ID A0A2N3PIA9_9HELI Unreviewed; 422 AA.
AC A0A2N3PIA9;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 28-JAN-2026, entry version 19.
DE SubName: Full=Apolipoprotein N-acyltransferase {ECO:0000313|EMBL:PKT80399.1};
GN ORFNames=BCM31_03165 {ECO:0000313|EMBL:PKT80399.1};
OS Helicobacter winghamensis.
OC Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
OC Campylobacterales; Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=157268 {ECO:0000313|EMBL:PKT80399.1, ECO:0000313|Proteomes:UP000233350};
RN [1] {ECO:0000313|EMBL:PKT80399.1, ECO:0000313|Proteomes:UP000233350}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=295_13 {ECO:0000313|EMBL:PKT80399.1,
RC ECO:0000313|Proteomes:UP000233350};
RA Zanoni R.G., Florio D., Caffara M., Renzi M., Parisi A., Pasquali F.,
RA Manfreda G.;
RT "Detection of Helicobacter winghamensis from caecal content of red fox
RT (Vulpes vulpes).";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
CC -!- SIMILARITY: Belongs to the CN hydrolase family. Apolipoprotein N-
CC acyltransferase subfamily. {ECO:0000256|ARBA:ARBA00010065}.
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:PKT80399.1}.
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DR EMBL; MBPK01000043; PKT80399.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N3PIA9; -.
DR STRING; 556267.HWAG_00884; -.
DR OrthoDB; 9804277at2; -.
DR Proteomes; UP000233350; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; IPR059109; Lnt_membrane_dom.
DR NCBIfam; TIGR00546; lnt; 1.
DR PANTHER; PTHR38686; APOLIPOPROTEIN N-ACYLTRANSFERASE; 1.
DR PANTHER; PTHR38686:SF1; APOLIPOPROTEIN N-ACYLTRANSFERASE; 1.
DR Pfam; PF26365; ApoNAT_membrane; 1.
DR SUPFAM; SSF56317; Carbon-nitrogen hydrolase; 1.
DR PROSITE; PS50263; CN_HYDROLASE; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000313|EMBL:PKT80399.1};
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Lipoprotein {ECO:0000313|EMBL:PKT80399.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000233350};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:PKT80399.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 39..55
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 60..77
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 89..111
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 118..136
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 151..168
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 206..422
FT /note="CN hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS50263"
SQ SEQUENCE 422 AA; 48827 MW; F2E53F3E06EF4D71 CRC64;
MLGQKVLANR LHGILAGILC ALFLSAFIYL EHFLDNKNFP LYSTLFAILG LFLYFKLSRL
GAFVCGGILG ILWFYWVGFS FRFYDLSHLI PLVWIVFFVV YGALFYLFCF FSSPFYRLVA
LTLSSFIHPF GFNWFIPEVI LTKSYFFPSK FTLFLLLCSI LILSAFLAKK LYKTSLIWLC
SFALLLPHNT EIKKDSNIMP LRIKTTHFEV PQDERWQTNQ MPNILTQNFE TILKAKNAGY
DLVILPETAF PLSLNLQSAL LEKLKEESKE IAILTGAIFQ DSIQEKPRFF NSAYLFQNGE
MQVFHKLILV PFGEKIPLPN FIAKWMNAFF FDGAQDFIAQ DFIAPNFAWI KNQKFQIAIC
YEATRDEFYA NSPSNLIAIS NNAWFVPSIE PTLQKLLMLY FSKNHNTTIY HSSNASEDFT
LH
//