1703929 {ECO:0000313|EMBL:OKI93327.1, ECO:0000313|Proteomes:UP000186839};
RN   [1] {ECO:0000313|EMBL:OKI93327.1, ECO:0000313|Proteomes:UP000186839}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CB01249 {ECO:0000313|EMBL:OKI93327.1,
RC   ECO:0000313|Proteomes:UP000186839};
RX   PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA   Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA   Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA   Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT   "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL   MBio 7:e02104-e02116(2016).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-I
CC       family. {ECO:0000256|RuleBase:RU003750}.
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:OKI93327.1}.
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DR   EMBL; LISW01000009; OKI93327.1; -; Genomic_DNA.
DR   RefSeq; WP_073865562.1; NZ_LISW01000009.1.
DR   AlphaFoldDB; A0A1Q5DBV3; -.
DR   OrthoDB; 7390033at2; -.
DR   Proteomes; UP000186839; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016780; F:phosphotransferase activity, for other substituted phosphate groups; IEA:InterPro.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IEA:InterPro.
DR   Gene3D; 1.20.120.1760; -; 1.
DR   InterPro; IPR000462; CDP-OH_P_trans.
DR   InterPro; IPR043130; CDP-OH_PTrfase_TM_dom.
DR   InterPro; IPR048254; CDP_ALCOHOL_P_TRANSF_CS.
DR   InterPro; IPR014472; CHOPT.
DR   PANTHER; PTHR10414:SF37; BB IN A BOXCAR, ISOFORM C; 1.
DR   PANTHER; PTHR10414; ETHANOLAMINEPHOSPHOTRANSFERASE; 1.
DR   Pfam; PF01066; CDP-OH_P_transf; 1.
DR   PROSITE; PS00379; CDP_ALCOHOL_P_TRANSF; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186839};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003750};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        74..91
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        139..160
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        187..206
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        212..231
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   243 AA;  25752 MW;  AA9841A6870B3577 CRC64;
     METTTTVLGR LRGAQKTAKG VSLYSRYVNR PAGRVFAAAA YRLGMTPNQV TLTSAAFTFT
     ALACVALVRP GPGMAVLVYL GLAVGFALDS ADGQLARLTG RGGPDGEWLD HVVDCAKMIL
     VHTVVLIAFH RYFALPGDGW LLLPLGFLFV AVLTFCAGLL REQLGKAAAH GAAAAPGPAA
     PPSRLRAVAL LPADYGVFCL VFLLLGDETA FRTGYAVLAA VHALFLVLFL GKWFRELKAL
     RAH
//
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