ID A0A2G0CDH2_9BACT Unreviewed; 587 AA.
AC A0A2G0CDH2;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=Apolipoprotein N-acyltransferase {ECO:0000256|HAMAP-Rule:MF_01148};
DE Short=ALP N-acyltransferase {ECO:0000256|HAMAP-Rule:MF_01148};
DE EC=2.3.1.269 {ECO:0000256|HAMAP-Rule:MF_01148};
GN Name=lnt {ECO:0000256|HAMAP-Rule:MF_01148,
GN ECO:0000313|EMBL:PHK98005.1};
GN ORFNames=CGL56_12490 {ECO:0000313|EMBL:PHK98005.1};
OS Neolewinella marina.
OC Bacteria; Bacteroidota; Saprospiria; Saprospirales; Lewinellaceae;
OC Neolewinella.
OX NCBI_TaxID=438751 {ECO:0000313|EMBL:PHK98005.1, ECO:0000313|Proteomes:UP000226437};
RN [1] {ECO:0000313|EMBL:PHK98005.1, ECO:0000313|Proteomes:UP000226437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MKG-38 {ECO:0000313|EMBL:PHK98005.1,
RC ECO:0000313|Proteomes:UP000226437};
RA Wang K.;
RT "The draft genome sequence of Lewinella marina KCTC 32374.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the phospholipid dependent N-acylation of the N-
CC terminal cysteine of apolipoprotein, the last step in lipoprotein
CC maturation. {ECO:0000256|HAMAP-Rule:MF_01148}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a glycerophospholipid + N-terminal S-1,2-diacyl-sn-glyceryl-L-
CC cysteinyl-[lipoprotein] = a 2-acyl-sn-glycero-3-phospholipid + H(+) +
CC N-acyl-S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein];
CC Xref=Rhea:RHEA:48228, Rhea:RHEA-COMP:14681, Rhea:RHEA-COMP:14684,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:136912, ChEBI:CHEBI:140656,
CC ChEBI:CHEBI:140657, ChEBI:CHEBI:140660; EC=2.3.1.269;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01148};
CC -!- PATHWAY: Protein modification; lipoprotein biosynthesis (N-acyl
CC transfer). {ECO:0000256|HAMAP-Rule:MF_01148}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01148};
CC Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_01148}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the CN hydrolase family. Apolipoprotein N-
CC acyltransferase subfamily. {ECO:0000256|HAMAP-Rule:MF_01148}.
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:PHK98005.1}.
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DR EMBL; PDLO01000005; PHK98005.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G0CDH2; -.
DR OrthoDB; 9804277at2; -.
DR UniPathway; UPA00666; -.
DR Proteomes; UP000226437; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016410; F:N-acyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0042158; P:lipoprotein biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd07571; ALP_N-acyl_transferase; 1.
DR Gene3D; 3.60.110.10; Carbon-nitrogen hydrolase; 1.
DR HAMAP; MF_01148; Lnt; 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 NCBIfam; TIGR00546; lnt; 1.
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 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315, ECO:0000256|HAMAP-
KW Rule:MF_01148};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_01148}; Lipoprotein {ECO:0000313|EMBL:PHK98005.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01148};
KW Reference proteome {ECO:0000313|Proteomes:UP000226437};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01148};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_01148};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_01148}.
FT TRANSMEM 6..24
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT TRANSMEM 31..51
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT TRANSMEM 71..95
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT TRANSMEM 107..125
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT TRANSMEM 131..152
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT TRANSMEM 201..223
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT TRANSMEM 235..254
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT DOMAIN 266..544
FT /note="CN hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS50263"
SQ SEQUENCE 587 AA; 65103 MW; 6B3CB88A3DFC1687 CRC64;
MRNRLPYAIG CFVLAALTAW LMYTRAASEE LWGYLPLLLY LLTWAGTVLV ASRSATAPAR
RRLLLSTATG LLLGLGFPGY LPAPVLLFVA WVPLLLLQRE TESTRTVFWH GYNAFLLYNI
IATFWVTNTA FFAGLFAVTV NSLLMCIPWL LFHWTSRVSP RVSYLALIAA WVSFEHFHYN
WSLNWPWLTL GNGFAQFPSL VQWYEITGVL GGTVWILVVN WLVLRFYLSR PPRPVPVSLL
LALVLPIAAS LWRYQTYETP AGGGSITVSA IQPNFEPHYE KFSGSAEEQL GVLLDLSTRA
IAEVDGPVDY LLLPETTFSR VEEGDPLAEP TLATFLRDLP PNRVRHLVTG VSAYHRFAPG
EAVTDAVRYY PAAGGGEIAL EALNGAVQVE LPDRDVQTYR KGVFVPGAES FPFRKVLFFL
EPLVNSLGGS VAGLGTQTDR TPFTGESAAV APVICYESVF GEYFTGYVRE GAQAAFVMTN
DGWWDDTPGH LQHLWFSSLR AIETRRAVVR SANLGACAFI DPRGKIMSRT YYDERGYLNG
TLPLNDALTP YVRYGDILAR VAALLAVMAL LSNLARTLRR RGGALQP
//
