ID A0A285EBY9_9ACTN Unreviewed; 554 AA.
AC A0A285EBY9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Apolipoprotein N-acyltransferase {ECO:0000313|EMBL:SNX96555.1};
GN ORFNames=SAMN06893097_104270 {ECO:0000313|EMBL:SNX96555.1};
OS Geodermatophilus sabuli.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Geodermatophilus.
OX NCBI_TaxID=1564158 {ECO:0000313|EMBL:SNX96555.1, ECO:0000313|Proteomes:UP000219514};
RN [1] {ECO:0000313|EMBL:SNX96555.1, ECO:0000313|Proteomes:UP000219514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 46844 {ECO:0000313|EMBL:SNX96555.1,
RC ECO:0000313|Proteomes:UP000219514};
RA Ehlers B., Leendertz F.H.;
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; OBDO01000004; SNX96555.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A285EBY9; -.
DR OrthoDB; 4532287at2; -.
DR Proteomes; UP000219514; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0016410; F:N-acyltransferase activity; IEA:InterPro.
DR GO; GO:0042158; P:lipoprotein biosynthetic process; IEA:InterPro.
DR Gene3D; 3.60.110.10; Carbon-nitrogen hydrolase; 1.
DR InterPro; IPR004563; Apolipo_AcylTrfase.
DR InterPro; IPR003010; C-N_Hydrolase.
DR InterPro; IPR036526; C-N_Hydrolase_sf.
DR InterPro; IPR045378; LNT_N.
DR PANTHER; PTHR38686; APOLIPOPROTEIN N-ACYLTRANSFERASE; 1.
DR PANTHER; PTHR38686:SF1; APOLIPOPROTEIN N-ACYLTRANSFERASE; 1.
DR Pfam; PF00795; CN_hydrolase; 1.
DR Pfam; PF20154; LNT_N; 1.
DR SUPFAM; SSF56317; Carbon-nitrogen hydrolase; 1.
DR PROSITE; PS50263; CN_HYDROLASE; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000313|EMBL:SNX96555.1};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Lipoprotein {ECO:0000313|EMBL:SNX96555.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000219514};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:SNX96555.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 35..65
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 77..98
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 104..127
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 139..160
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 172..193
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 214..233
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 268..491
FT /note="CN hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS50263"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 526..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 554 AA; 58527 MW; A42254FB62E630CC CRC64;
MATISGDPVA TSAGAAVRGR PSRVRRPYPG GRSPWVWLLL GTLLLPFANL QTLIPLTAWV
APVFLMRFSR SQRPLTGLLV LTVAMSLALL AGLRNGFFPV EDGVGYYLFV AMLGLGGALP
FAVDRLLAPR LTGLPRTLVF PAAVTTADFI GTISSAYGAA GSTAYSQYAG LPLLQLASVT
GIWGLTFLVS WLAPVVNELW ERGLEGSRHR SPSVVFAATL AAALVFGGAQ LAFATPAADT
VRVAALAPDR QLSDLAYSAP PLTPGDPAER AAVRDEYFRP VLDELFERSE REAEAGAEII
AWSEAAALTL EEEQSAVVAR AADLAREHGV YLQVSMMVQL ADAGDGSDGA AVNENHAVLM
DPRGTVVWDY LKSKPVPGDG HDPGPGIVPT VDTPYGRLAT IICQDDFFPG LVRQAGRAGV
DILLVPSSDW RSISAWHAQQ APFRAVENGV ALVRPTRQGI SLATDAQGRL LGHKADYFTA
ADQTLVVSVP TQGTGTWYAR MGDTVAFASA VGLLVLTRAA WNSRSRRRDG GAAPAATGSD
QAERPAPLDG VATR
//