LPQL_MYCTU
ID LPQL_MYCTU Reviewed; 500 AA.
AC P96264; F2GMD5; I6XV80; L0T5B2;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Probable lipoprotein aminopeptidase LpqL {ECO:0000303|PubMed:9634230};
DE EC=3.4.11.1 {ECO:0000250|UniProtKB:Q9HZQ8};
DE AltName: Full=Leucine aminopeptidase;
DE AltName: Full=Lipoprotein LpqL;
DE Flags: Precursor;
GN Name=lpqL; OrderedLocusNames=Rv0418; ORFNames=LH57_02235;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27294 / TMC 102 / H37Rv;
RA Hazbon M.H., Riojas M.A., Damon A.M., Alalade R.O., Cantwell B.J.,
RA Monaco A., King S., Sohrabi A.;
RT "Phylogenetic analysis of Mycobacterial species using whole genome
RT sequences.";
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [4]
RP MASS SPECTROMETRY, DIACYLGLYCEROL AT CYS-25, PALMITOYLATION AT CYS-25,
RP LIPIDATION, POST-TRANSLATIONAL MODIFICATIONS, AND EXPRESSION IN M.BOVIS.
RC STRAIN=H37Rv;
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: An aminopeptidase; acts on free N-terminal amino groups with
CC a very strong preference for Leu in the first position.
CC {ECO:0000250|UniProtKB:Q9HZQ8}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa
CC is preferably Leu, but may be other amino acids including Pro
CC although not Arg or Lys, and Yaa may be Pro. Amino acid amides and
CC methyl esters are also readily hydrolyzed, but rates on arylamides
CC are exceedingly low.; EC=3.4.11.1;
CC Evidence={ECO:0000250|UniProtKB:Q9HZQ8};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P80561};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:P80561};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303,
CC ECO:0000305|PubMed:24093492}.
CC -!- PTM: Modified by Lgt on Cys-25 with an S-linked diacylglycerol with a
CC mixture of C16 and C19 fatty acids (palmitic and tuberculostearic
CC acid), signal peptide is removed by LspA, modified by Lnt with an
CC amide-linked mixture of C16 and C19 fatty acids, expressed in M.bovis
CC (PubMed:24093492). {ECO:0000269|PubMed:24093492}.
CC -!- MASS SPECTROMETRY: Mass=54200; Method=MALDI; Note=Expressed in M.bovis,
CC lipidated.; Evidence={ECO:0000269|PubMed:24093492};
CC -!- SIMILARITY: Belongs to the peptidase M28 family. M28A subfamily.
CC {ECO:0000305}.
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DR EMBL; CP009480; AIR13138.1; -; Genomic_DNA.
DR EMBL; AL123456; CCP43149.1; -; Genomic_DNA.
DR RefSeq; NP_214932.1; NC_000962.3.
DR RefSeq; WP_003402133.1; NZ_NVQJ01000002.1.
DR AlphaFoldDB; P96264; -.
DR SMR; P96264; -.
DR STRING; 83332.Rv0418; -.
DR MEROPS; M28.001; -.
DR MEROPS; M28.003; -.
DR PaxDb; P96264; -.
DR PRIDE; P96264; -.
DR DNASU; 886381; -.
DR GeneID; 886381; -.
DR KEGG; mtu:Rv0418; -.
DR PATRIC; fig|83332.111.peg.459; -.
DR TubercuList; Rv0418; -.
DR eggNOG; COG2234; Bacteria.
DR HOGENOM; CLU_024336_0_2_11; -.
DR OMA; YRVNNCV; -.
DR PhylomeDB; P96264; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005576; C:extracellular region; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008235; F:metalloexopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR CDD; cd03876; M28_SGAP_like; 1.
DR InterPro; IPR029514; Ape3.
DR InterPro; IPR045175; M28_fam.
DR InterPro; IPR041756; M28_SGAP-like.
DR InterPro; IPR003137; PA_domain.
DR InterPro; IPR007484; Peptidase_M28.
DR PANTHER; PTHR12147; PTHR12147; 1.
DR PANTHER; PTHR12147:SF17; PTHR12147:SF17; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW Aminopeptidase; Cell membrane; Hydrolase; Lipoprotein; Membrane;
KW Metal-binding; Palmitate; Protease; Reference proteome; Signal; Zinc.
FT SIGNAL 1..24
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 25..500
FT /note="Probable lipoprotein aminopeptidase LpqL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303,
FT ECO:0000305|PubMed:24093492"
FT /id="PRO_0000434901"
FT DOMAIN 140..231
FT /note="PA"
FT /evidence="ECO:0000255"
FT ACT_SITE 316
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 271
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 283
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 283
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 317
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 345
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 448
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT SITE 447
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT LIPID 25
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:24093492"
FT LIPID 25
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000269|PubMed:24093492"
SQ SEQUENCE 500 AA; 52042 MW; CD19BF47D8DB25EF CRC64;
MVNKSRMMPA VLAVAVVVAF LTTGCIRWST QSRPVVNGPA AAEFAVALRN RVSTDAMMAH
LSKLQDIANA NDGTRAVGTP GYQASVDYVV NTLRNSGFDV QTPEFSARVF KAEKGVVTLG
GNTVEARALE YSLGTPPDGV TGPLVAAPAD DSPGCSPSDY DRLPVSGAVV LVDRGVCPFA
QKEDAAAQRG AVALIIADNI DEQAMGGTLG ANTDVKIPVV SVTKSVGFQL RGQSGPTTVK
LTASTQSFKA RNVIAQTKTG SSANVVMAGA HLDSVPEGPG INDNGSGVAA VLETAVQLGN
SPHVSNAVRF AFWGAEEFGL IGSRNYVESL DIDALKGIAL YLNFDMLASP NPGYFTYDGD
QSLPLDARGQ PVVPEGSAGI ERTFVAYLKM AGKTAQDTSF DGRSDYDGFT LAGIPSGGLF
SGAEVKKSAE QAELWGGTAD EPFDPNYHQK TDTLDHIDRT ALGINGAGVA YAVGLYAQDL
GGPNGVPVMA DRTRHLIAKP
