LPQN_MYCTU
ID LPQN_MYCTU Reviewed; 228 AA.
AC O53780; F2GMM8; I6WYS7; Q7D9L3;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Lipoprotein LpqN {ECO:0000305};
DE Flags: Precursor;
GN Name=lpqN {ECO:0000303|PubMed:30118682};
GN OrderedLocusNames=Rv0583c {ECO:0000312|EMBL:CCP43321.1};
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 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 [3]
RP FUNCTION IN VIRULENCE, INTERACTION WITH HOST CBL, SUBCELLULAR LOCATION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=30118682; DOI=10.1016/j.molcel.2018.07.010;
RA Penn B.H., Netter Z., Johnson J.R., Von Dollen J., Jang G.M., Johnson T.,
RA Ohol Y.M., Maher C., Bell S.L., Geiger K., Golovkine G., Du X., Choi A.,
RA Parry T., Mohapatra B.C., Storck M.D., Band H., Chen C., Jaeger S.,
RA Shales M., Portnoy D.A., Hernandez R., Coscoy L., Cox J.S., Krogan N.J.;
RT "An Mtb-human protein-protein interaction map identifies a switch between
RT host antiviral and antibacterial responses.";
RL Mol. Cell 71:637-648(2018).
RN [4]
RP FUNCTION IN VIRULENCE.
RX PubMed=30118676; DOI=10.1016/j.molcel.2018.08.006;
RA Eoh H., Jung J.U.;
RT "Bacterial protein reshapes host defense toward antiviral responses.";
RL Mol. Cell 71:483-484(2018).
RN [5] {ECO:0007744|PDB:6E5D, ECO:0007744|PDB:6E5F, ECO:0007744|PDB:6MNA}
RP X-RAY CRYSTALLOGRAPHY (1.37 ANGSTROMS) OF APOPROTEIN AND IN COMPLEXES WITH
RP DODECYL TREHALOSE AND TREHALOSE 6-DECANOATE, FUNCTION, INTERACTION WITH
RP MMPL2; MMPL11 AND AG85, AND DISRUPTION PHENOTYPE.
RX PubMed=31471317; DOI=10.1074/jbc.ra119.008781;
RA Melly G.C., Stokas H., Dunaj J.L., Hsu F.F., Rajavel M., Su C.C., Yu E.W.,
RA Purdy G.E.;
RT "Structural and functional evidence that lipoprotein LpqN supports cell
RT envelope biogenesis in Mycobacterium tuberculosis.";
RL J. Biol. Chem. 294:15711-15723(2019).
CC -!- FUNCTION: Involved in cell envelope biogenesis. May act as a membrane
CC fusion protein, connecting MmpL transporters with periplasmic proteins,
CC and play a role in cell envelope lipid changes during biofilm
CC maturation. {ECO:0000269|PubMed:31471317}.
CC -!- FUNCTION: Is also a virulence factor required for intracellular
CC survival (PubMed:30118682). Associates with CBL, a host ubiquitin
CC ligase, and probably blocks the normal functions of CBL and disturbs
CC CBL-mediated antibacterial activity (PubMed:30118682). Interaction
CC counteracts antibacterial defense but causes a reciprocal enhancement
CC of antiviral defense (PubMed:30118676, PubMed:30118682).
CC {ECO:0000269|PubMed:30118682, ECO:0000305|PubMed:30118676}.
CC -!- SUBUNIT: Interacts with the periplasmic loop domains of the mycolate
CC transporters MmpL3 and MmpL11. Also interacts with secreted cell
CC envelope biosynthetic enzymes such as Ag85A. These interactions are
CC weak and may require a putative mycobacterial adapter protein or
CC molecule (PubMed:31471317). Interacts with human ubiquitin ligase CBL
CC (PubMed:30118682). {ECO:0000269|PubMed:30118682,
CC ECO:0000269|PubMed:31471317}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
CC Secreted {ECO:0000269|PubMed:30118682}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutant grows at a normal rate and has a
CC normal cell envelope lipid profile, but shows altered lipid profiles
CC during biofilm maturation (PubMed:31471317). Mutant is attenuated in
CC macrophages, but growth is restored when host CBL is removed
CC (PubMed:30118682). {ECO:0000269|PubMed:30118682,
CC ECO:0000269|PubMed:31471317}.
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DR EMBL; AL123456; CCP43321.1; -; Genomic_DNA.
DR RefSeq; NP_215097.1; NC_000962.3.
DR RefSeq; WP_003403052.1; NZ_NVQJ01000033.1.
DR PDB; 6E5D; X-ray; 1.65 A; A=1-228.
DR PDB; 6E5F; X-ray; 1.37 A; A=1-228.
DR PDB; 6MNA; X-ray; 1.75 A; A=1-228.
DR PDBsum; 6E5D; -.
DR PDBsum; 6E5F; -.
DR PDBsum; 6MNA; -.
DR AlphaFoldDB; O53780; -.
DR SMR; O53780; -.
DR STRING; 83332.Rv0583c; -.
DR PaxDb; O53780; -.
DR PRIDE; O53780; -.
DR DNASU; 887733; -.
DR GeneID; 887733; -.
DR KEGG; mtu:Rv0583c; -.
DR PATRIC; fig|83332.111.peg.644; -.
DR TubercuList; Rv0583c; -.
DR eggNOG; ENOG5034BUD; Bacteria.
DR OMA; GFDATQI; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005576; C:extracellular region; HDA:MTBBASE.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR InterPro; IPR019674; Lipoprotein_LpqN/LpqT-like.
DR Pfam; PF10738; Lpp-LpqN; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Cell wall biogenesis/degradation; Lipoprotein;
KW Membrane; Palmitate; Reference proteome; Secreted; Signal; Virulence.
FT SIGNAL 1..19
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 20..228
FT /note="Lipoprotein LpqN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT /id="PRO_5010295865"
FT REGION 26..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 20
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 20
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT HELIX 61..66
FT /evidence="ECO:0007829|PDB:6E5F"
FT TURN 67..69
FT /evidence="ECO:0007829|PDB:6E5F"
FT STRAND 70..74
FT /evidence="ECO:0007829|PDB:6E5F"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:6E5F"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:6E5F"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:6E5F"
FT STRAND 106..111
FT /evidence="ECO:0007829|PDB:6E5F"
FT STRAND 120..131
FT /evidence="ECO:0007829|PDB:6E5F"
FT HELIX 134..140
FT /evidence="ECO:0007829|PDB:6E5F"
FT HELIX 143..146
FT /evidence="ECO:0007829|PDB:6E5F"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:6E5F"
FT STRAND 158..162
FT /evidence="ECO:0007829|PDB:6E5F"
FT STRAND 165..176
FT /evidence="ECO:0007829|PDB:6E5F"
FT STRAND 179..192
FT /evidence="ECO:0007829|PDB:6E5F"
FT STRAND 195..206
FT /evidence="ECO:0007829|PDB:6E5F"
FT HELIX 207..209
FT /evidence="ECO:0007829|PDB:6E5F"
FT HELIX 210..223
FT /evidence="ECO:0007829|PDB:6E5F"
FT STRAND 225..227
FT /evidence="ECO:0007829|PDB:6E5F"
SQ SEQUENCE 228 AA; 23682 MW; 1F0821C9E9947526 CRC64;
MKHFTAAVAT VALSLALAGC SFNIKTDSAP TTSPTTTSPT TSTTTTSATT SAQAAGPNYT
IADYIRDNHI QETPVHHGDP GSPTIDLPVP DDWRLLPESS RAPYGGIVYT QPADPNDPPT
IVAILSKLTG DIDPAKVLQF APGELKNLPG FQGSGDGSAA TLGGFSAWQL GGSYSKNGKL
RTVAQKTVVI PSQGAVFVLQ LNADALDDET MTLMDAANVI DEQTTITP
