LNT_SINMW
ID LNT_SINMW Reviewed; 531 AA.
AC Q52910; A6U5H4;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 3.
DT 25-MAY-2022, entry version 131.
DE RecName: Full=Apolipoprotein N-acyltransferase {ECO:0000255|HAMAP-Rule:MF_01148};
DE Short=ALP N-acyltransferase {ECO:0000255|HAMAP-Rule:MF_01148};
DE EC=2.3.1.269 {ECO:0000255|HAMAP-Rule:MF_01148};
GN Name=lnt {ECO:0000255|HAMAP-Rule:MF_01148}; Synonyms=actA;
GN OrderedLocusNames=Smed_0044;
OS Sinorhizobium medicae (strain WSM419) (Ensifer medicae).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=366394;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8868435; DOI=10.1099/13500872-142-3-601;
RA Tiwari R.P., Reeve W.G., Dilworth M.J., Glenn A.R.;
RT "An essential role for actA in acid tolerance of Rhizobium meliloti.";
RL Microbiology 142:601-610(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WSM419;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Reeve W.G.,
RA Richardson P.;
RT "Complete sequence of Sinorhizobium medicae WSM419 chromosome.";
RL Submitted (JUN-2007) 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:0000255|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:0000255|HAMAP-Rule:MF_01148};
CC -!- PATHWAY: Protein modification; lipoprotein biosynthesis (N-acyl
CC transfer). {ECO:0000255|HAMAP-Rule:MF_01148}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01148}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01148}.
CC -!- SIMILARITY: Belongs to the CN hydrolase family. Apolipoprotein N-
CC acyltransferase subfamily. {ECO:0000255|HAMAP-Rule:MF_01148,
CC ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB81867.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=ABR58904.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; L13845; AAB81867.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP000738; ABR58904.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_024325025.1; NC_009636.1.
DR RefSeq; YP_001325739.1; NC_009636.1.
DR AlphaFoldDB; Q52910; -.
DR SMR; Q52910; -.
DR STRING; 366394.Smed_0044; -.
DR EnsemblBacteria; ABR58904; ABR58904; Smed_0044.
DR GeneID; 61611171; -.
DR KEGG; smd:Smed_0044; -.
DR PATRIC; fig|366394.8.peg.3098; -.
DR eggNOG; COG0815; Bacteria.
DR HOGENOM; CLU_019563_3_1_5; -.
DR OMA; IPQSMKW; -.
DR OrthoDB; 1291198at2; -.
DR UniPathway; UPA00666; -.
DR Proteomes; UP000001108; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; -; 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 Pfam; PF00795; CN_hydrolase; 1.
DR Pfam; PF20154; LNT_N; 1.
DR SUPFAM; SSF56317; SSF56317; 1.
DR TIGRFAMs; TIGR00546; lnt; 1.
DR PROSITE; PS50263; CN_HYDROLASE; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Cell inner membrane; Cell membrane; Membrane; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..531
FT /note="Apolipoprotein N-acyltransferase"
FT /id="PRO_0000178090"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT TRANSMEM 34..54
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT TRANSMEM 69..89
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT TRANSMEM 136..156
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT TRANSMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT TRANSMEM 507..527
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT DOMAIN 243..493
FT /note="CN hydrolase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT ACT_SITE 287
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT ACT_SITE 351
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT ACT_SITE 405
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT CONFLICT 477..478
FT /note="Missing (in Ref. 1; AAB81867)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 531 AA; 57027 MW; 0B0A4C0954DACF78 CRC64;
MERLAGRIIL LSGVSRAFVG FLAGLLAVLA QPPFGIFAAA FVSFPVLVWL IDGVAPDPSD
GAFRRLRQPA AIGWSFGFGY FLGGLWWLGN ALLVEADAFA WAIPLAVVGL PAVLGVFYAL
AVVIARCLWS DGWGRIAALA LGFGIAEWLR GFVFTGFPWN AIGYAAMPMP LMMQSASVVN
LSTINMLAVF VFAAPALIWT GKGARTGLAI AVALFTAHIA FGFYRLAQPA PPSAAPQMAV
RVVQPVIDQA KKLDDRERAS IFEDHLSLTA APVQGGGKRP DIVVWPETSI PFILTDNPDA
LARIAEVLKD GQILVAGAVR AEDAGAGLPS RYYNSVYVID DRGQIIGAAD KVHLVPFGEY
LPYEDLLTSW GLSSIAASMP GGFSAARMRP VLTLPGGRRL YPMICYEAIF ADEVDANARL
ADVLLNVTND AWFGDTPGPR QHFHQAQLRA VETGIPMIRA ANTGISAVVD ARGVLVLVLG
YNYRGVLDTI LPGKLPTLTD VPTRSRIFWL SMAILSIVAS FSRFGFNIRK N
