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Database: UniProt
Entry: A0A0Q8XJU4_9SPHN
LinkDB: A0A0Q8XJU4_9SPHN
Original site: A0A0Q8XJU4_9SPHN 
ID   A0A0Q8XJU4_9SPHN        Unreviewed;       286 AA.
AC   A0A0Q8XJU4;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=CDP-alcohol phosphatidyltransferase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=ASE13_03105 {ECO:0000313|EMBL:KRC81396.1};
OS   Sphingomonas sp. Root241.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1736501 {ECO:0000313|EMBL:KRC81396.1, ECO:0000313|Proteomes:UP000051629};
RN   [1] {ECO:0000313|EMBL:KRC81396.1, ECO:0000313|Proteomes:UP000051629}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root241 {ECO:0000313|EMBL:KRC81396.1,
RC   ECO:0000313|Proteomes:UP000051629};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRC81396.1, ECO:0000313|Proteomes:UP000051629}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root241 {ECO:0000313|EMBL:KRC81396.1,
RC   ECO:0000313|Proteomes:UP000051629};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KRC81396.1}.
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DR   EMBL; LMIV01000001; KRC81396.1; -; Genomic_DNA.
DR   RefSeq; WP_056611290.1; NZ_LMIV01000001.1.
DR   AlphaFoldDB; A0A0Q8XJU4; -.
DR   STRING; 1736501.ASE13_03105; -.
DR   OrthoDB; 9790577at2; -.
DR   Proteomes; UP000051629; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   Pfam; PF01066; CDP-OH_P_transf; 1.
DR   PROSITE; PS00379; CDP_ALCOHOL_P_TRANSF; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003750};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        34..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        64..81
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        102..121
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        216..234
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        240..259
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   286 AA;  31005 MW;  6D6153F8D8FB2D18 CRC64;
     MTSPPPDGSR DRRIEDPTNL WIIHPAGRAL LPWFVARGIS ANAVSVIGLL LGGFAALAYA
     SWHAWPFAFL GLLFSVGWLI ADGLDGMVAR ATGTASALGR TLDGICDHGV FALIYILIAA
     SIGTLEIWAL AVAAGVLHAV QSSLYEGERA RFHRRCKGLV SAPPAPSRNP LVRLYDWVAG
     SVDRVAFLFD AALQREADPA ALGQAYGARA AKPMRLMSLL SANVRVYAIF FACLAGNPRY
     FFWFELIPLT AILVVGLTWH RTVESRLLRN AESASEHSSQ SHIQRT
//
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