ID D2PMV4_KRIFD Unreviewed; 522 AA.
AC D2PMV4;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 79.
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 OrderedLocusNames=Kfla_3599 {ECO:0000313|EMBL:ADB32656.1};
OS Kribbella flavida (strain DSM 17836 / JCM 10339 / NBRC 14399).
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Kribbellaceae; Kribbella.
OX NCBI_TaxID=479435 {ECO:0000313|EMBL:ADB32656.1, ECO:0000313|Proteomes:UP000007967};
RN [1] {ECO:0000313|Proteomes:UP000007967}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17836 / JCM 10339 / NBRC 14399
RC {ECO:0000313|Proteomes:UP000007967};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA Saunders E., Brettin T., Detter J.C., Han C., Larimer F., Land M.,
RA Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D.,
RA Pukall R., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Kribbella flavida DSM 17836.";
RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADB32656.1, ECO:0000313|Proteomes:UP000007967}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17836 / JCM 10339 / NBRC 14399
RC {ECO:0000313|Proteomes:UP000007967};
RX PubMed=21304701;
RA Pukall R., Lapidus A., Glavina Del Rio T., Copeland A., Tice H.,
RA Cheng J.-F., Lucas S., Chen F., Nolan M., LaButti K., Pati A., Ivanova N.,
RA Mavrommatis K., Mikhailova N., Pitluck S., Bruce D., Goodwin L., Land M.,
RA Hauser L., Chang Y.-J., Jeffries C.D., Chen A., Palaniappan K., Chain P.,
RA Rohde M., Goeker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.-P., Brettin T.;
RT "Complete genome sequence of Kribbella flavida type strain (IFO 14399).";
RL Stand. Genomic Sci. 2:186-193(2010).
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}.
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DR EMBL; CP001736; ADB32656.1; -; Genomic_DNA.
DR RefSeq; WP_012921212.1; NC_013729.1.
DR AlphaFoldDB; D2PMV4; -.
DR STRING; 479435.Kfla_3599; -.
DR KEGG; kfl:Kfla_3599; -.
DR eggNOG; COG0815; Bacteria.
DR HOGENOM; CLU_019563_0_1_11; -.
DR OrthoDB; 9804277at2; -.
DR UniPathway; UPA00666; -.
DR Proteomes; UP000007967; Chromosome.
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:ADB32656.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01148};
KW Reference proteome {ECO:0000313|Proteomes:UP000007967};
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 7..27
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT TRANSMEM 33..51
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT TRANSMEM 58..76
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT TRANSMEM 82..102
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT TRANSMEM 109..130
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT TRANSMEM 150..174
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT TRANSMEM 181..203
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT TRANSMEM 479..498
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT DOMAIN 212..466
FT /note="CN hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS50263"
FT REGION 299..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 502..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..522
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 522 AA; 55130 MW; 353A125633C86A9A CRC64;
MERLRALVRL VPRILVAVGA GALLGLAFEP HDYPWLAVVA VPLFLAALNG VSVKGGILVG
AGFGITYYAV LVPWLSVIGG DAAIALAILE GLFYAVFGAL ASQVLKHKLW MLWIPCLWVA
TEFATASVPF GGFPWGRLAW AFTDSPLGRL AAVVGIAGLS FVVALLGVLA YAAVLRRRSG
FGLRAVALVA GLAIVGVSFL ISLPTDGNGK SVTAAMVQGN VPGKGLEFLG RARTVTKNHV
TATLDLQKQV EAGSQVKPDL VIWPENSTDI DPYKDPETRR DIETAVQAVK VPILVGAVTE
GPGPNERQTT GIVWDPATGP GQRYAKRHPV PFGEYIPFRD QLLPYIKRLE MVGRQTAPGV
GPGLMPINGV LYGDLICFEL AYDSVVSDLA KGGAQILVVQ TNNATYGGTG QPEQQFAITR
MRAIETGRTV LIASTSGISG VVRPDGTVEH KSGQFVPDVY VASVPVRDAQ TLATRLGGWP
QWILTGLGII GAVLALAARR NRRPADPGTP PVATPSAEKV PV
//
