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Database: UniProt
Entry: A0A0N0IB42_9GAMM
LinkDB: A0A0N0IB42_9GAMM
Original site: A0A0N0IB42_9GAMM 
ID   A0A0N0IB42_9GAMM        Unreviewed;       434 AA.
AC   A0A0N0IB42;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   SubName: Full=PTS system DHA-specific IIA component {ECO:0000313|EMBL:KPD03573.1};
DE            EC=2.7.-.- {ECO:0000313|EMBL:KPD03573.1};
DE            EC=2.7.1.121 {ECO:0000313|EMBL:KPD03573.1};
DE            EC=2.7.3.9 {ECO:0000313|EMBL:KPD03573.1};
GN   ORFNames=M992_1166 {ECO:0000313|EMBL:KPD03573.1};
OS   Moellerella wisconsensis ATCC 35017.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Moellerella.
OX   NCBI_TaxID=1354267 {ECO:0000313|EMBL:KPD03573.1, ECO:0000313|Proteomes:UP000053226};
RN   [1] {ECO:0000313|EMBL:KPD03573.1, ECO:0000313|Proteomes:UP000053226}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35017 {ECO:0000313|EMBL:KPD03573.1,
RC   ECO:0000313|Proteomes:UP000053226};
RA   Plunkett G.III., Neeno-Eckwall E.C., Glasner J.D., Perna N.T.;
RT   "ATOL: Assembling a taxonomically balanced genome-scale reconstruction of
RT   the evolutionary history of the Enterobacteriaceae.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007837}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KPD03573.1}.
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DR   EMBL; LGAA01000010; KPD03573.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N0IB42; -.
DR   Proteomes; UP000053226; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0047324; F:phosphoenolpyruvate-glycerone phosphotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008965; F:phosphoenolpyruvate-protein phosphotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:InterPro.
DR   CDD; cd00367; PTS-HPr_like; 1.
DR   Gene3D; 3.30.1340.10; HPr-like; 1.
DR   Gene3D; 3.50.30.10; Phosphohistidine domain; 1.
DR   Gene3D; 3.40.50.510; Phosphotransferase system, mannose-type IIA component; 1.
DR   Gene3D; 1.10.274.10; PtsI, HPr-binding domain; 1.
DR   InterPro; IPR000032; HPr-like.
DR   InterPro; IPR035895; HPr-like_sf.
DR   InterPro; IPR008279; PEP-util_enz_mobile_dom.
DR   InterPro; IPR036637; Phosphohistidine_dom_sf.
DR   InterPro; IPR004701; PTS_EIIA_man-typ.
DR   InterPro; IPR036662; PTS_EIIA_man-typ_sf.
DR   InterPro; IPR008731; PTS_EIN.
DR   InterPro; IPR001020; PTS_HPr_His_P_site.
DR   InterPro; IPR036618; PtsI_HPr-bd_sf.
DR   NCBIfam; TIGR01003; PTS_HPr_family; 1.
DR   PANTHER; PTHR46244; PHOSPHOENOLPYRUVATE-PROTEIN PHOSPHOTRANSFERASE; 1.
DR   PANTHER; PTHR46244:SF3; PHOSPHOENOLPYRUVATE-PROTEIN PHOSPHOTRANSFERASE; 1.
DR   Pfam; PF03610; EIIA-man; 1.
DR   Pfam; PF05524; PEP-utilisers_N; 1.
DR   Pfam; PF00391; PEP-utilizers; 1.
DR   Pfam; PF00381; PTS-HPr; 1.
DR   PRINTS; PR00107; PHOSPHOCPHPR.
DR   SUPFAM; SSF47831; Enzyme I of the PEP:sugar phosphotransferase system HPr-binding (sub)domain; 1.
DR   SUPFAM; SSF55594; HPr-like; 1.
DR   SUPFAM; SSF52009; Phosphohistidine domain; 1.
DR   SUPFAM; SSF53062; PTS system fructose IIA component-like; 1.
DR   PROSITE; PS51096; PTS_EIIA_TYPE_4; 1.
DR   PROSITE; PS51350; PTS_HPR_DOM; 1.
DR   PROSITE; PS00369; PTS_HPR_HIS; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000053226};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KPD03573.1}.
FT   DOMAIN          1..90
FT                   /note="PTS EIIA type-4"
FT                   /evidence="ECO:0000259|PROSITE:PS51096"
FT   DOMAIN          112..199
FT                   /note="HPr"
FT                   /evidence="ECO:0000259|PROSITE:PS51350"
SQ   SEQUENCE   434 AA;  47416 MW;  C69C2BFB15762E14 CRC64;
     MEAIEALSDA NAIILLMDLG SAVLSAQTAV ELLSTDLAAK TYFCAAPIVE GAIAITVAAS
     SKINISIDTL LSDAENSLIA KQAQLGDLTI HSNIAPLCVD NINTQNIDIK NSVNYLWVVR
     NINGLHARPA AKIAAVLTPF DAQLILEKGS QQVNPKNMNQ IALLQIRQGD QINLIASGNQ
     SEEAINAFKI LAANNFGESL DNSTTLFYGQ KAIEPIVSGL SFQWTRSKPS SISTIVDQQS
     KLAKQQLTTA LTRVSHNLNL IAQHAKKMYG TSIAEIFHGH IALLSDEEII QQLNQYIEQH
     QANAYTAIDK VFADISAQYR QINDNYLQAR YLDIDDLRRQ LLLSLTGQKT QFPPFEHPTL
     LISDTLYPSE IIQLACSNII GIALSDSSPY AHTAIIAQKM GIPILVNLGD KILSIQNNRQ
     LIINLQKLSL SIRS
//
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