ID   THIX_CORGL              Reviewed;         190 AA.
AC   P42461;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2002, sequence version 2.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Thiamine biosynthesis protein X;
DE   Flags: Precursor;
GN   Name=thiX; OrderedLocusNames=Cgl2332, cg2561;
OS   Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS   JCM 1318 / LMG 3730 / NCIMB 10025).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=196627;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA   Ikeda M., Nakagawa S.;
RT   "The Corynebacterium glutamicum genome: features and impacts on
RT   biotechnological processes.";
RL   Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA   Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA   Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA   Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA   Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA   Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT   "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT   impact on the production of L-aspartate-derived amino acids and vitamins.";
RL   J. Biotechnol. 104:5-25(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-133.
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=8206824; DOI=10.1128/jb.176.12.3474-3483.1994;
RA   Reinscheid D.J., Eikmanns B.J., Sahm H.;
RT   "Characterization of the isocitrate lyase gene from Corynebacterium
RT   glutamicum and biochemical analysis of the enzyme.";
RL   J. Bacteriol. 176:3474-3483(1994).
CC   -!- FUNCTION: Is necessary for biosynthesis of the 4-methyl-5-(beta-
CC       hydroxyethyl)thiazol component from which thiamine is formed.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC       ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
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DR   EMBL; BA000036; BAB99725.1; -; Genomic_DNA.
DR   EMBL; BX927154; CAF20675.1; -; Genomic_DNA.
DR   EMBL; X75504; CAA53220.1; -; Genomic_DNA.
DR   PIR; I40714; I40714.
DR   RefSeq; NP_601532.1; NC_003450.3.
DR   RefSeq; WP_011015045.1; NC_006958.1.
DR   AlphaFoldDB; P42461; -.
DR   SMR; P42461; -.
DR   KEGG; cgb:cg2561; -.
DR   KEGG; cgl:Cgl2332; -.
DR   PATRIC; fig|196627.13.peg.2265; -.
DR   eggNOG; ENOG5031J0M; Bacteria.
DR   HOGENOM; CLU_121345_0_0_11; -.
DR   OMA; KIFGDHT; -.
DR   Proteomes; UP000000582; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR027273; Neocarzinostatin-like.
DR   SUPFAM; SSF49319; SSF49319; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Lipoprotein; Membrane; Palmitate; Reference proteome;
KW   Signal; Thiamine biosynthesis.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           23..190
FT                   /note="Thiamine biosynthesis protein X"
FT                   /id="PRO_0000022491"
FT   REGION          43..68
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        43..65
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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"
SQ   SEQUENCE   190 AA;  19251 MW;  97314A02BB10EFDB CRC64;
     MSISRTVFGI AATAALSAAL VACSPPHQQD SPVQRTNEIL TTSQNPTSAS STSTSSATTT
     SSAPVEEDVE IVVSPAALVD GEQVTFEISG LDPEGGYYAA ICDSVANPGN PVPSCTGEMA
     DFTSQAWLSN SQPGATVEIA EDGTATVELE ATATGTGLDC TTQACVAKVF GDHTEGFRDV
     AEVPVTFAAA