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Database: UniProt
Entry: N8TUQ5_ACILW
LinkDB: N8TUQ5_ACILW
Original site: N8TUQ5_ACILW 
ID   N8TUQ5_ACILW            Unreviewed;       765 AA.
AC   N8TUQ5;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 54.
DE   RecName: Full=phosphoenolpyruvate--protein phosphotransferase {ECO:0000256|ARBA:ARBA00012232};
DE            EC=2.7.3.9 {ECO:0000256|ARBA:ARBA00012232};
GN   ORFNames=F980_00567 {ECO:0000313|EMBL:ENU63658.1};
OS   Acinetobacter lwoffii NIPH 715.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=1217669 {ECO:0000313|EMBL:ENU63658.1, ECO:0000313|Proteomes:UP000018422};
RN   [1] {ECO:0000313|EMBL:ENU63658.1, ECO:0000313|Proteomes:UP000018422}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIPH 715 {ECO:0000313|EMBL:ENU63658.1,
RC   ECO:0000313|Proteomes:UP000018422};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA   Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA   Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA   Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA   Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA   Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Acinetobacter lwoffii NIPH 715.";
RL   Submitted (FEB-2013) 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}.
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:ENU63658.1}.
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DR   EMBL; APOT01000028; ENU63658.1; -; Genomic_DNA.
DR   RefSeq; WP_004729445.1; NZ_KB849264.1.
DR   AlphaFoldDB; N8TUQ5; -.
DR   PATRIC; fig|1217669.3.peg.534; -.
DR   HOGENOM; CLU_007308_7_1_6; -.
DR   Proteomes; UP000018422; Unassembled WGS sequence.
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; 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.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Phosphotransferase system {ECO:0000256|ARBA:ARBA00022683};
KW   Pyruvate {ECO:0000313|EMBL:ENU63658.1};
KW   Sugar transport {ECO:0000256|ARBA:ARBA00022597};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ENU63658.1};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          21..168
FT                   /note="GAF"
FT                   /evidence="ECO:0000259|SMART:SM00065"
FT   COILED          213..247
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   765 AA;  85476 MW;  D6FD359C10429A4D CRC64;
     MSNMQLDTLR RIVQEINAST SLHESLDIMV KHVAEAMQVD VCSIYLLDER NQRYLLMASK
     GLNAESVGHV SLQTGEGLVG LVGQREEIVN LDNAPKHERF LFLPETGEEI YNSFLGVPVM
     YRRKVMGVLV VQNKESQDFS EAAESFLVTL CAQLSGVIAH AHAVGNIDVF RKPSNLPAYK
     TFQGVSGSGG IALGRAVILY PPADLAAVPD READDISEEL ELLDNALNSV REEIQSLDDK
     MQDALMAEER ALFSVFLRML DENALPAEIK AFIREGHWAQ GAVRIVIDNH VAQFSQMEDD
     YLRERVADLK DLGRRILARL QEADASHREL TDESILIGEE ISTAALVELP VDKIAAIVTT
     EGAMNSHMVI VARALGIPTV VGVTELPINT LDDVEMIVDA HQGRVFINPP RRLRSRYKEI
     QKEEEQIAKD LRQYETKDAI TPDGVAVKLY VNTGLMIDVV RGVQRGAKGV GLYRSEIPFM
     LRDRFPGEEE QRAIYRQQLS HFANKPVVMR TLDIGADKDL PYFSIEEENS ALGWRGIRFT
     LDHPEIFSSQ IRAMLKASIG LNNLHILLPM VTSVSEVEEA LYLLERDHAA IQEEEQVKVN
     KPKLGIMVEV PSVLHQIDEF SELVDFFSVG SNDLTQYLLA VDRNNPRVAN VYSHLHPAVL
     RALTRLVQDC HRNEKPVSIC GEMAGDPLSA VLLMAMGFNT LSMSSSNILR VRKTICHVPM
     SDAQELLAHV LKMDNPLMVK SWLEYYFRTH GLGDMVKSAS RMVSA
//
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