ID Q2NRH1_SODGM Unreviewed; 748 AA.
AC Q2NRH1;
DT 07-FEB-2006, integrated into UniProtKB/TrEMBL.
DT 07-FEB-2006, sequence version 1.
DT 27-MAR-2024, entry version 121.
DE RecName: Full=phosphoenolpyruvate--protein phosphotransferase {ECO:0000256|ARBA:ARBA00012232};
DE EC=2.7.3.9 {ECO:0000256|ARBA:ARBA00012232};
GN Name=ptsI_2 {ECO:0000313|EMBL:CRL46254.1};
GN OrderedLocusNames=SG1979 {ECO:0000313|EMBL:BAE75254.1};
GN ORFNames=SGGMMB4_04711 {ECO:0000313|EMBL:CRL46254.1};
OS Sodalis glossinidius (strain morsitans).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Bruguierivoracaceae; Sodalis.
OX NCBI_TaxID=343509 {ECO:0000313|EMBL:BAE75254.1, ECO:0000313|Proteomes:UP000001932};
RN [1] {ECO:0000313|EMBL:BAE75254.1, ECO:0000313|Proteomes:UP000001932}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=morsitans {ECO:0000313|Proteomes:UP000001932}, and Morsitans
RC {ECO:0000313|EMBL:BAE75254.1};
RX PubMed=16365377; DOI=10.1101/gr.4106106;
RA Toh H., Weiss B.L., Perkin S.A.H., Yamashita A., Oshima K., Hattori M.,
RA Aksoy S.;
RT "Massive genome erosion and functional adaptations provide insights into
RT the symbiotic lifestyle of Sodalis glossinidius in the tsetse host.";
RL Genome Res. 16:149-156(2006).
RN [2] {ECO:0000313|EMBL:CRL46254.1, ECO:0000313|Proteomes:UP000245838}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B4 {ECO:0000313|EMBL:CRL46254.1}, and morsitans
RC {ECO:0000313|Proteomes:UP000245838};
RA Goodhead I.;
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-histidyl-[protein] + phosphoenolpyruvate = N(pros)-phospho-
CC L-histidyl-[protein] + pyruvate; Xref=Rhea:RHEA:23880, Rhea:RHEA-
CC COMP:9745, Rhea:RHEA-COMP:9746, ChEBI:CHEBI:15361, ChEBI:CHEBI:29979,
CC ChEBI:CHEBI:58702, ChEBI:CHEBI:64837; EC=2.7.3.9;
CC Evidence={ECO:0000256|ARBA:ARBA00000683};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family.
CC {ECO:0000256|ARBA:ARBA00007837}.
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DR EMBL; AP008232; BAE75254.1; -; Genomic_DNA.
DR EMBL; LN854557; CRL46254.1; -; Genomic_DNA.
DR RefSeq; WP_011411709.1; NZ_LN854557.1.
DR STRING; 343509.SG1979; -.
DR KEGG; sgl:SG1979; -.
DR eggNOG; COG3605; Bacteria.
DR HOGENOM; CLU_007308_7_1_6; -.
DR OrthoDB; 9765468at2; -.
DR BioCyc; SGLO343509:SGP1_RS18165-MONOMER; -.
DR Proteomes; UP000001932; Chromosome.
DR Proteomes; UP000245838; Chromosome sggmmb4_Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008965; F:phosphoenolpyruvate-protein phosphotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:InterPro.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR Gene3D; 3.50.30.10; Phosphohistidine domain; 1.
DR Gene3D; 1.10.274.10; PtsI, HPr-binding domain; 1.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR008279; PEP-util_enz_mobile_dom.
DR InterPro; IPR018274; PEP_util_AS.
DR InterPro; IPR000121; PEP_util_C.
DR InterPro; IPR023151; PEP_util_CS.
DR InterPro; IPR036637; Phosphohistidine_dom_sf.
DR InterPro; IPR006318; PTS_EI-like.
DR InterPro; IPR008731; PTS_EIN.
DR InterPro; IPR036618; PtsI_HPr-bd_sf.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR NCBIfam; TIGR01417; PTS_I_fam; 1.
DR PANTHER; PTHR46244:SF1; PHOSPHOENOLPYRUVATE-DEPENDENT PHOSPHOTRANSFERASE SYSTEM; 1.
DR PANTHER; PTHR46244; PHOSPHOENOLPYRUVATE-PROTEIN PHOSPHOTRANSFERASE; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF05524; PEP-utilisers_N; 1.
DR Pfam; PF00391; PEP-utilizers; 1.
DR Pfam; PF02896; PEP-utilizers_C; 1.
DR PRINTS; PR01736; PHPHTRNFRASE.
DR SMART; SM00065; GAF; 1.
DR SUPFAM; SSF47831; Enzyme I of the PEP:sugar phosphotransferase system HPr-binding (sub)domain; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR SUPFAM; SSF52009; Phosphohistidine domain; 1.
DR PROSITE; PS00742; PEP_ENZYMES_2; 1.
DR PROSITE; PS00370; PEP_ENZYMES_PHOS_SITE; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphotransferase system {ECO:0000256|ARBA:ARBA00022683};
KW Pyruvate {ECO:0000313|EMBL:CRL46254.1};
KW Sugar transport {ECO:0000256|ARBA:ARBA00022597};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CRL46254.1};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 17..164
FT /note="GAF"
FT /evidence="ECO:0000259|SMART:SM00065"
SQ SEQUENCE 748 AA; 82981 MW; 01B00EABDEA02CC0 CRC64;
MLTRLREIVE KVAAAPRLSD SLDILVNETC QAMNTEVCSV YLADNDRRCY YLMATRGLFK
PRGRTITLAF DQGIVGLVGR LAEPINLADA HTHPSFKYIP AVKEERFRSF LGVPIIHRRQ
LLGVLVVQQR EHRQFDESEE SFMVTLATQM AGILPQSQLN ALFSQYRQTR IRALAAAPGV
AIAQGWVDSS QPSLDQVYQA SSLDSGHERE RLTLALNESV AEFCRLSKRF TASAQKDSAA
VFDLYSHLLN DARLKRDLFA EIDGGAVAEW AVKLVIERFA EKFALLSDSY LRERAGDLRS
LGQRLLFHLD DSARNVIQWP SRFVLVADEL SASLLAEVPQ DKLVGVVVRD GAANSHAAIL
VRAMGIPTVM GVDIQPLLLN QRLLIVDGYR GELLVDPEPV LVQEYQRLVS EERELTRLAE
DDVEQPAALK SGESIQVMLN AGLSAEHEQR LDNRVDGIGL YRTEIPFMLQ NGFPSEEEQV
AQYQGMLQLF PGKSVTLRTL DVGADKQLPY MPISEENPCL GWRGIRITLD QPEIFLIQVR
AMLRANAATG NLSILLPMIT SVDEIDEARR LIDRAGREVE EVLGYALPKP RIGIMVEVPA
MVFMLPALVS RVDFLSVGTN DLTQYLLAVD RNNTRVAAMY DSLHPAMLQV LQKIISESQR
LGFACSLCGE MAGDPMGALL LAGMGYRSLS MNGRSVARIK YLLRNVALGE AQGLAERVIG
AQNSIEVHHQ VAAFMERRGL GGLIRGGR
//
