XYPA_MYCS2
ID XYPA_MYCS2 Reviewed; 349 AA.
AC A0QYB3;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Xylitol-binding protein {ECO:0000303|PubMed:26560079};
DE Flags: Precursor;
GN Name=xypA {ECO:0000303|PubMed:26560079};
GN OrderedLocusNames=MSMEG_3598 {ECO:0000312|EMBL:ABK73733.1},
GN MSMEI_3515 {ECO:0000312|EMBL:AFP39978.1};
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 (1.40 ANGSTROMS) OF 25-349 IN COMPLEX WITH XYLITOL,
RP FUNCTION, AND INDUCTION.
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 likely involved in xylitol
CC import. Binds xylitol. {ECO:0000269|PubMed:26560079}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
CC -!- INDUCTION: Up-regulated during growth on D-threitol relative to growth
CC on glycerol. {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; ABK73733.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP39978.1; -; Genomic_DNA.
DR RefSeq; WP_003895054.1; NZ_SIJM01000008.1.
DR RefSeq; YP_887901.1; NC_008596.1.
DR PDB; 4RS3; X-ray; 1.40 A; A=25-349.
DR PDB; 5HKO; X-ray; 1.20 A; A=25-349.
DR PDBsum; 4RS3; -.
DR PDBsum; 5HKO; -.
DR AlphaFoldDB; A0QYB3; -.
DR SMR; A0QYB3; -.
DR STRING; 246196.MSMEI_3515; -.
DR PRIDE; A0QYB3; -.
DR EnsemblBacteria; ABK73733; ABK73733; MSMEG_3598.
DR EnsemblBacteria; AFP39978; AFP39978; MSMEI_3515.
DR GeneID; 66734984; -.
DR KEGG; msg:MSMEI_3515; -.
DR KEGG; msm:MSMEG_3598; -.
DR PATRIC; fig|246196.19.peg.3548; -.
DR eggNOG; COG1879; Bacteria.
DR OMA; QAVFAHN; -.
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: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="Xylitol-binding protein"
FT /id="PRO_5005658518"
FT BINDING 42
FT /ligand="xylitol"
FT /ligand_id="ChEBI:CHEBI:17151"
FT /evidence="ECO:0000269|PubMed:26560079,
FT ECO:0007744|PDB:4RS3"
FT BINDING 121
FT /ligand="xylitol"
FT /ligand_id="ChEBI:CHEBI:17151"
FT /evidence="ECO:0000269|PubMed:26560079,
FT ECO:0007744|PDB:4RS3"
FT BINDING 173
FT /ligand="xylitol"
FT /ligand_id="ChEBI:CHEBI:17151"
FT /evidence="ECO:0000269|PubMed:26560079,
FT ECO:0007744|PDB:4RS3"
FT BINDING 224
FT /ligand="xylitol"
FT /ligand_id="ChEBI:CHEBI:17151"
FT /evidence="ECO:0000269|PubMed:26560079,
FT ECO:0007744|PDB:4RS3"
FT BINDING 249
FT /ligand="xylitol"
FT /ligand_id="ChEBI:CHEBI:17151"
FT /evidence="ECO:0000269|PubMed:26560079,
FT ECO:0007744|PDB:4RS3"
FT BINDING 269
FT /ligand="xylitol"
FT /ligand_id="ChEBI:CHEBI:17151"
FT /evidence="ECO:0000269|PubMed:26560079,
FT ECO:0007744|PDB:4RS3"
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:5HKO"
FT HELIX 46..61
FT /evidence="ECO:0007829|PDB:5HKO"
FT STRAND 64..70
FT /evidence="ECO:0007829|PDB:5HKO"
FT HELIX 75..87
FT /evidence="ECO:0007829|PDB:5HKO"
FT STRAND 91..96
FT /evidence="ECO:0007829|PDB:5HKO"
FT HELIX 104..112
FT /evidence="ECO:0007829|PDB:5HKO"
FT STRAND 117..122
FT /evidence="ECO:0007829|PDB:5HKO"
FT STRAND 130..135
FT /evidence="ECO:0007829|PDB:5HKO"
FT HELIX 137..152
FT /evidence="ECO:0007829|PDB:5HKO"
FT STRAND 156..162
FT /evidence="ECO:0007829|PDB:5HKO"
FT HELIX 168..181
FT /evidence="ECO:0007829|PDB:5HKO"
FT STRAND 187..194
FT /evidence="ECO:0007829|PDB:5HKO"
FT HELIX 199..213
FT /evidence="ECO:0007829|PDB:5HKO"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:5HKO"
FT STRAND 219..224
FT /evidence="ECO:0007829|PDB:5HKO"
FT HELIX 225..237
FT /evidence="ECO:0007829|PDB:5HKO"
FT HELIX 252..259
FT /evidence="ECO:0007829|PDB:5HKO"
FT STRAND 262..268
FT /evidence="ECO:0007829|PDB:5HKO"
FT HELIX 271..286
FT /evidence="ECO:0007829|PDB:5HKO"
FT TURN 304..306
FT /evidence="ECO:0007829|PDB:5HKO"
FT HELIX 307..314
FT /evidence="ECO:0007829|PDB:5HKO"
FT HELIX 318..335
FT /evidence="ECO:0007829|PDB:5HKO"
SQ SEQUENCE 349 AA; 36081 MW; 55E8B6B503898246 CRC64;
MNITSKIGAI AAAGAVGLGL TACGAGDTAA NSDTKRIGVT VYDMSSFITE GKEGMDTYAK
ANNIELVWNS ANNDVSTQAS QVDSLINQGV DAIIVVPVQA DSLGPQVASA KSKGIPLLAV
NAALETPDLA GNVQPDDVAA GAQEMQMMAD RLGGKGNIVI LQGPLGGSGE INRGKGIDQV
LAKYPDIKVL AKDTANWKRD EAVNKMKNWI SSFGPQIDGV VAQNDDMGLG ALQALKEAGR
TGVPIVGIDG IEDGLNAVKS GDFIGTSLQN GTVELSAGLA VADALVKGED VKTDPVYVMP
AITKDNVDVA IEHVVTERQK FLDGLVELTQ QNLKTGDIAY EGIPGQTQP
