ID   Y129_MYCGE              Reviewed;         117 AA.
AC   Q49397;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Putative phosphotransferase enzyme IIB component MG129;
DE            EC=2.7.1.-;
DE   AltName: Full=Putative PTS system EIIB component;
GN   OrderedLocusNames=MG129;
OS   Mycoplasma genitalium (strain ATCC 33530 / DSM 19775 / NCTC 10195 / G37)
OS   (Mycoplasmoides genitalium).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=243273;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX   PubMed=7569993; DOI=10.1126/science.270.5235.397;
RA   Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A.,
RA   Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M.,
RA   Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L.,
RA   Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M.,
RA   Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S.,
RA   Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.;
RT   "The minimal gene complement of Mycoplasma genitalium.";
RL   Science 270:397-403(1995).
CC   -!- FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase
CC       system (PTS), a major carbohydrate active -transport system, catalyzes
CC       the phosphorylation of incoming sugar substrates concomitant with their
CC       translocation across the cell membrane. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- DOMAIN: The EIIB domain is phosphorylated by phospho-EIIA on a
CC       cysteinyl or histidyl residue, depending on the transported sugar.
CC       Then, it transfers the phosphoryl group to the sugar substrate
CC       concomitantly with the sugar uptake processed by the EIIC domain.
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DR   EMBL; L43967; AAC71347.1; -; Genomic_DNA.
DR   PIR; C64214; C64214.
DR   RefSeq; WP_009885683.1; NZ_AAGX01000002.1.
DR   AlphaFoldDB; Q49397; -.
DR   SMR; Q49397; -.
DR   STRING; 243273.MG_129; -.
DR   EnsemblBacteria; AAC71347; AAC71347; MG_129.
DR   KEGG; mge:MG_129; -.
DR   eggNOG; COG1264; Bacteria.
DR   HOGENOM; CLU_2082212_0_0_14; -.
DR   OMA; WLYWRIK; -.
DR   OrthoDB; 2058018at2; -.
DR   BioCyc; MGEN243273:G1GJ2-142-MON; -.
DR   Proteomes; UP000000807; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008982; F:protein-N(PI)-phosphohistidine-sugar phosphotransferase activity; IEA:InterPro.
DR   GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.1360.60; -; 1.
DR   InterPro; IPR036878; Glu_permease_IIB.
DR   InterPro; IPR001996; PTS_IIB_1.
DR   SUPFAM; SSF55604; SSF55604; 1.
DR   PROSITE; PS51098; PTS_EIIB_TYPE_1; 1.
PE   3: Inferred from homology;
KW   Membrane; Phosphoprotein; Phosphotransferase system; Reference proteome;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..117
FT                   /note="Putative phosphotransferase enzyme IIB component
FT                   MG129"
FT                   /id="PRO_0000210429"
FT   TRANSMEM        1..21
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          42..117
FT                   /note="PTS EIIB type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00421"
SQ   SEQUENCE   117 AA;  13457 MW;  7C1874801EB31ABF CRC64;
     MKWLLWLGYI FSFGLLYLWI VKKSKQIAQQ PNTKLVESTS IPFKVKDFVS ACGGKENFVN
     IKTTPTQLIV TFKDVNSVSL TKLNALNIKG INKNQNQFRF VLGNFVNELK KKIEDEQ