LPQW_MYCS2
ID LPQW_MYCS2 Reviewed; 627 AA.
AC A0R2I8; I7GDK5;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 86.
DE RecName: Full=Probable monoacyl phosphatidylinositol tetramannoside-binding protein LpqW;
DE Flags: Precursor;
GN OrderedLocusNames=MSMEG_5130, MSMEI_5002;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
RN [4]
RP IDENTIFICATION.
RX PubMed=16455649; DOI=10.1074/jbc.m511709200;
RA Kovacevic S., Anderson D., Morita Y.S., Patterson J., Haites R.,
RA McMillan B.N., Coppel R., McConville M.J., Billman-Jacobe H.;
RT "Identification of a novel protein with a role in lipoarabinomannan
RT biosynthesis in mycobacteria.";
RL J. Biol. Chem. 281:9011-9017(2006).
RN [5]
RP FUNCTION IN THE LIPOARABINOMANNANS BIOSYNTHESIS.
RX PubMed=18344361; DOI=10.1128/jb.00200-08;
RA Crellin P.K., Kovacevic S., Martin K.L., Brammananth R., Morita Y.S.,
RA Billman-Jacobe H., McConville M.J., Coppel R.L.;
RT "Mutations in pimE restore lipoarabinomannan synthesis and growth in a
RT Mycobacterium smegmatis lpqW mutant.";
RL J. Bacteriol. 190:3690-3699(2008).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 28-627.
RX PubMed=16698034; DOI=10.1016/j.jmb.2006.04.012;
RA Marland Z., Beddoe T., Zaker-Tabrizi L., Lucet I.S., Brammananth R.,
RA Whisstock J.C., Wilce M.C., Coppel R.L., Crellin P.K., Rossjohn J.;
RT "Hijacking of a substrate-binding protein scaffold for use in mycobacterial
RT cell wall biosynthesis.";
RL J. Mol. Biol. 359:983-997(2006).
CC -!- FUNCTION: May directly or indirectly regulate the accessibility of the
CC key branch point intermediate, monoacyl phosphatidylinositol
CC tetramannoside (AcPIM4), to the elongating alpha-1,6
CC mannosyltransferases which could regulate the lipoarabinomannans (LAMs)
CC biosynthesis. {ECO:0000269|PubMed:18344361}.
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylinositol metabolism.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 5 family.
CC {ECO:0000305}.
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DR EMBL; CP000480; ABK73363.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP41446.1; -; Genomic_DNA.
DR RefSeq; WP_011730336.1; NZ_SIJM01000038.1.
DR RefSeq; YP_889376.1; NC_008596.1.
DR PDB; 2GRV; X-ray; 2.40 A; A/B/C=28-627.
DR PDBsum; 2GRV; -.
DR AlphaFoldDB; A0R2I8; -.
DR SMR; A0R2I8; -.
DR STRING; 246196.MSMEI_5002; -.
DR PRIDE; A0R2I8; -.
DR EnsemblBacteria; ABK73363; ABK73363; MSMEG_5130.
DR EnsemblBacteria; AFP41446; AFP41446; MSMEI_5002.
DR GeneID; 66736448; -.
DR KEGG; msg:MSMEI_5002; -.
DR KEGG; msm:MSMEG_5130; -.
DR PATRIC; fig|246196.19.peg.5006; -.
DR eggNOG; COG0747; Bacteria.
DR OMA; TPRVMQL; -.
DR OrthoDB; 162819at2; -.
DR UniPathway; UPA00949; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; Chromosome.
DR GO; GO:0009247; P:glycolipid biosynthetic process; IDA:UniProtKB.
DR GO; GO:0046488; P:phosphatidylinositol metabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR InterPro; IPR039424; SBP_5.
DR InterPro; IPR000914; SBP_5_dom.
DR PANTHER; PTHR30290; PTHR30290; 1.
DR Pfam; PF00496; SBP_bac_5; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Lipid biosynthesis; Lipid metabolism;
KW Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome;
KW Signal; Virulence.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..627
FT /note="Probable monoacyl phosphatidylinositol
FT tetramannoside-binding protein LpqW"
FT /id="PRO_0000393728"
FT REGION 29..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 501..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..524
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 55..61
FT /evidence="ECO:0007829|PDB:2GRV"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:2GRV"
FT HELIX 77..86
FT /evidence="ECO:0007829|PDB:2GRV"
FT STRAND 90..95
FT /evidence="ECO:0007829|PDB:2GRV"
FT STRAND 102..107
FT /evidence="ECO:0007829|PDB:2GRV"
FT TURN 109..111
FT /evidence="ECO:0007829|PDB:2GRV"
FT STRAND 112..119
FT /evidence="ECO:0007829|PDB:2GRV"
FT TURN 120..123
FT /evidence="ECO:0007829|PDB:2GRV"
FT STRAND 124..129
FT /evidence="ECO:0007829|PDB:2GRV"
FT HELIX 143..155
FT /evidence="ECO:0007829|PDB:2GRV"
FT HELIX 165..167
FT /evidence="ECO:0007829|PDB:2GRV"
FT STRAND 168..174
FT /evidence="ECO:0007829|PDB:2GRV"
FT TURN 175..178
FT /evidence="ECO:0007829|PDB:2GRV"
FT STRAND 179..186
FT /evidence="ECO:0007829|PDB:2GRV"
FT HELIX 191..193
FT /evidence="ECO:0007829|PDB:2GRV"
FT HELIX 201..204
FT /evidence="ECO:0007829|PDB:2GRV"
FT HELIX 210..213
FT /evidence="ECO:0007829|PDB:2GRV"
FT STRAND 224..232
FT /evidence="ECO:0007829|PDB:2GRV"
FT TURN 233..236
FT /evidence="ECO:0007829|PDB:2GRV"
FT STRAND 237..242
FT /evidence="ECO:0007829|PDB:2GRV"
FT STRAND 247..249
FT /evidence="ECO:0007829|PDB:2GRV"
FT STRAND 254..260
FT /evidence="ECO:0007829|PDB:2GRV"
FT HELIX 264..272
FT /evidence="ECO:0007829|PDB:2GRV"
FT STRAND 278..281
FT /evidence="ECO:0007829|PDB:2GRV"
FT HELIX 285..292
FT /evidence="ECO:0007829|PDB:2GRV"
FT STRAND 298..312
FT /evidence="ECO:0007829|PDB:2GRV"
FT HELIX 317..319
FT /evidence="ECO:0007829|PDB:2GRV"
FT HELIX 322..330
FT /evidence="ECO:0007829|PDB:2GRV"
FT HELIX 334..342
FT /evidence="ECO:0007829|PDB:2GRV"
FT STRAND 344..346
FT /evidence="ECO:0007829|PDB:2GRV"
FT STRAND 354..356
FT /evidence="ECO:0007829|PDB:2GRV"
FT HELIX 373..382
FT /evidence="ECO:0007829|PDB:2GRV"
FT STRAND 386..388
FT /evidence="ECO:0007829|PDB:2GRV"
FT STRAND 408..411
FT /evidence="ECO:0007829|PDB:2GRV"
FT STRAND 417..423
FT /evidence="ECO:0007829|PDB:2GRV"
FT HELIX 427..442
FT /evidence="ECO:0007829|PDB:2GRV"
FT STRAND 446..452
FT /evidence="ECO:0007829|PDB:2GRV"
FT HELIX 454..459
FT /evidence="ECO:0007829|PDB:2GRV"
FT TURN 460..465
FT /evidence="ECO:0007829|PDB:2GRV"
FT STRAND 468..475
FT /evidence="ECO:0007829|PDB:2GRV"
FT HELIX 480..488
FT /evidence="ECO:0007829|PDB:2GRV"
FT TURN 491..493
FT /evidence="ECO:0007829|PDB:2GRV"
FT HELIX 554..556
FT /evidence="ECO:0007829|PDB:2GRV"
FT HELIX 557..564
FT /evidence="ECO:0007829|PDB:2GRV"
FT HELIX 570..583
FT /evidence="ECO:0007829|PDB:2GRV"
FT STRAND 587..599
FT /evidence="ECO:0007829|PDB:2GRV"
FT STRAND 603..605
FT /evidence="ECO:0007829|PDB:2GRV"
FT TURN 612..614
FT /evidence="ECO:0007829|PDB:2GRV"
FT HELIX 620..622
FT /evidence="ECO:0007829|PDB:2GRV"
SQ SEQUENCE 627 AA; 65675 MW; 9A73036C0814365E CRC64;
MGVPTPARRA RLTFGALLAV PTLLLGGCTV SPPPAPQSTE TTETTPPPPP KAPTQIIMAI
DSIGPGFNPH LLSDQSPVNA AIASLVLPSS FRPVPDPTSP TGSRWELDTT LLESAEVTNE
NPFTVTYKIR PEAQWTDNAP IAADDYWYLW RQMVSQPGVV DPAGYDLITG VQSVEGGKQA
VVTFSQPYPA WRELFNDILP AHIVKDIPGG FGAGLARAMP VTGGQFRVET IDPQRDEILL
ARNDRFWSVP AKPDLVLFRR GGAPAALADS IRNGDTQVAQ VHGGAATFAQ LSAIPDVRTA
RIVTPRVMQL TLRAQQPKLA DPQVRKAILG LIDVDLLASV GAGDDNTVTL AQAQVRSPSD
PGYVPTAPPA MTRDDALELL RDAGYVSEPV PPPDNTADDP PPDNGRERIV KDGVPLTIVL
GVASNDPTSV AVANTAADQL RNVGIDASVL ALDPVALYGD ALVNNRVDAV VGWRQAGGDL
ATVLASRYGC RALEATPVAT AVPGPATTTS QAPTTTTTTT PPATTTPTPT APIPAPESGE
LVQAPSNITG ICDRSIQPRI DAALDGTDDI ADVIQAVEPR LWNMATVLPI LQDTTIVAAG
PSVQNVSLTG AVPVGIVGDA GDWTKTK
