ULAB_MYCPN
ID ULAB_MYCPN Reviewed; 95 AA.
AC Q9EXD8;
DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Ascorbate-specific PTS system EIIB component {ECO:0000250|UniProtKB:P69822};
DE EC=2.7.1.194 {ECO:0000250|UniProtKB:P69822};
DE AltName: Full=Ascorbate-specific phosphotransferase enzyme IIB component {ECO:0000250|UniProtKB:P69822};
GN Name=ulaB; Synonyms=sgaB; OrderedLocusNames=MPN_495; ORFNames=MP347.1;
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).
RN [2]
RP IDENTIFICATION.
RC STRAIN=ATCC 29342 / M129;
RX PubMed=10954595; DOI=10.1093/nar/28.17.3278;
RA Dandekar T., Huynen M., Regula J.T., Ueberle B., Zimmermann C.U.,
RA Andrade M.A., Doerks T., Sanchez-Pulido L., Snel B., Suyama M., Yuan Y.P.,
RA Herrmann R., Bork P.;
RT "Re-annotating the Mycoplasma pneumoniae genome sequence: adding value,
RT function and reading frames.";
RL Nucleic Acids Res. 28:3278-3288(2000).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=ATCC 29342 / M129;
RX PubMed=11271496;
RX DOI=10.1002/1522-2683(200011)21:17<3765::aid-elps3765>3.0.co;2-6;
RA Regula J.T., Ueberle B., Boguth G., Goerg A., Schnoelzer M., Herrmann R.,
RA Frank R.;
RT "Towards a two-dimensional proteome map of Mycoplasma pneumoniae.";
RL Electrophoresis 21:3765-3780(2000).
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:P69822}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-ascorbate(out) + N(pros)-phospho-L-histidyl-[protein] = L-
CC ascorbate 6-phosphate(in) + L-histidyl-[protein];
CC Xref=Rhea:RHEA:42436, Rhea:RHEA-COMP:9745, Rhea:RHEA-COMP:9746,
CC ChEBI:CHEBI:29979, ChEBI:CHEBI:38290, ChEBI:CHEBI:61698,
CC ChEBI:CHEBI:64837; EC=2.7.1.194;
CC Evidence={ECO:0000250|UniProtKB:P69822};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- DOMAIN: The PTS EIIB type-2 domain is phosphorylated by phospho-EIIA on
CC a cysteinyl residue. Then, it transfers the phosphoryl group to the
CC sugar substrate concomitantly with the sugar uptake processed by the
CC PTS EIIC type-2 domain. {ECO:0000255|PROSITE-ProRule:PRU00422}.
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; AAG34743.1; -; Genomic_DNA.
DR RefSeq; NP_110183.1; NC_000912.1.
DR RefSeq; WP_010874851.1; NC_000912.1.
DR AlphaFoldDB; Q9EXD8; -.
DR SMR; Q9EXD8; -.
DR STRING; 272634.MPN_495; -.
DR EnsemblBacteria; AAG34743; AAG34743; MPN_495.
DR KEGG; mpn:MPN_495; -.
DR PATRIC; fig|272634.6.peg.535; -.
DR HOGENOM; CLU_159248_1_0_14; -.
DR OMA; QSKGMTN; -.
DR BioCyc; MPNE272634:G1GJ3-812-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: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 GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR InterPro; IPR036095; PTS_EIIB-like_sf.
DR InterPro; IPR013011; PTS_EIIB_2.
DR InterPro; IPR003501; PTS_EIIB_2/3.
DR Pfam; PF02302; PTS_IIB; 1.
DR SUPFAM; SSF52794; SSF52794; 1.
DR PROSITE; PS51099; PTS_EIIB_TYPE_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Kinase; Phosphoprotein; Phosphotransferase system;
KW Reference proteome; Transferase; Transport.
FT CHAIN 1..95
FT /note="Ascorbate-specific PTS system EIIB component"
FT /id="PRO_0000186688"
FT DOMAIN 1..95
FT /note="PTS EIIB type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00422"
FT ACT_SITE 12
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P00550, ECO:0000305"
FT MOD_RES 12
FT /note="Phosphocysteine"
FT /evidence="ECO:0000250|UniProtKB:P00550, ECO:0000305"
SQ SEQUENCE 95 AA; 10327 MW; 486BF2F3E2E4AEA9 CRC64;
MENKNLHIIA ACGNGMGTSM LIKIKVEKIM KELGYTAKVE ALSMGQTKGM EHSADIIISS
IHLTSEFNPN AKAKIVGVLN LMDENEIKQA LSKVL