PTMA_MYCPN
ID PTMA_MYCPN Reviewed; 143 AA.
AC P75145;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Mannitol-specific phosphotransferase enzyme IIA component {ECO:0000250|UniProtKB:P0A0E0};
DE AltName: Full=EIIA {ECO:0000250|UniProtKB:P0A0E0};
DE AltName: Full=EIII {ECO:0000250|UniProtKB:P0A0E0};
DE AltName: Full=PTS system mannitol-specific EIIA component {ECO:0000250|UniProtKB:P0A0E0};
GN Name=mtlF; OrderedLocusNames=MPN_653; ORFNames=MP189;
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 CmtAB PTS system is involved in D-mannitol transport.
CC {ECO:0000250|UniProtKB:P0A0E0}.
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}.
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DR EMBL; U00089; AAB95837.1; -; Genomic_DNA.
DR PIR; S73515; S73515.
DR RefSeq; NP_110342.1; NC_000912.1.
DR RefSeq; WP_010875010.1; NC_000912.1.
DR AlphaFoldDB; P75145; -.
DR SMR; P75145; -.
DR IntAct; P75145; 1.
DR STRING; 272634.MPN_653; -.
DR EnsemblBacteria; AAB95837; AAB95837; MPN_653.
DR GeneID; 66608660; -.
DR KEGG; mpn:MPN_653; -.
DR PATRIC; fig|272634.6.peg.717; -.
DR HOGENOM; CLU_072531_3_1_14; -.
DR OMA; EDYIQAM; -.
DR BioCyc; MPNE272634:G1GJ3-1043-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 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.
PE 3: Inferred from homology;
KW Cytoplasm; Kinase; Phosphoprotein; Phosphotransferase system;
KW Reference proteome; Sugar transport; Transferase; Transport.
FT CHAIN 1..143
FT /note="Mannitol-specific phosphotransferase enzyme IIA
FT component"
FT /id="PRO_0000186635"
FT DOMAIN 1..142
FT /note="PTS EIIA type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00417"
FT ACT_SITE 61
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P0A0E0,
FT ECO:0000255|PROSITE-ProRule:PRU00417"
FT MOD_RES 61
FT /note="Phosphohistidine; by HPr"
FT /evidence="ECO:0000250|UniProtKB:P00550,
FT ECO:0000250|UniProtKB:P0A0E0"
SQ SEQUENCE 143 AA; 16313 MW; AA672A4051E5E8CA CRC64;
MKLLKNNIYI NVYLKNKQEI FEFVFKKFKE DGAVLDSFLP AIVERDKAAS VAIGNYLFLP
HPVYDEIANI QKEKMVFIGL KDVINIDGQP IKFICGLALK GEHQMDALQS LAIAFSDPEE
VEKLVKDKDL TQDKVLEFLA KHN
