ID A0A128EDR8_9BACT Unreviewed; 401 AA.
AC A0A128EDR8;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 28-JAN-2026, entry version 26.
DE SubName: Full=Apolipoprotein N-acyltransferase {ECO:0000313|EMBL:CZE47084.1};
DE EC=2.3.1.- {ECO:0000313|EMBL:CZE47084.1};
GN Name=lnt {ECO:0000313|EMBL:CZE47084.1};
GN ORFNames=ERS672216_00707 {ECO:0000313|EMBL:CZE47084.1};
OS Campylobacter geochelonis.
OC Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
OC Campylobacterales; Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=1780362 {ECO:0000313|EMBL:CZE47084.1, ECO:0000313|Proteomes:UP000069632};
RN [1] {ECO:0000313|EMBL:CZE47084.1, ECO:0000313|Proteomes:UP000069632}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RC20 {ECO:0000313|EMBL:CZE47084.1,
RC ECO:0000313|Proteomes:UP000069632};
RG Pathogen Informatics;
RL Submitted (FEB-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}.
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DR EMBL; FIZP01000002; CZE47084.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A128EDR8; -.
DR Proteomes; UP000069632; 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; IPR059110; Lnt_campylobact.
DR InterPro; IPR059109; Lnt_membrane_dom.
DR NCBIfam; TIGR00546; lnt; 1.
DR NCBIfam; NF008934; PRK12291.1; 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:CZE47084.1};
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Lipoprotein {ECO:0000313|EMBL:CZE47084.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000069632};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CZE47084.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 41..63
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 69..88
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 95..114
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 126..143
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 176..401
FT /note="CN hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS50263"
SQ SEQUENCE 401 AA; 46698 MW; 90F20683279C625D CRC64;
MISNFIFLTL FDNLILEFIS PFLAIYGFYK LFDANRFEFF HTGFFIGILW FYWVSFSLVY
YGFAFLIPLE ILFFGLVYGL IFLVCGWWKN KFIRAILLIL ISYFYPFNFN WLNLELVLVP
GLFEPNLRGL CAIFAGILAF YYLKKFKLLG LFVGVILALQ ITQEKPNFLP LKTKLINTQI
SQYTKWNPKF SKQHIIEALN LIDEAIKDGY KFIVLPENAF VTHLNLEPNL EQILKEKSHF
STILTGALAY ENGRQYNSSF LFSKGSVQRF DKFILVPFGE EIPLPNFIKK ALNLLFFNGA
KDFDKASSFS DYKVDNQVIR NAICYEVTRS ETYKNSPKFV VAISNNGWFT PSTEPNLQRL
LIKYYATKHG TTVYHSVNGS KSEIITPKEL WVVKFINLFK K
//
