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Database: UniProt
Entry: A0A0Q7QMT8_9ACTN
LinkDB: A0A0Q7QMT8_9ACTN
Original site: A0A0Q7QMT8_9ACTN 
ID   A0A0Q7QMT8_9ACTN        Unreviewed;       240 AA.
AC   A0A0Q7QMT8;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=CDP-alcohol phosphatidyltransferase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=ASD11_12905 {ECO:0000313|EMBL:KQY60346.1};
OS   Aeromicrobium sp. Root495.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Aeromicrobium.
OX   NCBI_TaxID=1736550 {ECO:0000313|EMBL:KQY60346.1, ECO:0000313|Proteomes:UP000051970};
RN   [1] {ECO:0000313|EMBL:KQY60346.1, ECO:0000313|Proteomes:UP000051970}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root495 {ECO:0000313|EMBL:KQY60346.1,
RC   ECO:0000313|Proteomes:UP000051970};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQY60346.1, ECO:0000313|Proteomes:UP000051970}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root495 {ECO:0000313|EMBL:KQY60346.1,
RC   ECO:0000313|Proteomes:UP000051970};
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   -!- 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:KQY60346.1}.
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DR   EMBL; LMFJ01000001; KQY60346.1; -; Genomic_DNA.
DR   RefSeq; WP_056287719.1; NZ_LMFJ01000001.1.
DR   AlphaFoldDB; A0A0Q7QMT8; -.
DR   STRING; 1736550.ASD11_12905; -.
DR   OrthoDB; 7390033at2; -.
DR   Proteomes; UP000051970; 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   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   Reference proteome {ECO:0000313|Proteomes:UP000051970};
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        38..69
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        75..94
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        139..159
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        213..231
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   240 AA;  25523 MW;  D1E8D664264655AC CRC64;
     MTFTTDVRSA WDDLSGSQKS GAGVPWYMRV VNRRLGRVLA AVGARLGLVP DAMTALSALA
     FVAGAALFVA LPPSFAAAVV VVLLLQLGFA LDSADGQLAR LTGRGSVAGE WLDHVVDAGR
     LLLFHLAVGA AIVRHTELSL AWLLLPAVFG WLASVRFFAQ ILAEQLHRAA PAQEVPAAPE
     PVTSRSPWIQ LPADAGIVNA VLLLWPWTTM FLLGYGALAA ATALLTVATF VRKRRALRAW
//
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