ULAC_MYCPN
ID ULAC_MYCPN Reviewed; 159 AA.
AC P75292;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Ascorbate-specific PTS system EIIA component {ECO:0000250|UniProtKB:P69820};
DE AltName: Full=Ascorbate-specific phosphotransferase enzyme IIA component {ECO:0000250|UniProtKB:P69820};
GN Name=ulaC; Synonyms=sgaA; OrderedLocusNames=MPN_494; ORFNames=MP348;
OS Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS pneumoniae).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=272634;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29342 / M129;
RX PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT pneumoniae.";
RL Nucleic Acids Res. 24:4420-4449(1996).
CC -!- FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase
CC system (sugar PTS), a major carbohydrate active transport system,
CC catalyzes the phosphorylation of incoming sugar substrates
CC concomitantly with their translocation across the cell membrane. The
CC enzyme II UlaABC PTS system is involved in ascorbate transport.
CC {ECO:0000250|UniProtKB:P69820}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- DOMAIN: The PTS EIIA type-2 domain is phosphorylated by phospho-HPr on
CC a histidyl residue. Then, it transfers the phosphoryl group to the PTS
CC EIIB type-2 domain. {ECO:0000255|PROSITE-ProRule:PRU00417}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U00089; AAB95996.1; -; Genomic_DNA.
DR PIR; S73674; S73674.
DR RefSeq; NP_110182.1; NC_000912.1.
DR RefSeq; WP_010874850.1; NC_000912.1.
DR AlphaFoldDB; P75292; -.
DR SMR; P75292; -.
DR STRING; 272634.MPN_494; -.
DR EnsemblBacteria; AAB95996; AAB95996; MPN_494.
DR GeneID; 66608834; -.
DR KEGG; mpn:MPN_494; -.
DR PATRIC; fig|272634.6.peg.534; -.
DR HOGENOM; CLU_072531_2_0_14; -.
DR OMA; MGPYIIL; -.
DR BioCyc; MPNE272634:G1GJ3-811-MON; -.
DR Proteomes; UP000000808; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00211; PTS_IIA_fru; 1.
DR Gene3D; 3.40.930.10; -; 1.
DR InterPro; IPR016152; PTrfase/Anion_transptr.
DR InterPro; IPR002178; PTS_EIIA_type-2_dom.
DR Pfam; PF00359; PTS_EIIA_2; 1.
DR SUPFAM; SSF55804; SSF55804; 1.
DR PROSITE; PS51094; PTS_EIIA_TYPE_2; 1.
DR PROSITE; PS00372; PTS_EIIA_TYPE_2_HIS; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Kinase; Phosphoprotein; Phosphotransferase system;
KW Reference proteome; Transferase; Transport.
FT CHAIN 1..159
FT /note="Ascorbate-specific PTS system EIIA component"
FT /id="PRO_0000186685"
FT DOMAIN 9..152
FT /note="PTS EIIA type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00417"
FT ACT_SITE 71
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00417"
FT MOD_RES 71
FT /note="Phosphohistidine"
FT /evidence="ECO:0000250|UniProtKB:P69820"
SQ SEQUENCE 159 AA; 17808 MW; 85FEEAC315E735B6 CRC64;
MTKLDFKAVL KQHHTVRLHQ TAQDWKQAIQ LCIHPLIAAK LVQPAYFDDI LKSVAQYGPY
FIIAENVAMP HAQNNGTVQQ NCFSLVTLKE PVYFDNDPRP VRLLIGLAAT SAAIHTTEAL
PQIAALVEDT QVVKDLLDCC DETSLFAVID RVNLHKYLT
