ID A0A257CRN7_9BURK Unreviewed; 805 AA.
AC A0A257CRN7;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
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:OYT91724.1};
GN ORFNames=CFE43_12245 {ECO:0000313|EMBL:OYT91724.1};
OS Burkholderiales bacterium PBB3.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales.
OX NCBI_TaxID=2015565 {ECO:0000313|EMBL:OYT91724.1, ECO:0000313|Proteomes:UP000216249};
RN [1] {ECO:0000313|EMBL:OYT91724.1, ECO:0000313|Proteomes:UP000216249}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PBB3 {ECO:0000313|EMBL:OYT91724.1};
RA Kojadinovic M., Villain A., Puppo C., Fon Sing S., Prioretti L., Hubert P.,
RA Gregori G., Zhang Y., Sassi J.-F., Claverie J.-M., Blanc G., Gontero B.;
RT "A metagenomic investigation of the 'star' freshwater diatom Asterionella
RT formosa and its bacterial cohort.";
RL Submitted (JUN-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|ARBA:ARBA00010065,
CC ECO:0000256|HAMAP-Rule:MF_01148}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {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:OYT91724.1}.
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DR EMBL; NKIK01000019; OYT91724.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A257CRN7; -.
DR UniPathway; UPA00666; -.
DR Proteomes; UP000216249; 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 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:OYT91724.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01148};
KW Reference proteome {ECO:0000313|Proteomes:UP000216249};
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 13..36
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT TRANSMEM 48..69
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT TRANSMEM 81..104
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT TRANSMEM 111..130
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT TRANSMEM 150..175
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT TRANSMEM 187..206
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT TRANSMEM 492..513
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT TRANSMEM 583..605
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT TRANSMEM 696..714
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT TRANSMEM 734..760
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT TRANSMEM 781..800
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT DOMAIN 217..478
FT /note="CN hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS50263"
SQ SEQUENCE 805 AA; 86091 MW; 4496A37430E38AE7 CRC64;
MSGILASAAL SGLYVYDVAG IGWLLGFVAW VPWLLALSQR TSLRATLLCA YGMTVAYTAT
GFSWFGAAIG SYTQAGPATG VAVLLLAAPL FQPQIWVFAC VRFWATRQIG LWAGGLVAIA
AWVATEWLVP KMLGDTLGHG LHPSALLRQS AAWGGAAALT AALLITNECL ALVLARRAQG
AAAMARPLAI ALGLPLLLAG TGLVALQTAP VPSGKPLRMG LVQANIVDYE RLRQEKGAHA
VVREVLDTHF AMSYDAVVRQ HVDAVLWSET VYPTTFGHPK SADGAALDQE ILGIVHAAKV
PFVMGTYDLD AAGEYNAAAF VQADAGLIGM YRKTRLFPLT EAVPTWLDGP ALRRWLPWTG
HWLPGSGARV FPLRLADGRE IPVLPLICLD DVDTSLALQG ARLGAQAIVT LSNDSWFTTH
PQGAKLHQAV AAFRSIETGL PQFRVTTNGY SAAIDATGAI RVEAPMGARH LVVGDLPVPV
PVPTLMVRWG DWVGQASAAV VLMWALGTAW LGVARHPALV PHLELLRKRN DHSLPLNVRV
FVLPPWARLV AGVLRAFARG SLLWMGAAML LNDNLQSNTL AQIRLFATLF VAPELASWCV
LWAFAARATT DRDTLVVRSG ARSMRLALRD IAAVVPWRIP VPSRGVDVML ASGLRWPYAL
QVNDPAAFSR ALAASGGPAQ SAMALPHSPS RFGHPALKFV LLPTVLALVA FRLHQHIAYG
SSFGEYYTFG LRAYAISFGL WWAAWFMGVV LCAAALRAAI EVASGLIAFL QPAWMVPARA
VLERLGLLAL YAGLPGWLAL RALGG
//
