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Database: UniProt
Entry: A0LMU8_SYNFM
LinkDB: A0LMU8_SYNFM
Original site: A0LMU8_SYNFM 
ID   A0LMU8_SYNFM            Unreviewed;       210 AA.
AC   A0LMU8;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   27-MAR-2024, entry version 69.
DE   SubName: Full=CDP-alcohol phosphatidyltransferase {ECO:0000313|EMBL:ABK18750.1};
GN   OrderedLocusNames=Sfum_3077 {ECO:0000313|EMBL:ABK18750.1};
OS   Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB).
OC   Bacteria; Thermodesulfobacteriota; Syntrophobacteria; Syntrophobacterales;
OC   Syntrophobacteraceae; Syntrophobacter.
OX   NCBI_TaxID=335543 {ECO:0000313|EMBL:ABK18750.1, ECO:0000313|Proteomes:UP000001784};
RN   [1] {ECO:0000313|EMBL:ABK18750.1, ECO:0000313|Proteomes:UP000001784}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10017 / MPOB {ECO:0000313|Proteomes:UP000001784};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.G.,
RA   Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Boone D.R., Brockman F., Culley D., Ferry J., Gunsalus R.,
RA   McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J., Sieber J.,
RA   Stams A.J.M., Worm P., Henstra A.M., Richardson P.;
RT   "Complete sequence of Syntrophobacter fumaroxidans MPOB.";
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-I
CC       family. {ECO:0000256|RuleBase:RU003750}.
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DR   EMBL; CP000478; ABK18750.1; -; Genomic_DNA.
DR   RefSeq; WP_011699875.1; NC_008554.1.
DR   AlphaFoldDB; A0LMU8; -.
DR   STRING; 335543.Sfum_3077; -.
DR   KEGG; sfu:Sfum_3077; -.
DR   eggNOG; COG0558; Bacteria.
DR   HOGENOM; CLU_080384_1_0_7; -.
DR   InParanoid; A0LMU8; -.
DR   OrthoDB; 9785831at2; -.
DR   Proteomes; UP000001784; Chromosome.
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   Reference proteome {ECO:0000313|Proteomes:UP000001784};
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        33..61
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        115..135
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        155..176
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        182..202
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   210 AA;  23417 MW;  C7AC50D2F31641E7 CRC64;
     MLKGTPIETG YYNLLERLIV PKLVRFHLTP NHISLMGLVT SMLAGLAFVF FPLVGGILTL
     LTGLLDTLDG SLARATGQSK KFGAFLDSIL DRYTELIIYL GIWTYFYRQD AKTPFFSLLI
     LLILFGSLMV SYTRARAEGL GERCLVGFFQ RGERIILLGL SGILNPFVNL IASSGWTRDL
     MLFAGLLILA VGTNLTALWR FLHVLNKLRP
//
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