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Database: UniProt
Entry: A0A0M4QKK0_9PSEU
LinkDB: A0A0M4QKK0_9PSEU
Original site: A0A0M4QKK0_9PSEU 
ID   A0A0M4QKK0_9PSEU        Unreviewed;       779 AA.
AC   A0A0M4QKK0;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=CDP-alcohol phosphatidyltransferase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=XF36_21390 {ECO:0000313|EMBL:ALE85390.1};
OS   Pseudonocardia sp. HH130629-09.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Pseudonocardia.
OX   NCBI_TaxID=1641402 {ECO:0000313|EMBL:ALE85390.1, ECO:0000313|Proteomes:UP000062082};
RN   [1] {ECO:0000313|EMBL:ALE85390.1, ECO:0000313|Proteomes:UP000062082}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HH130629-09 {ECO:0000313|EMBL:ALE85390.1,
RC   ECO:0000313|Proteomes:UP000062082};
RX   PubMed=26438860; DOI=10.1073/pnas.1515348112;
RA   Sit C.S., Van Arnam E.B., Ramadhar T.R.;
RT   "Variable genetic architectures produce virtually identical molecules in
RT   bacterial symbionts of fungus-growing ants.";
RL   Proc. Natl. Acad. Sci. U.S.A. 112:13150-13154(2015).
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}.
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DR   EMBL; CP011868; ALE85390.1; -; Genomic_DNA.
DR   RefSeq; WP_060713351.1; NZ_CP011868.1.
DR   AlphaFoldDB; A0A0M4QKK0; -.
DR   KEGG; pseh:XF36_21390; -.
DR   PATRIC; fig|1641402.3.peg.4577; -.
DR   OrthoDB; 1376015at2; -.
DR   Proteomes; UP000062082; 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   Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR   InterPro; IPR017850; Alkaline_phosphatase_core_sf.
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   SUPFAM; SSF53649; Alkaline phosphatase-like; 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:UP000062082};
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        40..60
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        72..92
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        188..205
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        211..233
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        245..265
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        277..294
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        301..326
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        346..378
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        390..409
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   779 AA;  80358 MW;  9C0B0D20B32AAA9C CRC64;
     MLRKSSGPAA SAPVALQVVA GAALLAAVLA VLVPTTGAGA LRVTGAAVTG ALGAAMLLRA
     ARRAGERTLG PAGVVTLARG ALAVAVVSLV GLEGAGTVAL VTLTAVALVL DGVDGPIARR
     TGTVTALGAR FDMETDAFLL MVLSTHVAAT TGHWWVTALG LLRYAFVAAG RVAPWLRGEL
     PPRYSAKVVA ALQGVVLVVT AAGVLPVSAA LVAVGVALAA LVWSFGVSVV QLWRAADRHP
     FHTRRAAAAL FTTLCAALVG VILVLPADPV ALDPAGLLRL PIEAVLGAAV LALLPGRARW
     VAAALAGTLL AAVGLLKLAD IGFLTFQGRR FDAVSDWSLL GNAHDFLRGT AGAAGTVVVV
     LAGVVAVGLV AGTAGAVVRL GRLAARHRRA TVGVAALLAT AWLVVGTVAD ARLVAGVPVA
     AADGVAEVAH RAQQVPETLR ERRELTESLA RDGWDGAPPD ALLSALRGKD VVITFVESYG
     RNAQHAPEMA PRIRPVLTEA DARLTAAGYG ARSGVLTAPI NGGGSWLAHA TLFSGLSIAD
     QGAHDRLTAS DRLTLPRAFR DAGWETAVVT PATTREWPEA AFFGHQRVYA GDDLGYAGPP
     FSWSPMPDQY TLDAFSRLEL DRPDRGPLLG TVVLTSSHAP WSPVPPLLDP AGIGDGAVYG
     PYAGGQQSYD TIFSLDRETL RGDYLTSLEY ALRSATGWVA DRPGSDRDLV VLLLGDHEPG
     ATVSGPGAGS DVPISVITRD TEVLDRIDDW GWTPGLLPPP DAPPWPMAEF RDRILAAFS
//
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