PPMNT_MYCBP
ID PPMNT_MYCBP Reviewed; 874 AA.
AC A0A0H3M5A8;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 03-AUG-2022, entry version 30.
DE RecName: Full=Bifunctional apolipoprotein N-acyltransferase/polyprenol monophosphomannose synthase;
DE Includes:
DE RecName: Full=Apolipoprotein N-acyltransferase {ECO:0000303|PubMed:24093492};
DE Short=ALP N-acyltransferase {ECO:0000250|UniProtKB:P23930};
DE EC=2.3.1.269 {ECO:0000269|PubMed:24093492};
DE Includes:
DE RecName: Full=Polyprenol monophosphomannose synthase;
DE Short=PPM synthase;
DE Short=Polyprenol-P-Man synthase;
DE Short=Ppm1;
DE EC=2.4.1.- {ECO:0000250|UniProtKB:O53493};
DE AltName: Full=Dolichol-phosphate mannose synthase;
DE EC=2.4.1.83 {ECO:0000250|UniProtKB:O53493};
GN Name=lnt {ECO:0000303|PubMed:24093492}; Synonyms=ppm1 {ECO:0000305};
GN OrderedLocusNames=BCG_2070c;
OS Mycobacterium bovis (strain BCG / Pasteur 1173P2).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=410289;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCG / Pasteur 1173P2;
RX PubMed=17372194; DOI=10.1073/pnas.0700869104;
RA Brosch R., Gordon S.V., Garnier T., Eiglmeier K., Frigui W., Valenti P.,
RA Dos Santos S., Duthoy S., Lacroix C., Garcia-Pelayo C., Inwald J.K.,
RA Golby P., Garcia J.N., Hewinson R.G., Behr M.A., Quail M.A., Churcher C.,
RA Barrell B.G., Parkhill J., Cole S.T.;
RT "Genome plasticity of BCG and impact on vaccine efficacy.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:5596-5601(2007).
RN [2]
RP FUNCTION AS AN N-ACYLTRANSFERASE, AND DISRUPTION PHENOTYPE.
RC STRAIN=BCG / Pasteur 1173P2;
RX PubMed=24093492; DOI=10.1186/1471-2180-13-223;
RA Bruelle J.K., Tschumi A., Sander P.;
RT "Lipoproteins of slow-growing Mycobacteria carry three fatty acids and are
RT N-acylated by apolipoprotein N-acyltransferase BCG_2070c.";
RL BMC Microbiol. 13:223-223(2013).
CC -!- FUNCTION: Catalyzes the phospholipid dependent N-acylation of the N-
CC terminal cysteine of apolipoprotein, the last step in lipoprotein
CC maturation. {ECO:0000269|PubMed:24093492}.
CC -!- FUNCTION: Transfers mannose from GDP-mannose to lipid acceptors to form
CC polyprenol monophosphomannose (PPM). PMM is an alkai-stable sugar donor
CC which adds mannose-phosphate residues to triacylated-phosphatidyl-myo-
CC inositol mannosides (PIM2), eventually leading to generation of the
CC cell wall glycolipid lipoglycan modulins lipoarabinomannan (LAM) and
CC lipomannan (LM). {ECO:0000250|UniProtKB:O53493}.
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:0000269|PubMed:24093492};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dolichyl phosphate + GDP-alpha-D-mannose = a dolichyl beta-
CC D-mannosyl phosphate + GDP; Xref=Rhea:RHEA:21184, Rhea:RHEA-
CC COMP:9517, Rhea:RHEA-COMP:9527, ChEBI:CHEBI:57527, ChEBI:CHEBI:57683,
CC ChEBI:CHEBI:58189, ChEBI:CHEBI:58211; EC=2.4.1.83;
CC Evidence={ECO:0000250|UniProtKB:O53493};
CC -!- PATHWAY: Protein modification; lipoprotein biosynthesis (N-acyl
CC transfer).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- DOMAIN: Consists of 2 domains; the N-terminus (residues 1-593) has the
CC N-acyltransferase activity while the C-terminus (residues 594-874) has
CC polyprenol monophosphomannose (PPM) synthase activity.
CC {ECO:0000250|UniProtKB:O53493}.
CC -!- DISRUPTION PHENOTYPE: Loss of N-acylation of apolipoproteins.
CC {ECO:0000269|PubMed:24093492}.
CC -!- MISCELLANEOUS: In a number of other Mycobacteria, including M.avis,
CC M.leprae and M.smegmatis, these domains are encoded by 2 separate
CC adjacent genes. {ECO:0000305}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the CN hydrolase
CC family. Apolipoprotein N-acyltransferase subfamily.
CC -!- SIMILARITY: In the C-terminal section; belongs to the
CC glycosyltransferase 2 family. {ECO:0000305}.
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DR EMBL; AM408590; CAL72058.1; -; Genomic_DNA.
DR RefSeq; WP_003902238.1; NC_008769.1.
DR AlphaFoldDB; A0A0H3M5A8; -.
DR SMR; A0A0H3M5A8; -.
DR KEGG; mbb:BCG_2070c; -.
DR HOGENOM; CLU_014143_0_0_11; -.
DR OMA; ADEMPND; -.
DR BRENDA; 2.3.1.269; 3494.
DR UniPathway; UPA00666; -.
DR Proteomes; UP000001472; 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:0004582; F:dolichyl-phosphate beta-D-mannosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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 CDD; cd06442; DPM1_like; 1.
DR Gene3D; 3.60.110.10; -; 1.
DR Gene3D; 3.90.550.10; -; 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; IPR039528; DPM1-like.
DR InterPro; IPR001173; Glyco_trans_2-like.
DR InterPro; IPR045378; LNT_N.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR43398; PTHR43398; 1.
DR Pfam; PF00795; CN_hydrolase; 1.
DR Pfam; PF00535; Glycos_transf_2; 1.
DR Pfam; PF20154; LNT_N; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
DR SUPFAM; SSF56317; SSF56317; 1.
DR TIGRFAMs; TIGR00546; lnt; 1.
DR PROSITE; PS50263; CN_HYDROLASE; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Cell membrane; Hydrolase; Membrane; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..874
FT /note="Bifunctional apolipoprotein N-
FT acyltransferase/polyprenol monophosphomannose synthase"
FT /id="PRO_0000434583"
FT TRANSMEM 23..42
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:A0QZ13"
FT TRANSMEM 72..89
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:A0QZ13"
FT TRANSMEM 94..115
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:A0QZ13"
FT TRANSMEM 177..194
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:A0QZ13"
FT TRANSMEM 206..223
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:A0QZ13"
FT TRANSMEM 509..526
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:A0QZ13"
FT DOMAIN 241..497
FT /note="CN hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT REGION 1..593
FT /note="Apolipoprotein N-acyltransferase"
FT REGION 533..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 594..874
FT /note="Polyprenol monophosphomannose synthase"
FT REGION 852..874
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..551
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 294
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 359
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 409
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
SQ SEQUENCE 874 AA; 93824 MW; E00EADD2EC3238B4 CRC64;
MKLGAWVAAQ LPTTRTAVRT RLTRLVVSIV AGLLLYASFP PRNCWWAAVV ALALLAWVLT
HRATTPVGGL GYGLLFGLVF YVSLLPWIGE LVGPGPWLAL ATTCALFPGI FGLFAVVVRL
LPGWPIWFAV GWAAQEWLKS ILPFGGFPWG SVAFGQAEGP LLPLVQLGGV ALLSTGVALV
GCGLTAIALE IEKWWRTGGQ GDAPPAVVLP AACICLVLFA AIVVWPQVRH AGSGSGGEPT
VTVAVVQGNV PRLGLDFNAQ RRAVLDNHVE ETLRLAADVH AGLAQQPQFV IWPENSSDID
PFVNPDAGQR ISAAAEAIGA PILIGTLMDV PGRPRENPEW TNTAIVWNPG TGPADRHDKA
IVQPFGEYLP MPWLFRHLSG YADRAGHFVP GNGTGVVRIA GVPVGVATCW EVIFDRAPRK
SILGGAQLLT VPSNNATFNK TMSEQQLAFA KVRAVEHDRY VVVAGTTGIS AVIAPDGGEL
IRTDFFQPAY LDSQVRLKTR LTPATRWGPI LQWILVGAAA AVVLVAMRQN GWFPRPRRSE
PKGENDDSDA PPGRSEASGP PALSESDDEL IQPEQGGRHS SGFGRHRATS RSYMTTGQPA
PPAPGNRPSQ RVLVIIPTFN ERENLPVIHR RLTQACPAVH VLVVDDSSPD GTGQLADELA
QADPGRTHVM HRTAKNGLGA AYLAGFAWGL SREYSVLVEM DADGSHAPEQ LQRLLDAVDA
GADLAIGSRY VAGGTVRNWP WRRLVLSKTA NTYSRLALGI GIHDITAGYR AYRREALEAI
DLDGVDSKGY CFQIDLTWRT VSNGFVVTEV PITFTERELG VSKMSGSNIR EALVKVARWG
IEGRLSRSDH ARARPDIARP GAGGSRVSRA DVTE
