THPA_MYCS2
ID THPA_MYCS2 Reviewed; 349 AA.
AC A0QYB5;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=D-threitol-binding protein {ECO:0000303|PubMed:26560079};
DE Flags: Precursor;
GN Name=thpA {ECO:0000303|PubMed:26560079};
GN OrderedLocusNames=MSMEG_3599 {ECO:0000312|EMBL:ABK75932.1},
GN MSMEI_3516 {ECO:0000312|EMBL:AFP39979.1};
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 X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 25-349 IN COMPLEX WITH
RP D-THREITOL, FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=26560079; DOI=10.1021/jacs.5b08968;
RA Huang H., Carter M.S., Vetting M.W., Al-Obaidi N., Patskovsky Y.,
RA Almo S.C., Gerlt J.A.;
RT "A general strategy for the discovery of metabolic pathways: D-threitol, L-
RT threitol, and erythritol utilization in Mycobacterium smegmatis.";
RL J. Am. Chem. Soc. 137:14570-14573(2015).
CC -!- FUNCTION: Part of an ABC transporter complex involved in D-threitol
CC import. Binds D-threitol. Functions in the transport for the
CC degradation pathway of D-threitol, that allows M.smegmatis to grow on
CC this compound as the sole carbon source. {ECO:0000269|PubMed:26560079}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
CC -!- INDUCTION: Highly up-regulated during growth on D-threitol relative to
CC growth on glycerol. {ECO:0000269|PubMed:26560079}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are defective for growth
CC with D-threitol. {ECO:0000269|PubMed:26560079}.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 2 family.
CC {ECO:0000305}.
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DR EMBL; CP000480; ABK75932.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP39979.1; -; Genomic_DNA.
DR RefSeq; WP_011729193.1; NZ_SIJM01000008.1.
DR RefSeq; YP_887903.1; NC_008596.1.
DR PDB; 4RSM; X-ray; 1.60 A; A/B/C/D=25-349.
DR PDBsum; 4RSM; -.
DR AlphaFoldDB; A0QYB5; -.
DR SMR; A0QYB5; -.
DR STRING; 246196.MSMEI_3516; -.
DR PRIDE; A0QYB5; -.
DR EnsemblBacteria; ABK75932; ABK75932; MSMEG_3599.
DR EnsemblBacteria; AFP39979; AFP39979; MSMEI_3516.
DR GeneID; 66734985; -.
DR KEGG; msg:MSMEI_3516; -.
DR KEGG; msm:MSMEG_3599; -.
DR PATRIC; fig|246196.19.peg.3549; -.
DR eggNOG; COG1879; Bacteria.
DR OMA; MWDAAMA; -.
DR OrthoDB; 1378040at2; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IDA:UniProtKB.
DR GO; GO:0008643; P:carbohydrate transport; IGC:UniProtKB.
DR GO; GO:0009758; P:carbohydrate utilization; IMP:UniProtKB.
DR GO; GO:0071322; P:cellular response to carbohydrate stimulus; IDA:UniProtKB.
DR InterPro; IPR028082; Peripla_BP_I.
DR InterPro; IPR025997; SBP_2_dom.
DR Pfam; PF13407; Peripla_BP_4; 1.
DR SUPFAM; SSF53822; SSF53822; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Lipoprotein; Membrane; Palmitate;
KW Reference proteome; Signal; Sugar transport; Transport.
FT SIGNAL 1..22
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 23..349
FT /note="D-threitol-binding protein"
FT /id="PRO_5005658569"
FT BINDING 42
FT /ligand="D-threitol"
FT /ligand_id="ChEBI:CHEBI:48300"
FT /evidence="ECO:0000269|PubMed:26560079,
FT ECO:0007744|PDB:4RSM"
FT BINDING 121
FT /ligand="D-threitol"
FT /ligand_id="ChEBI:CHEBI:48300"
FT /evidence="ECO:0000269|PubMed:26560079,
FT ECO:0007744|PDB:4RSM"
FT BINDING 173
FT /ligand="D-threitol"
FT /ligand_id="ChEBI:CHEBI:48300"
FT /evidence="ECO:0000269|PubMed:26560079,
FT ECO:0007744|PDB:4RSM"
FT BINDING 224
FT /ligand="D-threitol"
FT /ligand_id="ChEBI:CHEBI:48300"
FT /evidence="ECO:0000269|PubMed:26560079,
FT ECO:0007744|PDB:4RSM"
FT BINDING 249
FT /ligand="D-threitol"
FT /ligand_id="ChEBI:CHEBI:48300"
FT /evidence="ECO:0000269|PubMed:26560079,
FT ECO:0007744|PDB:4RSM"
FT BINDING 269
FT /ligand="D-threitol"
FT /ligand_id="ChEBI:CHEBI:48300"
FT /evidence="ECO:0000269|PubMed:26560079,
FT ECO:0007744|PDB:4RSM"
FT LIPID 23
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 23
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT STRAND 35..42
FT /evidence="ECO:0007829|PDB:4RSM"
FT HELIX 46..61
FT /evidence="ECO:0007829|PDB:4RSM"
FT STRAND 64..70
FT /evidence="ECO:0007829|PDB:4RSM"
FT HELIX 75..87
FT /evidence="ECO:0007829|PDB:4RSM"
FT STRAND 91..96
FT /evidence="ECO:0007829|PDB:4RSM"
FT HELIX 104..112
FT /evidence="ECO:0007829|PDB:4RSM"
FT STRAND 117..122
FT /evidence="ECO:0007829|PDB:4RSM"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:4RSM"
FT HELIX 137..152
FT /evidence="ECO:0007829|PDB:4RSM"
FT STRAND 156..162
FT /evidence="ECO:0007829|PDB:4RSM"
FT HELIX 168..183
FT /evidence="ECO:0007829|PDB:4RSM"
FT STRAND 187..194
FT /evidence="ECO:0007829|PDB:4RSM"
FT HELIX 199..213
FT /evidence="ECO:0007829|PDB:4RSM"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:4RSM"
FT STRAND 219..224
FT /evidence="ECO:0007829|PDB:4RSM"
FT HELIX 225..237
FT /evidence="ECO:0007829|PDB:4RSM"
FT HELIX 252..260
FT /evidence="ECO:0007829|PDB:4RSM"
FT STRAND 261..268
FT /evidence="ECO:0007829|PDB:4RSM"
FT HELIX 271..286
FT /evidence="ECO:0007829|PDB:4RSM"
FT STRAND 301..303
FT /evidence="ECO:0007829|PDB:4RSM"
FT TURN 304..306
FT /evidence="ECO:0007829|PDB:4RSM"
FT HELIX 307..314
FT /evidence="ECO:0007829|PDB:4RSM"
FT TURN 315..317
FT /evidence="ECO:0007829|PDB:4RSM"
FT HELIX 318..323
FT /evidence="ECO:0007829|PDB:4RSM"
FT HELIX 325..335
FT /evidence="ECO:0007829|PDB:4RSM"
SQ SEQUENCE 349 AA; 36350 MW; B41D233996B74DF6 CRC64;
MRLGTTAFAI ASATALGLGL TACGAGDPAA NSDTTRIGVT VYDMSSFITA GKEGMDAYAK
DNNIELIWNS ANLDVSTQAS QVDSMINQGV DAIIVVPVQA DSLAPQVASA KAKGIPLVPV
NAALDSKDIA GNVQPDDVAA GAQEMQMMAD RLGGKGNIVI LQGPLGQSGE LDRSKGIEQV
LAKYPDIKVL AKDTANWKRD EAVNKMKNWI SGFGPQIDGV VAQNDDMGLG ALQALKESGR
TGVPIVGIDG IEDGLNAVKS GDFIGTSLQN GTVELAAGLA VANRLAKGEP VNKEPVYIMP
AITKDNVDVA IEHVVTERQQ FLDGLTELIN KNLETGDIAY EGIPGQKQP
